|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
562-918 |
1.07e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 562 IRTEQQAALQRLREEAETLQKAERASLEQKSRRA------LEQLREQLEAEERSAqaalraekeaekeaallqlrEQLEG 635
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAellllkLRELEAELEELEAEL--------------------EELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 636 ERKEAVAGLEKKHsAELEQlcssLEAKHQEvissLQKKIEGAQQKEEAQLQESLGWAEQRAHqkvhqvteyEQELSSLLR 715
Cdd:COG1196 254 ELEELEAELAELE-AELEE----LRLELEE----LELELEEAQAEEYELLAELARLEQDIAR---------LEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 716 DKRQEVEREHERKMDKMKEEHwQEMADARERYEAEERKQRadllghltgELERLRRAHERELESMRQEQDQQLEDLRRRH 795
Cdd:COG1196 316 ERLEELEEELAELEEELEELE-EELEELEEELEEAEEELE---------EAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 796 RDHERKLQDLEvELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEAtatHQHLEEAKKEHTHLLETKQQL 875
Cdd:COG1196 386 EELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE---EEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 160420304 876 RRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQ 918
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
548-1077 |
2.71e-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: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRtEQQAALQRLREEAETLQkAERASLEQKsRRALEQLREQLEAEERSAQAALRAekeaekeaalL 627
Cdd:COG1196 234 LRELEAELEELEAELE-ELEAELEELEAELAELE-AELEELRLE-LEELELELEEAQAEEYELLAELAR----------L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 628 QLREQLEGERKEAVAglekkhsAELEQLcssleakhQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVhqvtEYE 707
Cdd:COG1196 301 EQDIARLEERRRELE-------ERLEEL--------EEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 708 QELSSLLRDKRQEVEREHERkmdkmkEEHWQEMADARERyEAEERKQRADLLGHLTGELERLRRAHERELEsmRQEQDQQ 787
Cdd:COG1196 362 EAEEALLEAEAELAEAEEEL------EELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEE--LEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 788 LEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALER---EEATATHQHLEEAKKE 864
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlllLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 865 hTHLLETKQQLRRTIDDLRVRRVELEsQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNASPHPEPGLHIEDLR 944
Cdd:COG1196 513 -ALLLAGLRGLAGAVAVLIGVEAAYE-AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 945 KSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDE 1024
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 160420304 1025 DLPGTEVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEE 1077
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
547-1049 |
3.94e-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: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 547 LRAQVQSRTEAFEnqirtEQQAALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAAL-----RAEKEAE 621
Cdd:COG1196 272 LRLELEELELELE-----EAQAEEYELLAELARLEQDIA--RLEERRRELEERLEELEEELAELEEELeeleeELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 622 KEAALLQLREQLEGERKEAVAGLEKKHSAELEQLcSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLgwAEQRAHQKVH 701
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-EELEELAEELLEALRAAAELAAQLEELEEAEEA--LLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 702 QVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMR 781
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 782 QEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVK--------ARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATA 853
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 854 THQHLEEAKKEHTHLLETKQQLRRtiDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNASPH 933
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 934 PEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRSMRRRQTALKAAQQH-- 1011
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELle 739
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 160420304 1012 --WRHELASAQEVDEDLPGTEVLGNMRKNLNEETRHLDEM 1049
Cdd:COG1196 740 elLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
569-930 |
7.26e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 569 ALQRLREEAETLQKAERA---------SLEQKSRRAlEQLREqLEAEERSAQAALRAEKEAEKEAALLQLREQLegerkE 639
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIlnelerqlkSLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEEL-----K 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 640 AVAGLEKKHSAELEQLCSSLEAKHQEvISSLQKKIEGAQQKEEAQLQEslgwaeqrAHQKVHQVTEYEQELSSLlrdKRQ 719
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANE--------ISRLEQQKQILRERLANL---ERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 720 EVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLghltGELERLRRAHErELESMRQEQDQQLEDLRRRHRDHE 799
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE----AELEELEAELE-ELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 800 RKLQDLEVELSSrtkdVKARLAQLNVQEENIRKEKQLLLDAQRQAALEreeatATHQHLEEAKKEHTHLLETKQQLRRTI 879
Cdd:TIGR02168 393 LQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELK-----ELQAELEELEEELEELQEELERLEEAL 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 160420304 880 DDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNA 930
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
553-923 |
1.68e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 553 SRTEAFENQIRTEQQAALQRLREEAETLqKAERASLEQKSRRaLEQLREQLEAEERSAQAALRAEKEAekeaallqlREQ 632
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGL-KRELSSLQSELRR-IENRLDELSQELSDASRKIGEIEKE---------IEQ 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 633 LEGErkeavaglEKKHSAELEQLcssleakhQEVISSLQKKIEGAQQkEEAQLQESLGWAEQRAHqkvhqvtEYEQELSS 712
Cdd:TIGR02169 728 LEQE--------EEKLKERLEEL--------EEDLSSLEQEIENVKS-ELKELEARIEELEEDLH-------KLEEALND 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 713 LLRDKRQEVEREHERKMDKMKEEH--WQEMADARERyEAEERKQRADLLGHLTGELERLRraheRELESMRQEQDQQLED 790
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVsrIEARLREIEQ-KLNRLTLEKEYLEKEIQELQEQR----IDLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 791 LRRRHRDHERKLQDLEVELssrtKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAkkehthlLE 870
Cdd:TIGR02169 859 LNGKKEELEEELEELEAAL----RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-------LE 927
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160420304 871 TKQQLRRTIDDLRVRRVELESQV---DLLQAQSQRLQKHLSSLE----------AEVQRKQDVLKE 923
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKE 993
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
549-882 |
8.64e-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: 76.63 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 549 AQVQSRTEAFENQIRtEQQAALQRLREEAETLQKAERA--SLEQKSRRALEQLREQLEAEERSAqaalraekeaekeAAL 626
Cdd:TIGR02168 680 EELEEKIEELEEKIA-ELEKALAELRKELEELEEELEQlrKELEELSRQISALRKDLARLEAEV-------------EQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 627 LQLREQLEGERKEAVAGLEKKHsAELEQLCSSLEAkHQEVISSLQKKIEgaQQKEEAQLQESLGWAEQRAHQ----KVHQ 702
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELE-ERLEEAEEELAE-AEAEIEELEAQIE--QLKEELKALREALDELRAELTllneEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 703 VTEYEQELSSLLRDKRQEVEREHERKmdKMKEEHWQEMADARERYEAEERKQRADLLGHLtgeleRLRRAHERELESMRQ 782
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 783 EqdqqLEDLRRRHRDHERKLQDLEVELSSRTK---DVKARLAQLNVQEENIR--------------KEKQLLLDAQRQAA 845
Cdd:TIGR02168 895 E----LEELSEELRELESKRSELRRELEELREklaQLELRLEGLEVRIDNLQerlseeysltleeaEALENKIEDDEEEA 970
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 160420304 846 LER-------------------EEATATHQHLEEAKKEHTHLLETKQQLRRTIDDL 882
Cdd:TIGR02168 971 RRRlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
548-1091 |
1.84e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTEQQAALQRLRE--EAETLQKAERASLEQKSRRALEQLREQL--EAEE-RSAQAALRAEKEAEK 622
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIarKAEDaRKAEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 623 EAAllqlREQLEGERKEAVAGLEKKHSAEleqlcsslEAKHQEVIsslqKKIEGAQQKEEAQLQESLGWAEQrAHQKVHQ 702
Cdd:PTZ00121 1179 EAA----RKAEEVRKAEELRKAEDARKAE--------AARKAEEE----RKAEEARKAEDAKKAEAVKKAEE-AKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 703 VTEYEQELSSLLRDKRQEVEREH-ERKMDKMKEEhwqEMADARERYEAEERKQRadllghltgelERLRRAHE-RELESM 780
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHfARRQAAIKAE---EARKADELKKAEEKKKA-----------DEAKKAEEkKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 781 RQ--EQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHL 858
Cdd:PTZ00121 1308 KKkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 859 EEAKKEHtHLLETKQQLRRTIDDLRvRRVELESQVDLLQAQSQRLQK-HLSSLEAEVQRKQDVLKEMAAEmnASPHPEPG 937
Cdd:PTZ00121 1388 EEKKKAD-EAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKaDEAKKKAEEAKKADEAKKKAEE--AKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 938 LHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGvAVRNAKEflVRQTRSMRRRQTALKAAQQHWRHELA 1017
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE-AKKKADE--AKKAEEAKKADEAKKAEEAKKADEAK 1540
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160420304 1018 SAQEV---DEDLPGTEVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEEvsdEDTLKGSSIKK 1091
Cdd:PTZ00121 1541 KAEEKkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE---EKKMKAEEAKK 1614
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-1077 |
4.61e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 531 EEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEQQAALQRLREEA---ETLQKAERASLEQKSRRALEQLR--EQLEA 605
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArkaEEARKAEDAKKAEAARKAEEVRKaeELRKA 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 606 EE-RSAQAALRAEKEAEKEaallQLREQLEGERKEAVAGLEKKHSAELEQLCSSLEAKHQEVisslqKKIEGAQQKEEAQ 684
Cdd:PTZ00121 1197 EDaRKAEAARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI-----RKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 685 LQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQEVER-----EHERKMD--KMKEEHWQEMADARERyEAEERKQRAD 757
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEakkkaEEAKKADeaKKKAEEAKKKADAAKK-KAEEAKKAAE 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 758 L-------------LGHLTGELERLRRAHER---ELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTK--DVKAR 819
Cdd:PTZ00121 1347 AakaeaeaaadeaeAAEEKAEAAEKKKEEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKK 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 820 LAQLNVQEENIRK-EKQLLLDAQRQAALEREEATATHQHLEEAKKEHThlLETKQQLRRTIDDLRVRRVELESQVDLLQA 898
Cdd:PTZ00121 1427 AEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 899 QSQRLQKHLSSLEAEVQRKQDVLK--EMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRqf 976
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKkaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-- 1582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 977 lsAEgvAVRNAKEFLVRQTRSMRRRQTALKAAQ-QHWRHELASAQEVDEDLPGTEVLGNMRKNLNEETRHLDEMKSAMR- 1054
Cdd:PTZ00121 1583 --AE--EAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEe 1658
|
570 580
....*....|....*....|....*.
gi 160420304 1055 ---KGHDLLKKKEEKLIQLESSLQEE 1077
Cdd:PTZ00121 1659 nkiKAAEEAKKAEEDKKKAEEAKKAE 1684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-1080 |
5.57e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQkAERASLEQKsRRALEQLREQLEAEERSAQAALRAEKEAEKEAaLLQLREQLEGERKEAvagl 644
Cdd:COG4913 285 FAQRRLELLEAELEELR-AELARLEAE-LERLEARLDALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEER---- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 645 eKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQ------KEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDK- 717
Cdd:COG4913 358 -ERRRARLEALLAALGLPLPASAEEFAALRAEAAAllealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKs 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 718 ---------RQEVERE---HERKMD--------KMKEEHWQE-------------------MADARERYEAEERKQRADL 758
Cdd:COG4913 437 niparllalRDALAEAlglDEAELPfvgelievRPEEERWRGaiervlggfaltllvppehYAAALRWVNRLHLRGRLVY 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 759 LG-HLTGELERLRRAHEREL----------------ESMRQEQD-------QQLEDLRR-------------RHR----- 796
Cdd:COG4913 517 ERvRTGLPDPERPRLDPDSLagkldfkphpfrawleAELGRRFDyvcvdspEELRRHPRaitragqvkgngtRHEkddrr 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 797 ----------DHERKLQDLEVE---LSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAAlEREEATATHQHLEEAKK 863
Cdd:COG4913 597 rirsryvlgfDNRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEA 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 864 EHTHLLETK---QQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKemAAEMNASPHPEPGLhi 940
Cdd:COG4913 676 ELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALL-- 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 941 EDLRKSLDtnknqevssslslskeeIDLSMESVRQFLSAEgvaVRNAKEFLVRQTRSMRRrqtALKAAQQHWRHELASAQ 1020
Cdd:COG4913 752 EERFAAAL-----------------GDAVERELRENLEER---IDALRARLNRAEEELER---AMRAFNREWPAETADLD 808
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 1021 EVDEDLPGTEvlgNMRKNLNEE--TRHLDEMKSAmrkghdLLKKKEEKLIQLESSLQEEVSD 1080
Cdd:COG4913 809 ADLESLPEYL---ALLDRLEEDglPEYEERFKEL------LNENSIEFVADLLSKLRRAIRE 861
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
539-1091 |
1.24e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 539 EESRRLVCLRAQVQSRTEAFE-NQIRTEQQAALQRLREEAETLQKAER-ASLEQKSRRALEQLReqlEAEERSAQAALRA 616
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEaKKAEEERNNEEIRKFEEARMAHFARRqAAIKAEEARKADELK---KAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 617 EKEAEKEAallQLREQLEGERKeavAGLEKKHSAELEQLCSSLEAKHQEVisslQKKIEGAQQKEEAQLQESLGWAEQRA 696
Cdd:PTZ00121 1298 AEEKKKAD---EAKKKAEEAKK---ADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 697 HQKVHqvTEYEQELSSLLRDKRQEVereheRKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERE 776
Cdd:PTZ00121 1368 AAEKK--KEEAKKKADAAKKKAEEK-----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 777 LESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLA-QLNVQEENIRKEKqlllDAQRQAALEREEATATH 855
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKA----DEAKKAAEAKKKADEAK 1516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 856 QHLEEAKKEHTHLLETKQQL--------RRTIDDLR----VRRVELESQVDllQAQSQRLQKHLSSLEAEVQRKQDvlKE 923
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKAdeakkaeeKKKADELKkaeeLKKAEEKKKAE--EAKKAEEDKNMALRKAEEAKKAE--EA 1592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 924 MAAEMNASPHPEPGLHIEDLRKSLDTN-KNQEVSSSLSLSKEEIDLSMESVRQFLSAEgvAVRNAKEflvrqTRSMRRRQ 1002
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKiKAEELKKAEEEKKKVEQLKKKEAEEKKKAE--ELKKAEE-----ENKIKAAE 1665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 1003 TALKAAQQHWRHELASAQEVDEDLPGTEVlgnmrKNLNEETRHLDEMKSA----MRKGHDLLKKKEEKLIQLESSLQEEv 1078
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEAL-----KKEAEEAKKAEELKKKeaeeKKKAEELKKAEEENKIKAEEAKKEA- 1739
|
570
....*....|...
gi 160420304 1079 sDEDTLKGSSIKK 1091
Cdd:PTZ00121 1740 -EEDKKKAEEAKK 1751
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
519-1048 |
1.52e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 519 QLQKATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRALEQ 598
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 599 LREQLEaEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQlcsSLEAKHQEVIsslqKKIEGAQ 678
Cdd:PTZ00121 1475 AKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---AEEAKKADEA----KKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 679 QKEEAQLQESLGWAEQRahQKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRAdl 758
Cdd:PTZ00121 1547 KADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-- 1622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 759 lghltgelERLRRAherelesmrQEQDQQLEDLRRRHRDHERKLQdlevELSSRTKDVKARLAQLNVQEEnirKEKQLLL 838
Cdd:PTZ00121 1623 --------EELKKA---------EEEKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAE---EDKKKAE 1678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 839 DAQRQAALEREEATATHQHLEEAKKehthlletKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHlsslEAEVQRKQ 918
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKA 1746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 919 DVLKEMAAEMNASPH--PEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSA--EG-----VAVRNAKE 989
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHlkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiiEGgkegnLVINDSKE 1826
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 990 FLVRQTRSMR-RRQTALKAAQQHWRHELASAQEVDEDlpgtevlGNMRKNLNEETRHLDE 1048
Cdd:PTZ00121 1827 MEDSAIKEVAdSKNMQLEEADAFEKHKFNKNNENGED-------GNKEADFNKEKDLKED 1879
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
436-928 |
2.26e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 436 WEAQGLDQEEQDDSKSSIAEPQSKHTQGSEREHLQSSLHSQATEEgpLQTLEGQPEWKEAEgpgkdsvaspapLSLLQSL 515
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL--LEAEAELAEAEEEL------------EELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 516 LKAQLQKATAEEKEKEEETKIREEESRRLVcLRAQVQSRTEAfENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRA 595
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 596 lEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQLCSSL---EAKHQEVI----- 667
Cdd:COG1196 467 -ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigvEAAYEAALeaala 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 668 SSLQKKI----EGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLR---------DKRQEVEREHERKMDKMKE 734
Cdd:COG1196 546 AALQNIVveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdlvasDLREADARYYVLGDTLLGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 735 EHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTK 814
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 815 DVKARLAQLNVQEENIRKEkQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESqVD 894
Cdd:COG1196 706 ERELAEAEEERLEEELEEE-ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGP-VN 783
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 160420304 895 LL-----QAQSQRLQkHLSS----LEAEVQRKQDVLKEMAAEM 928
Cdd:COG1196 784 LLaieeyEELEERYD-FLSEqredLEEARETLEEAIEEIDRET 825
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
443-1076 |
2.56e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 443 QEEQDDSKSSIAEPQSKHTQGSER-EHLQSSLHSQATEegpLQTLEGQPEWKEAEGpgKDSVASPAPLSLLQSLLKAQLQ 521
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEiEELQKELYALANE---ISRLEQQKQILRERL--ANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 522 KATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRA-LEQL- 599
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArLERLe 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 600 --REQLEAEERSAQAALRAEKEAEKEAALLQLREQLEG-----ERKEAVAGLEKKHSAELEQLCSSLEAKHQEVIS---- 668
Cdd:TIGR02168 414 drRERLQQEIEELLKKLEEAELKELQAELEELEEELEElqeelERLEEALEELREELEEAEQALDAAERELAQLQArlds 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 669 --SLQKKIEGAQQ--KEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQEVE--------------REHE---- 726
Cdd:TIGR02168 494 leRLQENLEGFSEgvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVvenlnaakkaiaflKQNElgrv 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 727 ----------------RKMDKMKEEHWQEMADARERYEAEERKQRADLLGH------LTGELERLRRAHEREL------- 777
Cdd:TIGR02168 574 tflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRPGYRivtldgd 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 778 ---------------ESMRQEQDQQLEDLRRR-------HRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQ 835
Cdd:TIGR02168 654 lvrpggvitggsaktNSSILERRREIEELEEKieeleekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 836 LLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQ 915
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 916 RKQDVL--KEMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDL--------SMESVRQFLSAEGVAVR 985
Cdd:TIGR02168 814 LLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleALLNERASLEEALALLR 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 986 NAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQevdEDLPGTEV-LGNMRKNLNEETR-HLDEMKSAMRKGHDLLKKK 1063
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVrIDNLQERLSEEYSlTLEEAEALENKIEDDEEEA 970
|
730
....*....|...
gi 160420304 1064 EEKLIQLESSLQE 1076
Cdd:TIGR02168 971 RRRLKRLENKIKE 983
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
548-1077 |
5.22e-12 |
|
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: 70.77 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERasleqksrraLEQLREQLEAEERSAQAALraekeaekeAALL 627
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----------KQQLLKQLRARIEELRAQE---------AVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 628 QLREQLEGERKEAVAGLEKKHSAELEQ----LCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQv 703
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQqaqrIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRD- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 704 tEYEQELSSLLRDKRQEVEREHERKMDKMKE-------------EHWQEMADARERYEAEERKQRADLLGHLTGELERLR 770
Cdd:TIGR00618 360 -AHEVATSIREISCQQHTLTQHIHTLQQQKTtltqklqslckelDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 771 RAHERELESMRQEQDQQLE-----DLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIR--KEKQLLLDAQRQ 843
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEkihlqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCplCGSCIHPNPARQ 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 844 AALEREEATATHQHLEEAKKEHTHLLETkqqLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEV----QRKQD 919
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEED---VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlqNITVR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 920 VLKEMAAEMNASPHPEPGLHIEDLRKSLDTNkNQEVSSSLSLSKEEIDLSMESVRQFLSA-----EGVAVRNAKEFlvrQ 994
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLRKLQPEQD-LQDVRLHLQQCSQELALKLTALHALQLTltqerVREHALSIRVL---P 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 995 TRSMRRRQTALKAAQqhwrHELASAQEVDEDLPGT-EVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESS 1073
Cdd:TIGR00618 672 KELLASRQLALQKMQ----SEKEQLTYWKEMLAQCqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
....
gi 160420304 1074 LQEE 1077
Cdd:TIGR00618 748 LMHQ 751
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
559-910 |
1.23e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.60 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 559 ENQIRTEQQAaLQRLREEAETLqKAERASLEQksrrALEQLREQLEaeerSAQAALRAEKEAEK-EAALLQLREQLEgER 637
Cdd:PRK04863 299 RRQLAAEQYR-LVEMARELAEL-NEAESDLEQ----DYQAASDHLN----LVQTALRQQEKIERyQADLEELEERLE-EQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 638 KEAVAGL--------EKKHSAELEQLC--SSLeAKHQEVISSLQKKIEGAQQKEEAqLQESLGWAeQRAHQKVHQVTEYE 707
Cdd:PRK04863 368 NEVVEEAdeqqeeneARAEAAEEEVDElkSQL-ADYQQALDVQQTRAIQYQQAVQA-LERAKQLC-GLPDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 708 QELssllRDKRQEVE---REHERKMDkmkeehwqeMAD-ARERYEaeerkQRADLLGHLTGELERLR-----RAHERELE 778
Cdd:PRK04863 445 EEF----QAKEQEATeelLSLEQKLS---------VAQaAHSQFE-----QAYQLVRKIAGEVSRSEawdvaRELLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 779 SMRQeQDQQLEDLRRRHRDHERKLQdLEVELSSRTKDVKARLAQ-----LNVQEENIRKEkQLLLDAQRQAALEREEATA 853
Cdd:PRK04863 507 EQRH-LAEQLQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKnlddeDELEQLQEELE-ARLESLSESVSEARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 854 THQHLEEAKKEHTHL------------------------LETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSS 909
Cdd:PRK04863 584 LRQQLEQLQARIQRLaarapawlaaqdalarlreqsgeeFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
.
gi 160420304 910 L 910
Cdd:PRK04863 664 L 664
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
561-1077 |
1.77e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 69.23 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 561 QIRTEQQAALQRLREEAEtLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEA 640
Cdd:pfam02463 177 KLIEETENLAELIIDLEE-LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 641 VAGLEKKHSAELEQlcSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAH----QKVHQVTEYEQELSSLLRD 716
Cdd:pfam02463 256 SKQEIEKEEEKLAQ--VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVddeeKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 717 KRQEVEREHERK-MDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQ----LEDL 791
Cdd:pfam02463 334 KEEIEELEKELKeLEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKeaqlLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 792 RRRHRDHERKLQD------LEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKE- 864
Cdd:pfam02463 414 ARQLEDLLKEEKKeeleilEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRq 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 865 --------HTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNASPHPEP 936
Cdd:pfam02463 494 kleersqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 937 GLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRSMRRRQTALKAAQ--QHWRH 1014
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESglRKGVS 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160420304 1015 ELASAQEVDEDLPGTEVLGNMRKN--LNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEE 1077
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEiqELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
517-883 |
2.95e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 517 KAQLQKATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRAL 596
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 597 EQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGER----------KEAVAGLEKKHSAEL---EQLCSSLEAKH 663
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkaeeakkaDEAKKAEEKKKADELkkaEELKKAEEKKK 1565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 664 -------QEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQElssllRDKRQEVEREHE--RKMDKMKE 734
Cdd:PTZ00121 1566 aeeakkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-----KIKAEELKKAEEekKKVEQLKK 1640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 735 EHWQEMADARE-RYEAEERKQRADLLGHLTGE----LERLRRAHERELESMRQ-----EQDQQLEDLRRRHRDHERKLQD 804
Cdd:PTZ00121 1641 KEAEEKKKAEElKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAAEAlkkeaEEAKKAEELKKKEAEEKKKAEE 1720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 805 LEV----------ELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQhlEEAKKEHThllETKQQ 874
Cdd:PTZ00121 1721 LKKaeeenkikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDE---KRRME 1795
|
....*....
gi 160420304 875 LRRTIDDLR 883
Cdd:PTZ00121 1796 VDKKIKDIF 1804
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
566-1077 |
5.48e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 566 QQAALQRLREEAETLQKAERASLEQKsRRALEQLREQLEA-EERSAQAALraekeAEKEAALLQLREQL---EGERKEAV 641
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQ-RGSLDQLKAQIEEkEEKDLHERL-----NGLESELAELDEEIeryEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 642 AGLEkkhsaELEQLCSSLEAKHQEvISSLQKKIEGAQQKEEAQLQESLGWAEQrahqkVHQVTEYEQELSSLLRDKRQEV 721
Cdd:PRK02224 234 ETRD-----EADEVLEEHEERREE-LETLEAEIEDLRETIAETEREREELAEE-----VRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 722 ERehERKMDKMKEEHWQEMADARERYEAEERKQRADlLGHLTGELERLR----RAHER--ELESMRQEQDQQLEDLRRRH 795
Cdd:PRK02224 303 GL--DDADAEAVEARREELEDRDEELRDRLEECRVA-AQAHNEEAESLRedadDLEERaeELREEAAELESELEEAREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 796 RDHERKLQDLEVELssrtKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLL------ 869
Cdd:PRK02224 380 EDRREEIEELEEEI----EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcp 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 870 ETKQQLR-----RTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAevqrkqdvLKEMAAEmnasphpepglhIEDLR 944
Cdd:PRK02224 456 ECGQPVEgsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAED--------LVEAEDR------------IERLE 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 945 KSLDTnkNQEVSSSLSLSKEEIDLSMESVR---QFLSAEGVAVRNAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQE 1021
Cdd:PRK02224 516 ERRED--LEELIAERRETIEEKRERAEELReraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 160420304 1022 VDEDLPGTEVLGNMRKNLNEETRHLDEMKSAMRkghDLLKKKEEKLIQLESSLQEE 1077
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERR---ERLAEKRERKRELEAEFDEA 646
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
574-918 |
6.57e-11 |
|
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: 67.07 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 574 REEAETLQKAERASLEQKSRRALEQL--REQLEAEERSAQAALRAEKEAEKEaallQLREQLEGERkeavaglekkhsaE 651
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAE----QERMAMERER-------------E 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 652 LEQLcsSLEAKHQEVISSLQKKIegAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSsLLRDKRQEVEREHERKMDK 731
Cdd:pfam17380 350 LERI--RQEERKRELERIRQEEI--AMEISRMRELERLQMERQQKNERVRQELEAARKVK-ILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 732 MkeehwqemadareRYEAEERKQRadllghltgELERLRRAHERELESMRQE-QDQQLEDLRRRHRDHERKLQDLEVEls 810
Cdd:pfam17380 425 I-------------RAEQEEARQR---------EVRRLEEERAREMERVRLEeQERQQQVERLRQQEEERKRKKLELE-- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 811 sRTKDVKARLAQLN--VQEENIRKEKQLLLDAQRQAAL------EREEATATHQHLEEAKKEHTHLLETKQqlRRTIDDL 882
Cdd:pfam17380 481 -KEKRDRKRAEEQRrkILEKELEERKQAMIEEERKRKLlekemeERQKAIYEEERRREAEEERRKQQEMEE--RRRIQEQ 557
|
330 340 350
....*....|....*....|....*....|....*.
gi 160420304 883 RVRRVELESQVDLLQAQSQRLQKhlsSLEAEVQRKQ 918
Cdd:pfam17380 558 MRKATEERSRLEAMEREREMMRQ---IVESEKARAE 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
733-1028 |
8.66e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 733 KEEHWQEMADARERYEaEERKQRADLLGHLTGELERLRRAHeRELESMRQEQDQQLEDLRRRHRDHERKLQdlevELSSR 812
Cdd:TIGR02168 237 LREELEELQEELKEAE-EELEELTAELQELEEKLEELRLEV-SELEEEIEELQKELYALANEISRLEQQKQ----ILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 813 TKDVKARLAQLNVQEENIRKEKQLLLD--AQRQAALE--REEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVE 888
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEelAELEEKLEelKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 889 LESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVlkemaaemnasphpepglhIEDLRKSLDTNKNQEVSSSLSLSKEEIDL 968
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQE-------------------IEELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 969 SMESVRqflsaegvAVRNAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPG 1028
Cdd:TIGR02168 452 LQEELE--------RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
631-928 |
1.48e-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: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 631 EQLEGERKEAVAGLEKKHSAELEQLCSsleaKHQEVISSLQKKIEGAQQKEEAqLQESLGWAEQRAHQK----VHQVTEY 706
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLIS----EHEVEITGLTEKASSARSQANS-IQSQLEIIQEQARNQnsmyMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 707 EQELSSLlRDKRQEVEREHErkmDKMKEEHWQEMADARERYEAE-ERKQRADLLGHLTGELERL-RRAHERELE-SMRQE 783
Cdd:pfam15921 323 ESTVSQL-RSELREAKRMYE---DKIEELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLlADLHKREKElSLEKE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 784 QDQQLEDlrrRHRDHERKLQDLEVELSSRTKDVKARLAQLNVqeenirkekqllLDAQRQAALEREEAT--ATHQHLEEA 861
Cdd:pfam15921 399 QNKRLWD---RDTGNSITIDHLRRELDDRNMEVQRLEALLKA------------MKSECQGQMERQMAAiqGKNESLEKV 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160420304 862 KKEHTHLLETKQQLRRTIDDLRVRRVELESQvdllqaqsqrlQKHLSSLEAEVQRKQDVLKEMAAEM 928
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEELTAKKMTLESS-----------ERTVSDLTASLQEKERAIEATNAEI 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
568-820 |
1.63e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 568 AALQRLREEAETLQKAERASLE-QKSRRALEQLREQLE-----AEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAV 641
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDaREQIELLEPIRELAEryaaaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 642 AGLEkkhsAELEQLcSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLlrdkrqEV 721
Cdd:COG4913 305 ARLE----AELERL-EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL------GL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 722 EREHERKMDKMKEEHWQEMADARERYEAEERKQRAdllghltgELERLRRAHERELESMRQEqdqqLEDLRRRHRDHERK 801
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALA--------EAEAALRDLRRELRELEAE----IASLERRKSNIPAR 441
|
250
....*....|....*....
gi 160420304 802 LQDLEVELSSRTKDVKARL 820
Cdd:COG4913 442 LLALRDALAEALGLDEAEL 460
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
659-928 |
3.10e-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: 65.09 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 659 LEAKHQEVISSLQKKIEGAQQKEEAQ-LQESLGWAEQRAHqkVHQVTEYEQELSSLLRDkRQEVEREHErKMDKMKEEHW 737
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAERYQaLLKEKREYEGYEL--LKEKEALERQKEAIERQ-LASLEEELE-KLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 738 QEMADARERYEAEERKQRAdllghLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSrtkdVK 817
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKD-----LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK----LL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 818 ARLAQLNVQEENIRKEKQLLLDAQRQAALEREEataTHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQ 897
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270
....*....|....*....|....*....|.
gi 160420304 898 AQSQRLQKHLSSLEAEVQRKQDVLKEMAAEM 928
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
556-919 |
3.87e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 556 EAFENQIRtEQQAALQRLREEAETLqkAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKeaallQLREQLEG 635
Cdd:PRK02224 275 EELAEEVR-DLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-----AHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 636 ERKEAvAGLEKKhSAELEQLCSSLEA----------KHQEVISSLQKKIE---------GAQQKEEAQLQESLGWAEQRA 696
Cdd:PRK02224 347 LREDA-DDLEER-AEELREEAAELESeleeareaveDRREEIEELEEEIEelrerfgdaPVDLGNAEDFLEELREERDEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 697 HQKvhqVTEYEQELSSlLRDKRQEVER-----------------EH----ERKMDKmKEEHWQEMADARERYEA-EERKQ 754
Cdd:PRK02224 425 RER---EAELEATLRT-ARERVEEAEAlleagkcpecgqpvegsPHvetiEEDRER-VEELEAELEDLEEEVEEvEERLE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 755 RADLLGHLTGELERLRRAHER------ELESMRQEQDQQLEDLRRRHRDHERKLQDLE---VELSSRTKDVKARLAQLNV 825
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDleeliaERRETIEEKRERAEELRERAAELEAEAEEKReaaAEAEEEAEEAREEVAELNS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 826 QEENIRKEKQLLLDAQRQAAlEREEATATHQHLEEAKKehtHLLETKQQLRRTIDDLRVRRVELESQVD-----LLQAQS 900
Cdd:PRK02224 580 KLAELKERIESLERIRTLLA-AIADAEDEIERLREKRE---ALAELNDERRERLAEKRERKRELEAEFDearieEAREDK 655
|
410
....*....|....*....
gi 160420304 901 QRLQKHLSSLEAEVQRKQD 919
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELRE 674
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
565-927 |
8.65e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQKAerasleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGL 644
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL------QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 645 E--KKHSAELEQLCSSLEAKHQEvISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSL---LRDKRQ 719
Cdd:COG4717 149 EelEERLEELRELEEELEELEAE-LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAqeeLEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 720 EVEREHERKMDKMKEEHWQEMA-------------------------------------------DARERYEAEERKQRA 756
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 757 DLLGHLTG----ELERLRRAH--------ERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKA------ 818
Cdd:COG4717 308 QALPALEEleeeELEELLAALglppdlspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVedeeel 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 819 RLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQA 898
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420
....*....|....*....|....*....
gi 160420304 899 QSQrlqkhLSSLEAEVQRKQDVLKEMAAE 927
Cdd:COG4717 468 DGE-----LAELLQELEELKAELRELAEE 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
705-923 |
9.40e-10 |
|
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: 63.22 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 705 EYEQELSSLLRDKRQEVEREHERKMDKM--------KEEHWQEMADARERYEAEERKQRA-DLLGHLTGELERLRRAHER 775
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKMeqerlrqeKEEKAREVERRRKLEEAEKARQAEmDRQAAIYAEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 776 ELESMRQEQ-DQQLEDLRRRHRDHE----RKLQDLEVELSSRTKDVKARLaqlnvqeENIRKEKQLLLDAQRQAALEREE 850
Cdd:pfam17380 349 ELERIRQEErKRELERIRQEEIAMEisrmRELERLQMERQQKNERVRQEL-------EAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160420304 851 ATATHQHLEEAKKEHTHLLETKqqlrRTIDDLRVRRVELE--SQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKE 923
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEE----RAREMERVRLEEQErqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
548-843 |
2.51e-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: 62.01 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIrTEQQAALQRLREE-AETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAAL 626
Cdd:TIGR02169 239 KEAIERQLASLEEEL-EKLTEEISELEKRlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 627 lqlrEQLEGERKEAVAGLEKKhSAELEQLCSSLEAKHQEVIsSLQKKIEGAQQKEEAQLQEsLGWAEQRAHQKVHQVTEY 706
Cdd:TIGR02169 318 ----EDAEERLAKLEAEIDKL-LAEIEELEREIEEERKRRD-KLTEEYAELKEELEDLRAE-LEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 707 EQELSSLLRdKRQEVEREHERKMDKMKEEHwQEMADARERYEAEERKQRAdllghLTGELERLR---RAHERELESMRqe 783
Cdd:TIGR02169 391 REKLEKLKR-EINELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINE-----LEEEKEDKAleiKKQEWKLEQLA-- 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 784 qdQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIR--KEKQLLLDAQRQ 843
Cdd:TIGR02169 462 --ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggRAVEEVLKASIQ 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
712-905 |
3.40e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 712 SLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRAdlLGHLTGELERLRRAHErELESMRQEQDQQLEDL 791
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE--YAELQEELEELEEELE-ELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 792 RR--RHRDHERKLQDLEVELSS---RTKDVKARLAQLNVQEENIRKEKQLLLDAQRQ-AALEREEATATHQHLEEAKKEH 865
Cdd:COG4717 122 EKllQLLPLYQELEALEAELAElpeRLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 160420304 866 THLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQK 905
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-1098 |
4.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 531 EEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEqqaALQRLREEAETLQKAERASlEQKSRRALEQLREQLEAEERSA 610
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAE-AEAAADEAEAAEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 611 QAAlraekeaekeaallqlREQLEGERKEAVaglEKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLG 690
Cdd:PTZ00121 1374 EEA----------------KKKADAAKKKAE---EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 691 WAEQRAHQKvHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemadARERYEAEERKQRADLLGHLTGELERLR 770
Cdd:PTZ00121 1435 EAKKKAEEA-KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-------AEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 771 RAHERELESMRQEQDQQLEDLRRrhRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREE 850
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 851 AT--ATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSL-EAEVQRKQDVLKEMAAE 927
Cdd:PTZ00121 1585 EAkkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAA 1664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 928 MNASPHPEPGLHIEDLRKSLDTNKNQEvssSLSLSKEEIDLSMESVRQFLSAEgvaVRNAKEflVRQTRSMRRrqtaLKA 1007
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAA---EALKKEAEEAKKAEELKKKEAEE---KKKAEE--LKKAEEENK----IKA 1732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 1008 AQqhwrhelaSAQEVDEDlpgtevlgnmRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEEVSDEDTLKGS 1087
Cdd:PTZ00121 1733 EE--------AKKEAEED----------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
570
....*....|.
gi 160420304 1088 SIKKVTFDLSD 1098
Cdd:PTZ00121 1795 EVDKKIKDIFD 1805
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
550-837 |
4.21e-09 |
|
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: 60.91 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 550 QVQSRTEAFENQ-IRTEQQAALQRL--REEAETLQKAERASLEQKS-------RRALEQLRE--QLEAEERSAQAALRAE 617
Cdd:pfam17380 288 QQQEKFEKMEQErLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAaiyaeqeRMAMEREREleRIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 618 KEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQlcSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAH 697
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKV--KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 698 QKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERY----EAEERKQRADllghltgELERLRRAH 773
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilekELEERKQAMI-------EEERKRKLL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160420304 774 ERELEsmrQEQDQQLEDLRRRHRDHERKLQdLEVELSSRTKDVKARLAQLNVQEENIRKEKQLL 837
Cdd:pfam17380 519 EKEME---ERQKAIYEEERRREAEEERRKQ-QEMEERRRIQEQMRKATEERSRLEAMEREREMM 578
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-927 |
4.30e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 719 QEVEREHERKMDKMKeehwQEMADARERYEAEERKQRAdllghLTGELERLRRAhERELESMRQEQDQQLEDLRRRHRDH 798
Cdd:COG4942 19 ADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKA-----LLKQLAALERR-IAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 799 ERKLQDLEVELSSRTKDVKARLAQLnvQEENIRKEKQLLL------DAQRQAALEREEATATHQHLEEAKKEHTHLLETK 872
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRAL--YRLGRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 160420304 873 QQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAE 927
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
573-1099 |
7.64e-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: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 573 LREEAETLQKAERASLEQKSR-RALEQ----LREQLEAEERSAQAALRAEKEAEKEaaLLQLREQLEGERKEAVAGLE-- 645
Cdd:pfam01576 470 LQDTQELLQEETRQKLNLSTRlRQLEDernsLQEQLEEEEEAKRNVERQLSTLQAQ--LSDMKKKLEEDAGTLEALEEgk 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 646 KKHSAELEQLCSSLEAKHQEViSSLQKKIEGAQQKEEAQL-----QESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQE 720
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAY-DKLEKTKNRLQQELDDLLvdldhQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 721 VE---REHERKMDKMKEEhWQEMADARERYEAEERKQRADL---------LGHLTGELERLRRAHERELESMRqEQDQQL 788
Cdd:pfam01576 627 AEaeaREKETRALSLARA-LEEALEAKEELERTNKQLRAEMedlvsskddVGKNVHELERSKRALEQQVEEMK-TQLEEL 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 789 EDLRRRHRD---------------HERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEA-- 851
Cdd:pfam01576 705 EDELQATEDaklrlevnmqalkaqFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELea 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 852 --TATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVEL-------ESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLK 922
Cdd:pfam01576 785 qiDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 923 EMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEID-------LSMESVRQFLSAEGVA---VRNAKEFLV 992
Cdd:pfam01576 865 ELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNdrlrkstLQVEQLTTELAAERSTsqkSESARQQLE 944
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 993 RQTRSMRRR--------QTALKAAQQHWRHELASA-----QEVDEDLPGTEVLGNMRKNLNE-------ETRHLDEMKSA 1052
Cdd:pfam01576 945 RQNKELKAKlqemegtvKSKFKSSIAALEAKIAQLeeqleQESRERQAANKLVRRTEKKLKEvllqvedERRHADQYKDQ 1024
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 160420304 1053 MRKGHDLLKkkeekliQLESSLqEEVSDEDTLKGSSIKKVTFDLSDM 1099
Cdd:pfam01576 1025 AEKGNSRMK-------QLKRQL-EEAEEEASRANAARRKLQRELDDA 1063
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
664-1077 |
7.83e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 664 QEVISSLQKKIEGAQQ--KEEAQLQESLGWAEQRAHQKVHQVteyeQELSSLLRDKRQEVE--REHERKMDKMKEEHwqe 739
Cdd:PRK03918 168 GEVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEklEKEVKELEELKEEI--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 740 madareryeAEERKQRADLLGHLTGELERLR---------RAHERELESMRQEQDQ---------QLEDLRRRHRDHERK 801
Cdd:PRK03918 241 ---------EELEKELESLEGSKRKLEEKIReleerieelKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 802 LQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQR------------------QAALEREEATATHQHLEEAKK 863
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerhelyeeakakKEELERLKKRLTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 864 EHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKH-----LSSLEAEVQRKQDVLKEMAAEmnasphpepgl 938
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAE----------- 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 939 hIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMEsvRQFLSAEGVA--VRNAKEFLvrqtrsmrrRQTALKAAQQHWRhel 1016
Cdd:PRK03918 461 -LKRIEKELKEIEEKERKLRKELRELEKVLKKE--SELIKLKELAeqLKELEEKL---------KKYNLEELEKKAE--- 525
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160420304 1017 aSAQEVDEDLPGtevLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEE 1077
Cdd:PRK03918 526 -EYEKLKEKLIK---LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
714-917 |
8.10e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 714 LRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEER-KQRADLLGHLTGELERLRR---AHERELESMRQEQDQQLE 789
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAelaELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 790 DLRRRHRDHER--KLQDLEVELSS--------RTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLE 859
Cdd:COG4942 105 ELAELLRALYRlgRQPPLALLLSPedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 160420304 860 EAKKEhthLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRK 917
Cdd:COG4942 185 EERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
548-865 |
9.89e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLE--QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAA 625
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEelEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 626 LLQLREQLEGERKEAVAGLEKKHSAELEQLCSSL-------EAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQR--- 695
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALglp 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 696 AHQKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEE-----------------HWQEMADARERYEAEERKQRADL 758
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeeelrAALEQAEEYQELKEELEELEEQL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 759 LGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDvkARLAQLnvqeeniRKEKQLLL 838
Cdd:COG4717 412 EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAEL-------LQELEELK 482
|
330 340
....*....|....*....|....*..
gi 160420304 839 DAQRQAALEREEATATHQHLEEAKKEH 865
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREEY 509
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
726-867 |
1.25e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 59.02 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 726 ERKMDKMKEEHWQEMADAREryEAEERKQRADLlgHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDL 805
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK--EAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160420304 806 ---EVELSSRTKDVKARLAQLNVQEENI-RKEKQLLLDAQRQAALEREEATAthQHLEEAKKEHTH 867
Cdd:PRK12704 106 ekrEEELEKKEKELEQKQQELEKKEEELeELIEEQLQELERISGLTAEEAKE--ILLEKVEEEARH 169
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
547-955 |
2.75e-08 |
|
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: 58.70 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 547 LRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQ-KAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAA 625
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 626 LLQLRE-QLEGERKEAVAGLEKKHSAeLEQLCSSLEAKHQEVISSLQKKIEgAQQKEEAQLQESLGW---AEQRAHQKVH 701
Cdd:pfam12128 489 RLQSELrQARKRRDQASEALRQASRR-LEERQSALDELELQLFPQAGTLLH-FLRKEAPDWEQSIGKvisPELLHRTDLD 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 702 QVTEYEQELSSL------LRDKRQEV------EREHERKMDKMKEehwqEMADARERYEAEERKqradlLGHLTGELERL 769
Cdd:pfam12128 567 PEVWDGSVGGELnlygvkLDLKRIDVpewaasEEELRERLDKAEE----ALQSAREKQAAAEEQ-----LVQANGELEKA 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 770 RRAHERELES--------------MRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQ 835
Cdd:pfam12128 638 SREETFARTAlknarldlrrlfdeKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 836 LL-----------LDAQRQAALEREEATATHQ-------HLEEAKK--EHTHLLETKQQLR---RTIDDLRVRRVELESQ 892
Cdd:pfam12128 718 AYwqvvegaldaqLALLKAAIAARRSGAKAELkaletwyKRDLASLgvDPDVIAKLKREIRtleRKIERIAVRRQEVLRY 797
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160420304 893 VDLLQA----QSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNasphpepgLHIEDLRKSLDTNKNQEV 955
Cdd:pfam12128 798 FDWYQEtwlqRRPRLATQLSNIERAISELQQQLARLIADTK--------LRRAKLEMERKASEKQQV 856
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-824 |
4.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 542 RRLVCLRAQVQSRTEAFE--NQIRTEQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAAlraeke 619
Cdd:COG4913 610 AKLAALEAELAELEEELAeaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS------ 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 620 aekEAALLQLREQLEgERKEAVAGLEKKHsAELEQLCSSLEAKH---QEVISSLQKKIEGAQQKEEAQLQESLgwaEQRA 696
Cdd:COG4913 684 ---SDDLAALEEQLE-ELEAELEELEEEL-DELKGEIGRLEKELeqaEEELDELQDRLEAAEDLARLELRALL---EERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 697 HQkvHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEehwqEMADARERYEAEERKQRADL--LGHLTGELERLR---- 770
Cdd:COG4913 756 AA--ALGDAVERELRENLEERIDALRARLNRAEEELER----AMRAFNREWPAETADLDADLesLPEYLALLDRLEedgl 829
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 160420304 771 -RAHERELESMRQEQDQQLEDLRRRHRDHERklqdlevelssrtkDVKARLAQLN 824
Cdd:COG4913 830 pEYEERFKELLNENSIEFVADLLSKLRRAIR--------------EIKERIDPLN 870
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
514-840 |
5.02e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 514 SLLKAQLQKATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQI------RTEQQAALQRLREEAETLQ-KAERA 586
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleerLEEAEEELAEAEAEIEELEaQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 587 SLE-QKSRRALEQLREQLEAE-ERSAQAALRAEKEAEKEAALLQLREQLEGERKEAvagleKKHSAELEQLCSSLEAKhq 664
Cdd:TIGR02168 795 KEElKALREALDELRAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEEL-----SEDIESLAAEIEELEEL-- 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 665 evISSLQKKIEGAqQKEEAQLQESLGWAEQRAHQKVHQVTEYEQelssllrdKRQEVEREHERKMDKmkeehwqeMADAR 744
Cdd:TIGR02168 868 --IEELESELEAL-LNERASLEEALALLRSELEELSEELRELES--------KRSELRRELEELREK--------LAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 745 ERYeaEERKQRADLLghltgeLERLRRAHERELESMRQEQ---DQQLEDLRRRHRDHERKLQDL-EVELSSRT--KDVKA 818
Cdd:TIGR02168 929 LRL--EGLEVRIDNL------QERLSEEYSLTLEEAEALEnkiEDDEEEARRRLKRLENKIKELgPVNLAAIEeyEELKE 1000
|
330 340
....*....|....*....|..
gi 160420304 819 RLAQLNVQEENIRKEKQLLLDA 840
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
554-842 |
5.06e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 554 RTEAFENQIRT--EQQAALQRLREEAETLQKAERASLEQksrraLEQLREQLEAEERSAQAALRAEKEAEKEaalLQLRE 631
Cdd:TIGR02168 233 RLEELREELEElqEELKEAEEELEELTAELQELEEKLEE-----LRLEVSELEEEIEELQKELYALANEISR---LEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 632 QLEGERKEAVAGLEKKHSAELEQLCSSLEAKhQEVISSLQKKIEGAQQ--KEEAQLQESLGWAEQRAHQKVHQVTEYEQE 709
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDEL-AEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 710 LSSLLRDKRQEVEREHERKmdKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQD---Q 786
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEI--ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 787 QLEDLRRRHRDHERKLQDLEVELSSrtkdVKARLAQLNVQEENIRKE----KQLLLDAQR 842
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQ----LQARLDSLERLQENLEGFsegvKALLKNQSG 517
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
548-933 |
8.89e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERAS--LEQKSRRALEQLR--EQLEAEERSAQAALRAEKEaeke 623
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKrqLDRESDRNQELQKriRLLEKREAEAEEALREQAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 624 aallqlREQLEGERKEAVAGLEKKHSAELEQLCSSLEAKHQEvISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKvHQV 703
Cdd:pfam05557 77 ------LNRLKKKYLEALNKKLNEKESQLADAREVISCLKNE-LSELRRQIQRAELELQSTNSELEELQERLDLLK-AKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 704 TEYEQELSSLlrDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRadlLGHLTGELERLRR--AHERELESMR 781
Cdd:pfam05557 149 SEAEQLRQNL--EKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR---IPELEKELERLREhnKHLNENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 782 QEQDQQLEDLRR---RHRDHERKLQDLEVELSSRTKDVKA--RLAQ-----LNVQEENIRKEKQLLldaQRQAALEREEA 851
Cdd:pfam05557 224 LLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSwvKLAQdtglnLRSPEDLSRRIEQLQ---QREIVLKEENS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 852 TATHQ--HLEEAKKEhthLLETKQQLRRTIDDLRVRRVELESQVDllqaqsqRLQKHLSSLEAEVQRKQDVLKEMAAEMN 929
Cdd:pfam05557 301 SLTSSarQLEKARRE---LEQELAQYLKKIEDLNKKLKRHKALVR-------RLQRRVLLLTKERDGYRAILESYDKELT 370
|
....
gi 160420304 930 ASPH 933
Cdd:pfam05557 371 MSNY 374
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
740-930 |
1.38e-07 |
|
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: 54.16 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 740 MADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEqdqqLEDLRRRHRDHERKLQDLEVELssrtKDVKAR 819
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEI----EEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 820 LAQLNVQEENIRKEKQLlldaqrqAALEREEATATHQhLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAq 899
Cdd:COG1579 75 IKKYEEQLGNVRNNKEY-------EALQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA- 145
|
170 180 190
....*....|....*....|....*....|.
gi 160420304 900 sqRLQKHLSSLEAEVQRKQDVLKEMAAEMNA 930
Cdd:COG1579 146 --ELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
548-716 |
1.52e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRT------EQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAE 621
Cdd:COG3206 170 REEARKALEFLEEQLPElrkeleEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 622 KEAA--------------LLQLREQLEGERKEAVAGLEKKHS------AELEQLCSSLEAKHQEVISSLQKKIEGAQQkE 681
Cdd:COG3206 250 GSGPdalpellqspviqqLRAQLAELEAELAELSARYTPNHPdvialrAQIAALRAQLQQEAQRILASLEAELEALQA-R 328
|
170 180 190
....*....|....*....|....*....|....*
gi 160420304 682 EAQLQESLgwaeQRAHQKVHQVTEYEQELSSLLRD 716
Cdd:COG3206 329 EASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
578-882 |
1.64e-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: 56.00 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 578 ETLQKAERASLEQKSRRALEQLREQLEAEERSAQAAlraekeaekEAALLQLREQLEGERKEAVAGLEKKHSAELEQlcS 657
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA---------EEQLVQANGELEKASREETFARTALKNARLDL--R 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 658 SLEAKHQEVISSLQKKIEGAQQKEEAQLQESLgwAEQRAHQKVHQVTEYEQ-----ELSSLLRDKRQEVEREHERKMDKM 732
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLE--AQLKQLDKKHQAWLEEQkeqkrEARTEKQAYWQVVEGALDAQLALL 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 733 KEE--HWQEMADARERYEAEERKQRADLLG--------------HLTGELERL--RRAHERELESMRQEQ-DQQLEDLRR 793
Cdd:pfam12128 735 KAAiaARRSGAKAELKALETWYKRDLASLGvdpdviaklkreirTLERKIERIavRRQEVLRYFDWYQETwLQRRPRLAT 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 794 RHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQR--QAALEREEATATHQHLEEAKKEHTHLLET 871
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRglRCEMSKLATLKEDANSEQAQGSIGERLAQ 894
|
330
....*....|.
gi 160420304 872 KQQLRRTIDDL 882
Cdd:pfam12128 895 LEDLKLKRDYL 905
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
588-1076 |
1.88e-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: 55.75 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 588 LEQKSRRALEQLREQLEAE--ERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQLCSSL-EAKHQ 664
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDqyTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 665 EVISSLQKKIEGAQQKEEAQLQESLGWA-----EQRAHQKVHQVTEYEQELS-------------SLLRDKRQEVEREHE 726
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLrarieELRAQEAVLEETQERINRArkaaplaahikavTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 727 RKMDKMKEEHWQEMADARERYEAEERKQradLLGHLTGELERLRRAHERELeSMRQEQDQQLEDLRRRHRDHERK--LQD 804
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRR---LLQTLHSQEIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQKttLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 805 LEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEE----AKKEHTHLLETKQQLRRTID 880
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqcEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 881 DLRVRRVELESQVDLLQAQSQRLQKHlSSLEAEVQRKqdvLKEMAAEMNASPHPEPglhiedlrkslDTNKNQEVSSSLS 960
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGS---CIHPNPARQDIDNPGP-----------LTRRMQRGEQTYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 961 LSKEEIdlsmESVRqflsAEGVAVRNAKEFLVRQTRSMrrRQTALKAAQQHwrhelasaQEVDEDLPGTevlgnmrKNLN 1040
Cdd:TIGR00618 539 QLETSE----EDVY----HQLTSERKQRASLKEQMQEI--QQSFSILTQCD--------NRSKEDIPNL-------QNIT 593
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 160420304 1041 EETRHLDEMKSAMRK-----GHDLLKKKEEKLIQLESSLQE 1076
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDmlaceQHALLRKLQPEQDLQDVRLHL 634
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
541-912 |
1.88e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 541 SRRLVCLRAQVQSRTEAFENQ-IRTEQQAALQRLREEAETLQKAERAsLEQKSRRALEQLREqleaeersAQAALRAEKE 619
Cdd:COG3096 278 NERRELSERALELRRELFGARrQLAEEQYRLVEMARELEELSARESD-LEQDYQAASDHLNL--------VQTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 620 -AEKEAALLQLREQLEgERKEAVAGL--------EKKHSAELE--QLCSSLeAKHQEVISSLQKKIEGAQQ----KEEAQ 684
Cdd:COG3096 349 iERYQEDLEELTERLE-EQEEVVEEAaeqlaeaeARLEAAEEEvdSLKSQL-ADYQQALDVQQTRAIQYQQavqaLEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 685 LQ---ESLGWAEQRAHQKVHQvtEYEQELSSLLRDKRQEVE------REHERKMdkmkeEHWQEMADARERYEAEERKQ- 754
Cdd:COG3096 427 ALcglPDLTPENAEDYLAAFR--AKEQQATEEVLELEQKLSvadaarRQFEKAY-----ELVCKIAGEVERSQAWQTARe 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 755 ---RADLLGHLTGELERLRRAH---ERELESmRQEQDQQLEDLRRRH---RDHERKLQDLEVELSSRTKDVKARLAqlNV 825
Cdd:COG3096 500 llrRYRSQQALAQRLQQLRAQLaelEQRLRQ-QQNAERLLEEFCQRIgqqLDAAEELEELLAELEAQLEELEEQAA--EA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 826 QEENIRKEKQLLLDAQRQAALEREE-----ATATHQHLEEAKKEHthlLETKQQLRRTIDDLRVRRVELESQVDLLQAQS 900
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARApawlaAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERDELAARK 653
|
410
....*....|..
gi 160420304 901 QRLQKHLSSLEA 912
Cdd:COG3096 654 QALESQIERLSQ 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
750-1009 |
2.14e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 750 EERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEEN 829
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 830 IRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSS 909
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 910 LEAEVQRKQDVLKEMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKE 989
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260
....*....|....*....|
gi 160420304 990 FLVRQTRSMRRRQTALKAAQ 1009
Cdd:COG4372 249 EELLEEVILKEIEELELAIL 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-1073 |
2.21e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 655 LCSSLEAKHQEvISSLQKKIEGAQQKEEAQLQESLGWAEQRaHQKVHQVTEYEQELSSLLRDKRQEVE--REHERKMDKM 732
Cdd:COG4717 47 LLERLEKEADE-LFKPQGRKPELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEelREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 733 KE--EHWQEMADARERYEA------------EERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDH 798
Cdd:COG4717 125 LQllPLYQELEALEAELAElperleeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 799 ERKLQDLEVELssrtKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALERE--------EATATHQHLEEAKKEHTHLLE 870
Cdd:COG4717 205 QQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 871 TKQQLRrTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEaevqrkqdvLKEMAAEMNASPHPEPGlHIEDLRKSLDTN 950
Cdd:COG4717 281 LVLGLL-ALLFLLLAREKASLGKEAEELQALPALEELEEEE---------LEELLAALGLPPDLSPE-ELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 951 KNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAvrNAKEFLVRQTRSmrRRQTALKAAQQHWRHELASAQEVDEDLPGTE 1030
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGVE--DEEELRAALEQA--EEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 160420304 1031 VLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESS 1073
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
572-1076 |
2.44e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 572 RLREEAETLQK---AERASLEQKSRRaLEQLREQLEAEERSAQaalraEKEAEKEAALLQLREQLEgERKEAV------- 641
Cdd:pfam05483 82 KLYKEAEKIKKwkvSIEAELKQKENK-LQENRKIIEAQRKAIQ-----ELQFENEKVSLKLEEEIQ-ENKDLIkennatr 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 642 --AGLEKKHSAELEQLCSSLEAKHQE---VISSLQKKIEGA--------QQKEEAQLQESLGWAEQraHQKVHQVteyEQ 708
Cdd:pfam05483 155 hlCNLLKETCARSAEKTKKYEYEREEtrqVYMDLNNNIEKMilafeelrVQAENARLEMHFKLKED--HEKIQHL---EE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 709 ELSSLLRDKRQEVER---EHERKMDKMKE-----EHWQEMADARE---RYEAEERKQRADLLGHLTGELERLRRAHEREL 777
Cdd:pfam05483 230 EYKKEINDKEKQVSLlliQITEKENKMKDltfllEESRDKANQLEektKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 778 ESMR-----------------QEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIrkeKQLLLDA 840
Cdd:pfam05483 310 STQKaleedlqiatkticqltEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL---KIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 841 QRQAAlEREEATATHQH----LEEAKK---EHTHLLETKQQLRRTIDDLRVRRVELesqVDLLQAQSQRLQKHLSSLEAE 913
Cdd:pfam05483 387 QKKSS-ELEEMTKFKNNkeveLEELKKilaEDEKLLDEKKQFEKIAEELKGKEQEL---IFLLQAREKEIHDLEIQLTAI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 914 VQRKQDVLKEMaAEMNASPHPEPGLHIEdlrksLDTNKNQEVSSSLSLSKEEIDLSMESVRQflSAEGVAVRNAKEFLVR 993
Cdd:pfam05483 463 KTSEEHYLKEV-EDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMTLELKKH--QEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 994 QTRSMRRRQTALKAAQQHWRHEL-ASAQEVDEDLPGTEvlGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLES 1072
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSE--ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
....
gi 160420304 1073 SLQE 1076
Cdd:pfam05483 613 LHQE 616
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
443-923 |
3.98e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 443 QEEQDDSKSSIAEPQSKHTQ-GSEREHLQSSLHSQATeegplqtlegqpEWKEAEGpgkdsvaspaplslLQSLLKAQLQ 521
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlCEEKNALQEQLQAETE------------LCAEAEE--------------MRARLAARKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 522 KATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQIRtEQQAALQRL------------REEAETLQKAERASLE 589
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD-EEEAARQKLqlekvtteakikKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 590 QKSRRALEQ----LREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQLcssleakhQE 665
Cdd:pfam01576 151 SKERKLLEEriseFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL--------QE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 666 VISSLQKKIE---GAQQKEEAQLQESLGWAEQRAHQK---VHQVTEYEQELSSLLRDkrQEVEREHERKMDKMKEEHWQE 739
Cdd:pfam01576 223 QIAELQAQIAelrAQLAKKEEELQAALARLEEETAQKnnaLKKIRELEAQISELQED--LESERAARNKAEKQRRDLGEE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 740 MADARERYE---------AEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQ-------QLEDLRRRHRDHERKLQ 803
Cdd:pfam01576 301 LEALKTELEdtldttaaqQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaleelteQLEQAKRNKANLEKAKQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 804 DLEVELSSRTKDVKArLAQLNVQEENIRKEkqllLDAQRQAALEReeatathqhLEEAKKEHTHLLETKQQLRRTIDDLR 883
Cdd:pfam01576 381 ALESENAELQAELRT-LQQAKQDSEHKRKK----LEGQLQELQAR---------LSESERQRAELAEKLSKLQSELESVS 446
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 160420304 884 VRRVELESqvdllqaQSQRLQKHLSSLEAEVQRKQDVLKE 923
Cdd:pfam01576 447 SLLNEAEG-------KNIKLSKDVSSLESQLQDTQELLQE 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
640-853 |
6.29e-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: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 640 AVAGLEKKHSAELEQLcssleakhQEVISSLQKKIEgAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSL------ 713
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaelae 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 714 LRDKRQEVEREHERKMDKMKE--------------------EHWQEMADARERYEA--EERKQRADLLGHLTGELERLRR 771
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAEllralyrlgrqpplalllspEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 772 aherELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEA 851
Cdd:COG4942 168 ----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 160420304 852 TA 853
Cdd:COG4942 244 PA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
667-914 |
6.99e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 667 ISSLQKKIEGAQQKEEA--QLQEslgwAEQRAHQKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHwQEMADAR 744
Cdd:COG4913 237 LERAHEALEDAREQIELlePIRE----LAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL-ARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 745 ERYEAEERKQRADLLghltgELERLRRAHE-RELESMRQEQDQ---QLEDLRRRHRDHERKLQDLEVELSSRTKDVKARL 820
Cdd:COG4913 312 ERLEARLDALREELD-----ELEAQIRGNGgDRLEQLEREIERlerELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 821 AQLnvqeenirkeKQLLLDAQRQAALEREEATATHQHLEEAKKEHthlletkQQLRRTIDDLRVRRVELESQVDLLQAqs 900
Cdd:COG4913 387 AEA----------AALLEALEEELEALEEALAEAEAALRDLRREL-------RELEAEIASLERRKSNIPARLLALRD-- 447
|
250
....*....|....
gi 160420304 901 qRLQKHLSSLEAEV 914
Cdd:COG4913 448 -ALAEALGLDEAEL 460
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
444-1086 |
9.46e-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: 53.43 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 444 EEQDDSKSSIAEPQSKHTQGSEREHLQSSLHSQATEEGPLQTLEgqPEWKEAEgPGKDSVASPAPLSLLQsllKAQLQKA 523
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQE--AVLEETQ-ERINRARKAAPLAAHI---KAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 524 TAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEQ-QAALQRLREEAETlQKAERASLEQKS--RRALEQLR 600
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlHSQEIHIRDAHEV-ATSIREISCQQHtlTQHIHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 601 EQLEAEERSAQAAlraekeaekEAALLQLREQlegerkeaVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQK 680
Cdd:TIGR00618 386 QQKTTLTQKLQSL---------CKELDILQRE--------QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 681 EEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRdKRQEVEREHERKMDKMKEEhwQEMADARERYEAEERKQrADLLG 760
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL-QETRKKAVVLARLLELQEE--PCPLCGSCIHPNPARQD-IDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 761 HLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHER--KLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLL 838
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 839 DAQRQAALEreeatathQHLEEAKKEHT-HLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAE--VQ 915
Cdd:TIGR00618 605 EAEDMLACE--------QHALLRKLQPEqDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKelLA 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 916 RKQDVLKEMAAEMNASPHPEPGL-HIEDLRKSLDTnknqeVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAkeflvrQ 994
Cdd:TIGR00618 677 SRQLALQKMQSEKEQLTYWKEMLaQCQTLLRELET-----HIEEYDREFNEIENASSSLGSDLAAREDALNQS------L 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 995 TRSMRRRQTALKAaqQHWRHELASAQEVDEDLPGTEV------LGNMRKNLNEETRHLDEMKSAMRK----GHDLLKKKE 1064
Cdd:TIGR00618 746 KELMHQARTVLKA--RTEAHFNNNEEVTAALQTGAELshlaaeIQFFNRLREEDTHLLKTLEAEIGQeipsDEDILNLQC 823
|
650 660
....*....|....*....|..
gi 160420304 1065 EKLIQLESSLQEEVSDEDTLKG 1086
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLG 845
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
548-827 |
9.54e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRT-----EQQAALQRLREEAETLQK---AERASLEQKSRRAlEQLREQL-----EAEERSAQAAl 614
Cdd:PRK02224 484 LEDLEEEVEEVEERLERaedlvEAEDRIERLEERREDLEEliaERRETIEEKRERA-EELRERAaeleaEAEEKREAAA- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 615 raekeaekeaallQLREQLEGERkEAVAGLEKKhsaeLEQLCSSLEAkhQEVISSLQKKIEgaqqkeeaqlqeslgwaeq 694
Cdd:PRK02224 562 -------------EAEEEAEEAR-EEVAELNSK----LAELKERIES--LERIRTLLAAIA------------------- 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 695 rahqkvhqvtEYEQELSSlLRDKRQEV-EREHERKmDKMKE--EHWQEMADA--RERYE-AEERKQRA-DLLGHLTGELE 767
Cdd:PRK02224 603 ----------DAEDEIER-LREKREALaELNDERR-ERLAEkrERKRELEAEfdEARIEeAREDKERAeEYLEQVEEKLD 670
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 768 RLrRAHERELES---MRQEQDQQLEDLRRRHRDHERKLQDLEV------ELSSRTKDVKARLAQLNVQE 827
Cdd:PRK02224 671 EL-REERDDLQAeigAVENELEELEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQRNVET 738
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
565-820 |
1.42e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGL 644
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 645 EK--KHSAELEQLcssLEAKHQEvisslqkkiegaqQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELssLLRDKRQEVE 722
Cdd:pfam13868 194 EKaqDEKAERDEL---RAKLYQE-------------EQERKERQKEREEAEKKARQRQELQQAREEQI--ELKERRLAEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 723 REHERKMDKMKEEHWQEMaDARERYEAEERKQRadllghltgelerlRRAHERELESMRQEQDQQLEDLRRRHRDHERKL 802
Cdd:pfam13868 256 AEREEEEFERMLRKQAED-EEIEQEEAEKRRMK--------------RLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
250
....*....|....*...
gi 160420304 803 QDLEVELSSRTKDVKARL 820
Cdd:pfam13868 321 REEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
840-1067 |
1.56e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 840 AQRQAALE--REEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRK 917
Cdd:COG4942 23 AEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 918 QDVLKEMAAE---MNASPHPEPGLHIEDlrkSLDTNKNQEVssslslskeeidlsMESVRQFLSAEGVAVRNAKEFLVRQ 994
Cdd:COG4942 103 KEELAELLRAlyrLGRQPPLALLLSPED---FLDAVRRLQY--------------LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160420304 995 TRS---MRRRQTALKAAQQHWRHELASAQEVDEDLpgtevLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKL 1067
Cdd:COG4942 166 RAEleaERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
665-944 |
1.99e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.27 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 665 EVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSsllrdkrqEVEREHERKMDKMKEEHWQEMADAR 744
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELE--------ESKRETETGIQNLTAEIEQGQESLT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 745 ERYEAEeRKQRADLLGhltgeLERLRRAhERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLN 824
Cdd:COG5185 354 ENLEAI-KEEIENIVG-----EVELSKS-SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 825 VQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLlETKQQLRRTIDDLRVRRVELESQVDLLQAQsqrLQ 904
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD-EINRSVRSKKEDLNEELTQIESRVSTLKAT---LE 502
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 160420304 905 KHLSSLEAEVQRKQDVLKEMAAEMNASPHPEPGLHIEDLR 944
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
652-1092 |
2.13e-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: 52.33 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 652 LEQLCSSLEAKHQEvISSLQKKIEGAQQKEEaQLQESLGWAEQRAHQKVHQVTEYEQELSSLLrDKRQEVEREHERKMdk 731
Cdd:TIGR04523 199 LELLLSNLKKKIQK-NKSLESQISELKKQNN-QLKDNIEKKQQEINEKTTEISNTQTQLNQLK-DEQNKIKKQLSEKQ-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 732 mkeehwqemadareryeaEERKQRADLLGHLTGELERLrrahERELESMRQEQDQQL-EDLRRRHRDHERKLQDLEVELS 810
Cdd:TIGR04523 274 ------------------KELEQNNKKIKELEKQLNQL----KSEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQIS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 811 SRTKdvkaRLAQLNVQEENIRKEKQlllDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELE 890
Cdd:TIGR04523 332 QNNK----IISQLNEQISQLKKELT---NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 891 SQVDLLQAQSQRLQKHLSSLEAEVQRkqdvLKEMAAEMNASphpepglhIEDLRKSlDTNKNQEVssslslskEEIDLSM 970
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNSE--------IKDLTNQ-DSVKELII--------KNLDNTR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 971 ESVRQFLSAegvavrnakeflvrQTRSMRRRQTALKAAQQhwrhELASAQevdedlpgtevlgNMRKNLNEETRHLDEMK 1050
Cdd:TIGR04523 464 ESLETQLKV--------------LSRSINKIKQNLEQKQK----ELKSKE-------------KELKKLNEEKKELEEKV 512
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 160420304 1051 SAMRKGHDLLKKKEEKL------IQLE-SSLQEEV-SDEDTLKGSSIKKV 1092
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLesekkeKESKiSDLEDELnKDDFELKKENLEKE 562
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
565-864 |
2.47e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEgERKEAVAGL 644
Cdd:pfam13868 44 RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE-DQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 645 EKKhsaeleqlcsslEAKHQEVISSLQKKIEGAQQKEEAQLQEslgwaEQRAHQKVHQVTEYEQElsslLRDKRQEVERE 724
Cdd:pfam13868 123 EKQ------------RQLREEIDEFNEEQAEWKELEKEEEREE-----DERILEYLKEKAEREEE----REAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 725 HERKMDKMKEEHWQEMADARERYEAeerkqRADLLghltgELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQD 804
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDEL-----RAKLY-----QEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 805 LEVElssRTKDVKARLAQLNVQEENIRKEKQlllDAQRQAALEREEATATHQHLEEAKKE 864
Cdd:pfam13868 252 LAEE---AEREEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQ 305
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
668-864 |
3.03e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 668 SSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELssllrdkRQEVEREHERKMDKMKeehwqemadarery 747
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL-------RNEFEKELRERRNELQ-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 748 EAEER-KQRADLLGHltgELERLRRAhERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSsrtkdvkaRLAQLNVQ 826
Cdd:PRK12704 86 KLEKRlLQKEENLDR---KLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE--------RISGLTAE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 160420304 827 EenirkEKQLLLDAQRQAAleREEATAT-HQHLEEAKKE 864
Cdd:PRK12704 154 E-----AKEILLEKVEEEA--RHEAAVLiKEIEEEAKEE 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
738-926 |
4.11e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 738 QEMADARERYEAEERKQRAD-LLGHLTGELERLR---RAHERELESMRQEQDqqLEDLRRRHRDHERKLQDLEVELS--- 810
Cdd:COG3206 155 NALAEAYLEQNLELRREEARkALEFLEEQLPELRkelEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAear 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 811 SRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKK---EHTHLLETKQQLRRTIDDLRVR-- 885
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQLQQEaq 312
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 160420304 886 --RVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAA 926
Cdd:COG3206 313 riLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
556-1076 |
4.47e-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: 51.59 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 556 EAFENQIRT--EQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEkeaalLQLREQL 633
Cdd:TIGR00606 305 DLYHNHQRTvrEKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-----LATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 634 EGERKEAVAGLEKKHSAEL------------EQLCSSLEAKH---QEVISSLQKKIEGAQ----------QKEEAQLQES 688
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLvierqedeaktaAQLCADLQSKErlkQEQADEIRDEKKGLGrtielkkeilEKKQEELKFV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 689 LgWAEQRAHQKVHQVTEYEQELSSLLRD------------KRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRA 756
Cdd:TIGR00606 460 I-KELQQLEGSSDRILELDQELRKAERElskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 757 DLLGHLTGELERLRRAHER----------------ELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARL 820
Cdd:TIGR00606 539 MLTKDKMDKDEQIRKIKSRhsdeltsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 821 AQLNVQEENI-------------RKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTiddlrvrRV 887
Cdd:TIGR00606 619 EQLSSYEDKLfdvcgsqdeesdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT-------EA 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 888 ELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEM--AAEMNASPHPEPGLHIEDLRksldtNKNQEVSSSLSLSKEE 965
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlgLAPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKND 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 966 IDLSMESVRQFLSAEGVAvrnakEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTEVlgnmRKNLNEETRH 1045
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESA-----KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQV----NQEKQEKQHE 837
|
570 580 590
....*....|....*....|....*....|.
gi 160420304 1046 LDEMKSAMRKGHDLLKKKEEKLIQLESSLQE 1076
Cdd:TIGR00606 838 LDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
563-919 |
4.52e-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: 51.33 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 563 RTEQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVA 642
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 643 GLEKKHSAELEQLCSSL------EAKHQEVISSLQKKIEGAQ-------------QKE----EAQLQESLGWAEQRAHQK 699
Cdd:pfam01576 405 HKRKKLEGQLQELQARLseserqRAELAEKLSKLQSELESVSsllneaegkniklSKDvsslESQLQDTQELLQEETRQK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 700 V---HQVTEYEQELSSLLrdKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRAdllghltgeLERLRRAHERE 776
Cdd:pfam01576 485 LnlsTRLRQLEDERNSLQ--EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA---------LEEGKKRLQRE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 777 LESMRQ---EQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKA------RLAQLNVQEENIRKEKQLLLDAQRQAALE 847
Cdd:pfam01576 554 LEALTQqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNlekkqkKFDQMLAEEKAISARYAEERDRAEAEARE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 848 RE-EATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRR-------VELESQVDLLQAQSQRLQKHLSSLEAEVQRKQD 919
Cdd:pfam01576 634 KEtRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddvgknvHELERSKRALEQQVEEMKTQLEELEDELQATED 713
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
565-924 |
5.13e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.13 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERsaqaalraekeaeKEAALLQLREQLEGERKEAVAGL 644
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-------------LIIDLEELKLQELKLKEQAKKAL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 645 E------KKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAH-QKVHQVTEYEQELSSLLRDK 717
Cdd:pfam02463 211 EyyqlkeKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQvLKENKEEEKEKKLQEEELKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 718 RQEVEREHERKMDKMKEehwQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRD 797
Cdd:pfam02463 291 LAKEEEELKSELLKLER---RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 798 HERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQ---- 873
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgklt 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 160420304 874 QLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEM 924
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
584-892 |
6.13e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 584 ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEaallqlreqlegERKEAVAGLEKKHSAELEQLCSSLEAKH 663
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNS------------YEEDSELKPSGQGGLDEEEAFLDRTAKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 664 QE-VISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQEVErEHERKMDKMKEEHW-QEMA 741
Cdd:pfam02029 72 EErRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWsTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 742 DARERYEAEERKQRADllghlTGELERLRRAHERELESMRQEQDQQLED---LRRRHRDHERKLQDLEVELSSRTKDVKA 818
Cdd:pfam02029 151 QAEEEGEEEEDKSEEA-----EEVPTENFAKEEVKDEKIKKEKKVKYESkvfLDQKRGHPEVKSQNGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 819 RLAQLNV-----QEENIRKEKQLLLDAQRQ--AALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELES 891
Cdd:pfam02029 226 RQGGLSQsqereEEAEVFLEAEQKLEELRRrrQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEA 305
|
.
gi 160420304 892 Q 892
Cdd:pfam02029 306 E 306
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
590-856 |
6.70e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 590 QKSRRALEQLREQLEAEERSAQAAlraekeAEKEAALLQLREQLEgERKEAVAGLEKKHSAELEQlcssleAKHQEVISS 669
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEA------EERLEALEAELDALQ-ERREALQRLAEYSWDEIDV------ASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 670 LQKKIEGAQQ--KEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSlLRDKRQEVEREHERKMDkmKEEHWQEMADARERY 747
Cdd:COG4913 673 LEAELERLDAssDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQD--RLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 748 EAEERKQRADLLGHltgeLERLRRAHERELESMRQEQDQQLEDLRRRHRDHERK----LQDLEVELSSRTkDVKARLAQL 823
Cdd:COG4913 750 LLEERFAAALGDAV----ERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLP-EYLALLDRL 824
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 160420304 824 nVQEENIRKE---KQLLLDAQRQ------AALEREEATATHQ 856
Cdd:COG4913 825 -EEDGLPEYEerfKELLNENSIEfvadllSKLRRAIREIKER 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
550-912 |
8.44e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 550 QVQSRTEAFENQIRT--EQQAALQRLREEAETLQK--AERASLEQKSRRaLEQLREQLEAEERSAQAalRAEKEAEKEAA 625
Cdd:PRK03918 263 ELEERIEELKKEIEEleEKVKELKELKEKAEEYIKlsEFYEEYLDELRE-IEKRLSRLEEEINGIEE--RIKELEEKEER 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 626 LLQLREQLEGERKEaVAGLEKKHS---------AELEQLCSSLEAKHQEVISSLQKKIEGAQ---QKEEAQLQESLGWAE 693
Cdd:PRK03918 340 LEELKKKLKELEKR-LEELEERHElyeeakakkEELERLKKRLTGLTPEKLEKELEELEKAKeeiEEEISKITARIGELK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 694 QRAHQKVHQVTEYE----------QELSSllrDKRQEVEREHERKMDKMKEEhWQEMADARERYEAEERKQRADLLGHlt 763
Cdd:PRK03918 419 KEIKELKKAIEELKkakgkcpvcgRELTE---EHRKELLEEYTAELKRIEKE-LKEIEEKERKLRKELRELEKVLKKE-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 764 GELERLRRAHE--RELESMRQEQDqqLEDLRRRHRDHE---RKLQDLEVELSS------RTKDVKARLAQLNVQEENIRK 832
Cdd:PRK03918 493 SELIKLKELAEqlKELEEKLKKYN--LEELEKKAEEYEklkEKLIKLKGEIKSlkkeleKLEELKKKLAELEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 833 EKQLLLDAQRQAALER-EEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLE 911
Cdd:PRK03918 571 ELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
.
gi 160420304 912 A 912
Cdd:PRK03918 651 E 651
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
9.93e-06 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 43.26 E-value: 9.93e-06
10 20 30
....*....|....*....|....*....|
gi 160420304 58 LPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
543-910 |
1.13e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 543 RLVCLRAQVQSRTEAFENQIRTEQQAALQRLREEAetlqkAERASLEQKSRRALEQLREQLEAEERSAQAALRAekeaek 622
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLE-----AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV------ 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 623 eaallqlreqLEGERKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKK-IEGAQQKEEAQLQESLGWAEQRAHQKVH 701
Cdd:pfam12128 723 ----------VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQ 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 702 QVTEYE---QELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEER------KQRADLLGHLTG---ELERL 769
Cdd:pfam12128 793 EVLRYFdwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaseKQQVRLSENLRGlrcEMSKL 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 770 RRAHE----RELESMRQEQDQQLEDLRRRHR----DHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQ 841
Cdd:pfam12128 873 ATLKEdansEQAQGSIGERLAQLEDLKLKRDylseSVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLDY 952
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160420304 842 RQAALEREE-ATATHQHLEEAKKEHTHLL-ETKQQLRRTIDDLRVRrvelesqvdlLQAQSQRLQKHLSSL 910
Cdd:pfam12128 953 RKLVPYLEQwFDVRVPQSIMVLREQVSILgVDLTEFYDVLADFDRR----------IASFSRELQREVGEE 1013
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
741-931 |
1.18e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 741 ADARERYEAEERKQRADLLGHLTGELERLrrahERELESMRQEQDQ---QLEDLRRRHRDHERKLQDLEVELSSRTKDVK 817
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 818 ARLAQLNVQEENIRKEKQLLLDAQRQAALEREEA-----TATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQ 892
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSDFLDRLSAlskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 160420304 893 VDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNAS 931
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
774-1085 |
1.42e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 774 ERELESMRQEQDQQLEDLRRRhrdherkLQDLEVELSS----------RTKDVKARLAQLNVQEENIRKEKQLLLDAQRQ 843
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRER-------LEGLKRELSSlqselrrienRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 844 AALE----REEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESqvDLLQAQSQRLQKHLSSLEAEVQRKQD 919
Cdd:TIGR02169 735 LKERleelEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 920 VLKEMAAEMNASpHPEPGL------HIEDLRKSLDTNKN--QEVSSSLSLSKEEIDLSMESVRQF---LSAEGVAVRNAK 988
Cdd:TIGR02169 813 RLREIEQKLNRL-TLEKEYlekeiqELQEQRIDLKEQIKsiEKEIENLNGKKEELEEELEELEAAlrdLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 989 EFLVRQTRSMRRRQTALKAAQQHWRH---------------------ELASAQEVDEDLPGTEVLGNMRKNLNEETRHL- 1046
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKrlselkaklealeeelseiedPKGEDEEIPEEELSLEDVQAELQRVEEEIRALe 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 160420304 1047 -------DEMKSAMRKgHDLLKKKEEKLIQLESSLQEEVSDEDTLK 1085
Cdd:TIGR02169 972 pvnmlaiQEYEEVLKR-LDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
561-996 |
1.86e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 561 QIRTEQQAALQRLREEAETLQ------KAERASLEQKSRRALEQLrEQLEAEERSAQAALRAEKEAEKEAALLQLREQLE 634
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSfvvtefEATTCSLEELLRTEQQRL-EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 635 GERKEAVAGLEKK---HSAELEQLCSSLEAKHQEVISSLQkkiegAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELS 711
Cdd:pfam05483 407 LEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQ-----AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 712 sllRDKRQEVE-REHERKMDKMKEEHWQEMADARERYEAEE------RKQRADLLGHLTgELERLRRAHERELESMRQEQ 784
Cdd:pfam05483 482 ---KEKLKNIElTAHCDKLLLENKELTQEASDMTLELKKHQediincKKQEERMLKQIE-NLEEKEMNLRDELESVREEF 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 785 DQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLE----E 860
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeiK 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 861 AKKEHTHLLETKQQL-------RRTIDDLRVRRVELESQVDLLQA---QSQRLQKHLSsleaevQRKQDVLKEMAAEMNA 930
Cdd:pfam05483 638 VNKLELELASAKQKFeeiidnyQKEIEDKKISEEKLLEEVEKAKAiadEAVKLQKEID------KRCQHKIAEMVALMEK 711
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160420304 931 SPHPEPGLhIEDLRKSLDTNKNQEVSSSLSLSKEEIDLS-----MESVRQFLSAEgvavRNAKEFLVRQTR 996
Cdd:pfam05483 712 HKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELSnikaeLLSLKKQLEIE----KEEKEKLKMEAK 777
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
657-931 |
1.87e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 657 SSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAhQKVHQVTEYEQELSSLLRDKRQEVEREHERKmdKMKEEH 736
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRD-ELNAQVKELREEAQELREKRDELNEKVKELK--EERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 737 WQEMADAREryEAEERKQRADLLGHLTGELERLRRAHERElesmrqEQDQQLEDLRRrhrDHERKLQDLEVELSSRTKDV 816
Cdd:COG1340 84 NEKLNELRE--ELDELRKELAELNKAGGSIDKLRKEIERL------EWRQQTEVLSP---EEEKELVEKIKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 817 KArlaqlnvqeenIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLL 896
Cdd:COG1340 153 KK-----------ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA 221
|
250 260 270
....*....|....*....|....*....|....*
gi 160420304 897 QAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNAS 931
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
636-1068 |
2.59e-05 |
|
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: 48.66 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 636 ERKEAVAGLE--KKHS----AELEQLCSSLEAKHQEVISsLQKKIE--GAQQKEEAQ----LQESLGWAEQRA---HQKV 700
Cdd:pfam10174 269 DREEEIKQMEvyKSHSkfmkNKIDQLKQELSKKESELLA-LQTKLEtlTNQNSDCKQhievLKESLTAKEQRAailQTEV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 701 HQVTEYEQELSSLLRDKRQEVEREHERKMDKMKE-EHWQEMADARERYEAEERKQRADLLGHLT---GELERLRRAHER- 775
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQLRdkdKQLAGLKERVKSl 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 776 ------------ELESMRQEQDQQLEDLRRRHRDHERKLQDlevELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQ 843
Cdd:pfam10174 428 qtdssntdtaltTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 844 AALEREEATATHQHLE------EAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRK 917
Cdd:pfam10174 505 ASSLASSGLKKDSKLKsleiavEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 918 QDVLKEMAAEMNASPHPEPGLHIEDLRKSLDTNKnqevssslslskeeidlsmeSVRQFLSAEGVAVRNAKEFLVRQtrs 997
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAELESLTLRQMKEQNK--------------------KVANIKHGQQEMKKKGAQLLEEA--- 641
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160420304 998 mRRRQTALKAAQQHWRHE--LASAQEVDEDLPGTEV-LGNMRKNLNEETRHLDEMKSAMRKG-HDLLKKKEEKLI 1068
Cdd:pfam10174 642 -RRREDNLADNSQQLQLEelMGALEKTRQELDATKArLSSTQQSLAEKDGHLTNLRAERRKQlEEILEMKQEALL 715
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
715-928 |
2.60e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 715 RDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRR 794
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 795 HRDHERKLQDL---------EVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEatathQHLEEAKKEH 865
Cdd:pfam13868 111 QEEDQAEAEEKlekqrqlreEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER-----EEIEEEKERE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 866 T----HLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEA--EVQRKQDVLKEMAAEM 928
Cdd:pfam13868 186 IarlrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQElqQAREEQIELKERRLAE 254
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
570-953 |
2.74e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 570 LQRLREEAETLQKAERASLEQ----------------KSRRALEQ----LREQLEAEERSAQAA----LR----AEKEAE 621
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDlvsskddvgknvheleRSKRALEQqveeMKTQLEELEDELQATedakLRlevnMQALKA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 622 KEAALLQLREQLEGERKEAVAGLEKKHSAELEQlcsslEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQ--K 699
Cdd:pfam01576 728 QFERDLQARDEQGEEKRRQLVKQVRELEAELED-----ERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQlkK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 700 VH-QVTEYEQELSSLlRDKRQEV---EREHERKMDKMKEE--HWQEMADARERYEAEERKQRADLlghltgelerlrrah 773
Cdd:pfam01576 803 LQaQMKDLQRELEEA-RASRDEIlaqSKESEKKLKNLEAEllQLQEDLAASERARRQAQQERDEL--------------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 774 ERELESMRQEQDQQLEDLRRRhrdhERKLQDLEVELSSrtkdvkarlAQLNVQEENIRKEKQLLLDAQRQAALEREEATA 853
Cdd:pfam01576 867 ADEIASGASGKSALQDEKRRL----EARIAQLEEELEE---------EQSNTELLNDRLRKSTLQVEQLTTELAAERSTS 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 854 thQHLEEAKkehthlletkQQLRRTIDDLRVRRVELESQVdllqaqSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNASPH 933
Cdd:pfam01576 934 --QKSESAR----------QQLERQNKELKAKLQEMEGTV------KSKFKSSIAALEAKIAQLEEQLEQESRERQAANK 995
|
410 420
....*....|....*....|....*....
gi 160420304 934 ---------PEPGLHIEDLRKSLDTNKNQ 953
Cdd:pfam01576 996 lvrrtekklKEVLLQVEDERRHADQYKDQ 1024
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
693-920 |
3.01e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 693 EQRAHQKVHQVTEYEQELSSLLRDKRQEVErEHERKMDKMKEEHW----QEMADARERYEAEERKQRADLLGHLTgELER 768
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQLAEARAELA-EAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 769 LRRAHERELESMRQE-----QDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLL---DA 840
Cdd:COG3206 241 RLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaslEA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 841 QRQAALEREEATAthQHLEEAKKEHTHLLETKQQLRRtiddlrvrrveLESQVDLLQAQSQRLQKHLSslEAEVQRKQDV 920
Cdd:COG3206 321 ELEALQAREASLQ--AQLAQLEARLAELPELEAELRR-----------LEREVEVARELYESLLQRLE--EARLAEALTV 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
591-926 |
3.19e-05 |
|
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: 48.80 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 591 KSRRALEQLREQLEAEERSAQAALRaekeaekeaaLLQLREQLEgERKEAVAGLEKKHSAELEQLCSSLEA-KHQEVISS 669
Cdd:COG3096 283 LSERALELRRELFGARRQLAEEQYR----------LVEMARELE-ELSARESDLEQDYQAASDHLNLVQTAlRQQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 670 LQKKIEGAQQKEEAQLQESLGWAEQRAHQKVhQVTEYEQELSSL---LRDKRQEVEREHERKMdkmkeeHWQEMADARER 746
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEA-RLEAAEEEVDSLksqLADYQQALDVQQTRAI------QYQQAVQALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 747 yeAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEV---ELSSRTKDVKARlaql 823
Cdd:COG3096 425 --ARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagEVERSQAWQTAR---- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 824 nvqeENIRKEKQLLLDAQRQAALEREEATAtHQHLEEAKKEHTHLLETKQQLRRTI---DDLRVRRVELESQVDLLQAQS 900
Cdd:COG3096 499 ----ELLRRYRSQQALAQRLQQLRAQLAEL-EQRLRQQQNAERLLEEFCQRIGQQLdaaEELEELLAELEAQLEELEEQA 573
|
330 340
....*....|....*....|....*.
gi 160420304 901 QRLQKHLSSLEAEVQRKQDVLKEMAA 926
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
553-1072 |
3.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 553 SRTEAFENQIRTEQQAALQRLRE----EAETLQKAERASLEQKSRRALEQLREQLEAEERsaQAALRAEKEAEKEAALLQ 628
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREineiSSELPELREELEKLEKEVKELEELKEEIEELEK--ELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 629 LREQLEGERKEaVAGLEKKhSAELEQLcsSLEAKHQEVISSLQKKIEgaqqKEEAQLQESLGWAEQRAHQKVHQVTEYEQ 708
Cdd:PRK03918 264 LEERIEELKKE-IEELEEK-VKELKEL--KEKAEEYIKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 709 ELSSL--LRDKRQEVEREHERKmdKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHE------RELESM 780
Cdd:PRK03918 336 KEERLeeLKKKLKELEKRLEEL--EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEeieeeiSKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 781 RQEQDQQLEDLR-----------------RRHRDHERKlqDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLldaqRQ 843
Cdd:PRK03918 414 IGELKKEIKELKkaieelkkakgkcpvcgRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELREL----EK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 844 AALEREEATATHQHLEEAKkehthllETKQQLRR-TIDDLRVRRVELEsqvdLLQAQSQRLQKHLSSLEAEVQRKQDVLK 922
Cdd:PRK03918 488 VLKKESELIKLKELAEQLK-------ELEEKLKKyNLEELEKKAEEYE----KLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 923 EMAAEMNAsphpepglhIEDLRKSLdTNKNQEVSSSLSLSKEEIDLSMESVRQFLSaEGVAVRNAKEFLVRQTRSMRRRQ 1002
Cdd:PRK03918 557 KLAELEKK---------LDELEEEL-AELLKELEELGFESVEELEERLKELEPFYN-EYLELKDAEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 1003 TALKAAQQHWRHELASAQEVDEDLPGTEV--------------------LGNMRKNLNEETRHLDEMKSAMRKGHDLLKK 1062
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKkyseeeyeelreeylelsreLAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
570
....*....|
gi 160420304 1063 KEEKLIQLES 1072
Cdd:PRK03918 706 REKAKKELEK 715
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
3.66e-05 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 41.74 E-value: 3.66e-05
10 20 30
....*....|....*....|....*....|.
gi 160420304 59 PKGWKPCQNITGDLYYFNFDTGQSIWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
767-931 |
3.83e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.21 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 767 ERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKdvKARLAqLNVQEENIRKEKqllldAQRQAAL 846
Cdd:pfam04012 24 EKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE--KAQAA-LTKGNEELAREA-----LAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 847 EreeatathQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQA--QSQRLQKHL---------SSLEAEVQ 915
Cdd:pfam04012 96 E--------KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKArlKAAKAQEAVqtslgslstSSATDSFE 167
|
170
....*....|....*.
gi 160420304 916 RKQDVLKEMAAEMNAS 931
Cdd:pfam04012 168 RIEEKIEEREARADAA 183
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
677-953 |
3.86e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 677 AQQKEEAQLQESLGWAE--QRAHQKvhQVTEYEQELSSLLRDKRQEVEREheRKMDKMKEEHWQEMADARERYEAEERKQ 754
Cdd:PRK10929 20 ATAPDEKQITQELEQAKaaKTPAQA--EIVEALQSALNWLEERKGSLERA--KQYQQVIDNFPKLSAELRQQLNNERDEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 755 RADLLGHLTGELE-RLRRAHERELESMR---QEQD-------------QQLEDLRRRHRDHERKLQDLEvelSSRTKDVK 817
Cdd:PRK10929 96 RSVPPNMSTDALEqEILQVSSQLLEKSRqaqQEQDrareisdslsqlpQQQTEARRQLNEIERRLQTLG---TPNTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 818 ARLAQLNVqEENIRKEKQLLLDAQRQAALEREEATatHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVE--LESqVDL 895
Cdd:PRK10929 173 AQLTALQA-ESAALKALVDELELAQLSANNRQELA--RLRSELAKKRSQQLDAYLQALRNQLNSQRQREAEraLES-TEL 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160420304 896 LQAQSQRLQKHLSSlEAEVQRK-QDVLKEMAAEMN--ASPHPEPGLHIEDLRKSLDTNKNQ 953
Cdd:PRK10929 249 LAEQSGDLPKSIVA-QFKINRElSQALNQQAQRMDliASQQRQAASQTLQVRQALNTLREQ 308
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
560-848 |
3.93e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 560 NQIRTEQQAALQRLREEaetlqkaeraslEQKSRRALEQLREQLEAEERSA-QAALraEKEAEKEAALLQLREQLEgERK 638
Cdd:PRK04863 843 NRRRVELERALADHESQ------------EQQQRSQLEQAKEGLSALNRLLpRLNL--LADETLADRVEEIREQLD-EAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 639 EAVAGLEK--KHSAELEQLCSSLEAKHQEvISSLQKKIEGAQQKEEAQLQESLGWAE---QRAH---QKVHQVTEYEQEL 710
Cdd:PRK04863 908 EAKRFVQQhgNALAQLEPIVSVLQSDPEQ-FEQLKQDYQQAQQTQRDAKQQAFALTEvvqRRAHfsyEDAAEMLAKNSDL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 711 SSLLRDKRQEVEREHERKMDKMKE------EHWQEMADARERYEA-----EERKQRADLLG-HLTGELERLRRAHERELe 778
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQLRQaqaqlaQYNQVLASLKSSYDAkrqmlQELKQELQDLGvPADSGAEERARARRDEL- 1065
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160420304 779 smrqeqDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKA---RLAQLNVQEENIRKEKQLLLDAQRQAALER 848
Cdd:PRK04863 1066 ------HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKlerDYHEMREQVVNAKAGWCAVLRLVKDNGVER 1132
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
694-930 |
4.21e-05 |
|
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: 48.41 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 694 QRAHQKVHQ-VTEY---------EQELSsLLRDKRQEVEREHERkmdkmkeehwQEMADARERYEAEERKQRADLLGHLT 763
Cdd:COG3096 812 QRLHQAFSQfVGGHlavafapdpEAELA-ALRQRRSELERELAQ----------HRAQEQQLRQQLDQLKEQLQLLNKLL 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 764 GELERLRRA-HERELESMRQEQDQQLEDLR--RRHRDHERKLQDLEVELSSRTKD---VKARLAQLNVQEENIRKEKQLL 837
Cdd:COG3096 881 PQANLLADEtLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFAL 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 838 LD-AQRQAALEREEATathQHLEEAKKEHTHLletKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAevqr 916
Cdd:COG3096 961 SEvVQRRPHFSYEDAV---GLLGENSDLNEKL---RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA---- 1030
|
250
....*....|....
gi 160420304 917 KQDVLKEMAAEMNA 930
Cdd:COG3096 1031 KQQTLQELEQELEE 1044
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
576-925 |
5.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 576 EAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQ 654
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDdLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 655 LCSSLEAKHQEV---ISSLQKKIEGAQQKEEaQLQESLGWAEQR----------AHQKVHQVTEYEQELSSLLRDKRQEV 721
Cdd:PRK01156 410 ELNEINVKLQDIsskVSSLNQRIRALRENLD-ELSRNMEMLNGQsvcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREI 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 722 ERE----HERKMDKMKEEHWQEMADAReRYEAEERK---QRADLlGHLTGELERLRRAHERELESMRQEQDQQLEDLRRR 794
Cdd:PRK01156 489 EIEvkdiDEKIVDLKKRKEYLESEEIN-KSINEYNKiesARADL-EDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 795 HRDH-----ERKLQDLEV------ELSSRTKDVKARLAQLNVQ--------EENIRK----------------EKQLLLD 839
Cdd:PRK01156 567 RTSWlnalaVISLIDIETnrsrsnEIKKQLNDLESRLQEIEIGfpddksyiDKSIREieneannlnnkyneiqENKILIE 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 840 AQRQAALEREEATATHQHLEEAKKEHT-HLLETK---QQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQ 915
Cdd:PRK01156 647 KLRGKIDNYKKQIAEIDSIIPDLKEITsRINDIEdnlKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLE 726
|
410
....*....|
gi 160420304 916 RKQDVLKEMA 925
Cdd:PRK01156 727 SMKKIKKAIG 736
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
549-828 |
5.07e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.83 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 549 AQVQSRTEAFENQIRTEQQAALQRLREEAETLQKA---ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE-- 623
Cdd:pfam09731 142 ESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISrekATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPEtp 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 624 ----AALLQLREQLEGERKEA--VAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAH 697
Cdd:pfam09731 222 pklpEHLDNVEEKVEKAQSLAklVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLSK 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 698 QKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHEREL 777
Cdd:pfam09731 302 KLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHL 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 160420304 778 ESMRQEQDQQLEdlrrrhRDHERKLQD-LEVELSSRTKDVKARLAQLNVQEE 828
Cdd:pfam09731 382 KDVLVEQEIELQ------REFLQDIKEkVEEERAGRLLKLNELLANLKGLEK 427
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
548-805 |
8.77e-05 |
|
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: 47.25 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIrTEQQAALQRLREEAETLQK--AERASLEQKSrraLEQLREQLEAEERSAQAALRAEKEAEKEAA 625
Cdd:COG3096 845 RSELERELAQHRAQE-QQLRQQLDQLKEQLQLLNKllPQANLLADET---LADRLEELREELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 626 LLQ-----LR------EQLEGERKEAVAGLE--KKHSAELEQLCSSLEA-----------KHQEVISSLQKKIEGAqqkE 681
Cdd:COG3096 921 QLEplvavLQsdpeqfEQLQADYLQAKEQQRrlKQQIFALSEVVQRRPHfsyedavgllgENSDLNEKLRARLEQA---E 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 682 EAQLQeslgwAEQRAHQKVHQVTEYEQELSSLL--RDKRQEVEREHERKMDKMKeehWQEMADARERyeAEERKQRadll 759
Cdd:COG3096 998 EARRE-----AREQLRQAQAQYSQYNQVLASLKssRDAKQQTLQELEQELEELG---VQADAEAEER--ARIRRDE---- 1063
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 160420304 760 ghLTGELERLrRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDL 805
Cdd:COG3096 1064 --LHEELSQN-RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
658-836 |
1.38e-04 |
|
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: 45.52 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 658 SLEAKHQEVISSLQKKIEGAQQKEE--AQLQESLGW------------AEQRAHQKVHQVTEYEQELSSL--LRDKRQEV 721
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKliASLKEGSGVegldsstaltleLEELRQERDLLREEIQKLRGQIqqLRTELQEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 722 EREHERKMDKMKEEhwqeMADARERYEAEERKqradllghltgelerlRRAHERELESMRQEQDQQLEDLRR-------R 794
Cdd:pfam09787 81 EAQQQEEAESSREQ----LQELEEQLATERSA----------------RREAEAELERLQEELRYLEEELRRskatlqsR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 160420304 795 HRDHERKLQDLEVELSSRT------KDVKARLAQLNvqEENIRKEKQL 836
Cdd:pfam09787 141 IKDREAEIEKLRNQLTSKSqssssqSELENRLHQLT--ETLIQKQTML 186
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
482-885 |
1.58e-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: 46.04 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 482 PLQTLEGQPEWKEAEGPGKDSVASPAPLSLLQSLLKAQLQKATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQ 561
Cdd:pfam07888 2 PLDELVTLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 562 IrTEQQAALQRLREEAETLQKAERAslEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLE----GER 637
Cdd:pfam07888 82 V-AELKEELRQSREKHEELEEKYKE--LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETElermKER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 638 KEAVAGLEKKHSAELEQLCSSLEAKHQEvISSLQKKIEGA------QQKEEAQLQESLGWAEQR---AHQKVHQVTEYEQ 708
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEE-LRSLSKEFQELrnslaqRDTQVLQLQDTITTLTQKlttAHRKEAENEALLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 709 ELSSLlrdkrQEVEREHERKMDKMKEEhWQEMADARERYEAEERKQRADlLGHLTGELERLRRAhereLESMRQEQDQQL 788
Cdd:pfam07888 238 ELRSL-----QERLNASERKVEGLGEE-LSSMAAQRDRTQAELHQARLQ-AAQLTLQLADASLA----LREGRARWAQER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 789 EDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKqlllDAQR-QAALEREEATATHQHLEEAKKEHTH 867
Cdd:pfam07888 307 ETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK----DCNRvQLSESRRELQELKASLRVAQKEKEQ 382
|
410
....*....|....*...
gi 160420304 868 LLETKQQLRRTIDDLRVR 885
Cdd:pfam07888 383 LQAEKQELLEYIRQLEQR 400
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
560-997 |
1.74e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 560 NQIRTEQQAALQRLRE--EAETLQKAERASLEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEAALLQLREQLEGE 636
Cdd:COG5278 82 EEARAEIDELLAELRSltADNPEQQARLDELEALIDQWLAELEQVIALrRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 637 RKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRD 716
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 717 KRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHR 796
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 797 DHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLR 876
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 877 RTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVS 956
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 160420304 957 SSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRS 997
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
560-837 |
1.83e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 560 NQIRTEQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAeersaqaaLRAEKEAEKEAALLQLREQLEgERKE 639
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE--------LEEKLKKYNLEELEKKAEEYE-KLKE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 640 AVAGLEKkhsaELEQLCSSLEaKHQEVISSLqKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSL------ 713
Cdd:PRK03918 533 KLIKLKG----EIKSLKKELE-KLEELKKKL-AELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyle 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 714 LRDKRQEVEREhERKMDKMKEEHWQEMAD-ARERYEAEERKQRADLLGHLTGElERLRRAHER--ELESMRQEQDQQLED 790
Cdd:PRK03918 607 LKDAEKELERE-EKELKKLEEELDKAFEElAETEKRLEELRKELEELEKKYSE-EEYEELREEylELSRELAGLRAELEE 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 160420304 791 LRRRHRDHERKLQDLEVELSSRTK------DVKARLAQLNVQEENIRKEKQLL 837
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKakkeleKLEKALERVEELREKVKKYKALL 737
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
552-675 |
1.89e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 552 QSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEaeERSAQAALRAEKEAEKEAALLQLRE 631
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLD--RKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 160420304 632 QLEgERKEAVAGLEKKHSAELEQLC--SSLEAKhQEVISSLQKKIE 675
Cdd:PRK12704 125 ELE-KKEEELEELIEEQLQELERISglTAEEAK-EILLEKVEEEAR 168
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
766-918 |
2.00e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.01 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 766 LERLRRAHERELESMRQEqDQQLedlrrrhRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRqaa 845
Cdd:smart00787 142 LEGLKEGLDENLEGLKED-YKLL-------MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK--- 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 846 lerEEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDllQAQSQRLQ------KHLSSLEAEVQRKQ 918
Cdd:smart00787 211 ---EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA--EAEKKLEQcrgftfKEIEKLKEQLKLLQ 284
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
2.05e-04 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 39.89 E-value: 2.05e-04
10 20 30
....*....|....*....|....*....|.
gi 160420304 57 PLPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
735-931 |
2.09e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 735 EHWQEMADARERYE-----AEERKQRADLLGHLTGELERLR-RAHErelesmrqeqDQQLEDLRRRHRDHER---KLQDL 805
Cdd:COG0497 162 EAYRAWRALKKELEelradEAERARELDLLRFQLEELEAAAlQPGE----------EEELEEERRRLSNAEKlreALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 806 EVELSSRTKDVKARLAQLNVQEENIRKekqllLDAQRQAALER-EEATAthqHLEEAKKEHTHLLET------------- 871
Cdd:COG0497 232 LEALSGGEGGALDLLGQALRALERLAE-----YDPSLAELAERlESALI---ELEEAASELRRYLDSlefdperleevee 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160420304 872 -KQQLRR-------TIDDLRVRRVELESQVDLLQAQSQRLQKhlssLEAEVQRKQDVLKEMAAEMNAS 931
Cdd:COG0497 304 rLALLRRlarkygvTVEELLAYAEELRAELAELENSDERLEE----LEAELAEAEAELLEAAEKLSAA 367
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
728-1087 |
2.32e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 728 KMDKMKEEhwqemadaRERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEV 807
Cdd:pfam02463 166 RLKRKKKE--------ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 808 ELSSRTKDVKARLAQL--------NVQEENIRKEKQLLLDAQRQAALEREEAtathqhleeakkehtHLLETKQQLRRTI 879
Cdd:pfam02463 238 RIDLLQELLRDEQEEIesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELK---------------LLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 880 DDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAemnasPHPEPGLHIEDLRKSLDTNKNQEvsssl 959
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI-----KREAEEEEEEELEKLQEKLEQLE----- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 960 slskEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRSmrrRQTALKAAQQHWRHELASAQEVDEDLPGTEVLGNMRKNL 1039
Cdd:pfam02463 373 ----EELLAKKKLESERLSSAAKLKEEELELKSEEEKE---AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 160420304 1040 NEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEEVSDEDTLKGS 1087
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
570-1080 |
3.36e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 570 LQRLREEAETLQKAERASLEQKSRRALEQLR-EQLEAEERSAQAALRAEKEAEKEAALLQlREQLEGERKEavagLEKKH 648
Cdd:pfam07111 72 LQELRRLEEEVRLLRETSLQQKMRLEAQAMElDALAVAEKAGQAEAEGLRAALAGAEMVR-KNLEEGSQRE----LEEIQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 649 SAELEQLcSSLEAKHQEVISSLQKKIEGaqqkeeaqLQESLGWAEQRAHQKVHQVTEYEQElSSLLRDKRQEVEREHERK 728
Cdd:pfam07111 147 RLHQEQL-SSLTQAHEEALSSLTSKAEG--------LEKSLNSLETKRAGEAKQLAEAQKE-AELLRKQLSKTQEELEAQ 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 729 ---MDKMKEEHWQEMADARERYEAE-ERKQRADLLGHL---------TGELERLR--------RAHEREL-------ESM 780
Cdd:pfam07111 217 vtlVESLRKYVGEQVPPEVHSQTWElERQELLDTMQHLqedradlqaTVELLQVRvqslthmlALQEEELtrkiqpsDSL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 781 RQEQDQQLEDLRRRHRDH------ERKLQDLevELSSRTKDVKARLAQLNVQEENIRKE----KQLLLDAQRQAALEREE 850
Cdd:pfam07111 297 EPEFPKKCRSLLNRWREKvfalmvQLKAQDL--EHRDSVKQLRGQVAELQEQVTSQSQEqailQRALQDKAAEVEVERMS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 851 ATATHQHLEEA----KKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAA 926
Cdd:pfam07111 375 AKGLQMELSRAqearRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 927 EM-------NASPHPEPGLHIE-DLRKSLdtnknQEVSSSLSLSKEEIDLSMESVRQflsaegvAVRNAKEflvrQTRSM 998
Cdd:pfam07111 455 KValaqlrqESCPPPPPAPPVDaDLSLEL-----EQLREERNRLDAELQLSAHLIQQ-------EVGRARE----QGEAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 999 RRRqtaLKAAQQHWRHELASAQEVDEDLpgTEVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKK-EEKLIQLESSLQEE 1077
Cdd:pfam07111 519 RQQ---LSEVAQQLEQELQRAQESLASV--GQQLEVARQGQQESTEEAASLRQELTQQQEIYGQAlQEKVAEVETRLREQ 593
|
...
gi 160420304 1078 VSD 1080
Cdd:pfam07111 594 LSD 596
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
517-924 |
4.43e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 517 KAQLQKATAEEKEKEEETK--IREEESRRLVCLRAQVQSRTEAFENQIRTEQQAA--LQRLREEAETL--QKAERASLEQ 590
Cdd:pfam01576 121 KLQLEKVTTEAKIKKLEEDilLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAksLSKLKNKHEAMisDLEERLKKEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 591 KSRRALEQLREQLEAEERSAQAALraekeAEKEAALLQLREQL---EGERKEAVAGLEKKHSAELEQLCSSLEAKHQevI 667
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTDLQEQI-----AELQAQIAELRAQLakkEEELQAALARLEEETAQKNNALKKIRELEAQ--I 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 668 SSLQKKIE---GAQQKEEAQ--------------LQESLGwaEQRAHQKVHqvTEYEQELSSLLRDKRQEVeREHERKMD 730
Cdd:pfam01576 274 SELQEDLEserAARNKAEKQrrdlgeelealkteLEDTLD--TTAAQQELR--SKREQEVTELKKALEEET-RSHEAQLQ 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 731 KMKEEHWQEMADARERYEAEER------KQRADLLG---HLTGELERLRRAhERELESMRQEQDQQLEDLRRRHRDHER- 800
Cdd:pfam01576 349 EMRQKHTQALEELTEQLEQAKRnkanleKAKQALESenaELQAELRTLQQA-KQDSEHKRKKLEGQLQELQARLSESERq 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 801 ------KLQDLEVELSSRT--------------KDVKARLAQLN-----VQEENIRK-----------------EKQLLL 838
Cdd:pfam01576 428 raelaeKLSKLQSELESVSsllneaegkniklsKDVSSLESQLQdtqelLQEETRQKlnlstrlrqledernslQEQLEE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 839 DAQRQAALEREEATATHQHLEEAKKEHTHLL------ETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEA 912
Cdd:pfam01576 508 EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGtlealeEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
490
....*....|..
gi 160420304 913 EVQRKQDVLKEM 924
Cdd:pfam01576 588 DLDHQRQLVSNL 599
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
655-927 |
4.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 655 LCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGwAEQRAHQKVhqvteYEQELSSLlrDKRQEVEREHErKMDKMKE 734
Cdd:PRK11281 20 LCLSSAFARAASNGDLPTEADVQAQLDALNKQKLLE-AEDKLVQQD-----LEQTLALL--DKIDRQKEETE-QLKQQLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 735 EHWQEMADARERYEAEERKQRADLLghltgelERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLqdleVELSSRTK 814
Cdd:PRK11281 91 QAPAKLRQAQAELEALKDDNDEETR-------ETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQL----VSLQTQPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 815 DVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKE-HTHLLETKQQLRrtidDLrvrrveLESQV 893
Cdd:PRK11281 160 RAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDlQRKSLEGNTQLQ----DL------LQKQR 229
|
250 260 270
....*....|....*....|....*....|....
gi 160420304 894 DLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAE 927
Cdd:PRK11281 230 DYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQ 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
702-837 |
5.66e-04 |
|
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: 42.99 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 702 QVTEYEQELSSLlRDKRQEVEREHErKMDKMKEEHWQEMADARERYEAEERKQR----ADLLGHLTGELERLRRAHErEL 777
Cdd:COG1579 32 ELAELEDELAAL-EARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGnvrnNKEYEALQKEIESLKRRIS-DL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 778 ESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLL 837
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
707-930 |
5.80e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 707 EQELSsLLRDKRQEVEREherkmdkmKEEHWQEMADARERYEAEerKQRADLLGHLTGELERLRR-AHERELESMRqEQD 785
Cdd:PRK04863 836 EAELR-QLNRRRVELERA--------LADHESQEQQQRSQLEQA--KEGLSALNRLLPRLNLLADeTLADRVEEIR-EQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 786 QQLEDLRRRHRDHERKLQDLEVELSSRTKDvKARLAQLnvqEENIRKEKQLLLDAQRQA-ALEREEATATHQHLEEAKKE 864
Cdd:PRK04863 904 DEAEEAKRFVQQHGNALAQLEPIVSVLQSD-PEQFEQL---KQDYQQAQQTQRDAKQQAfALTEVVQRRAHFSYEDAAEM 979
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160420304 865 HTHLLETKQQLRRTIDDLRVRRVELESQvdLLQAQSQRLQKH--LSSLEAEVQRKQDVLKEMAAEMNA 930
Cdd:PRK04863 980 LAKNSDLNEKLRQRLEQAEQERTRAREQ--LRQAQAQLAQYNqvLASLKSSYDAKRQMLQELKQELQD 1045
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
738-877 |
6.17e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 738 QEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHER---KLQDLEVELSSRTK 814
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160420304 815 DVKARLAQLNVQEENIRKEkqllldAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRR 877
Cdd:PRK12705 113 ALSARELELEELEKQLDNE------LYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEE 169
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
774-928 |
6.38e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 774 ERELESMRQEQDQQLEDlrrrhRDHERKlQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLldaqrqaalereeata 853
Cdd:PRK12704 48 KKEAEAIKKEALLEAKE-----EIHKLR-NEFEKELRERRNELQKLEKRLLQKEENLDRKLELL---------------- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160420304 854 thqhleeaKKEHTHLLETKQQLRRTIDDLRVRRVELEsqvDLLQAQSQRLQkHLSSLEAEvQRKQDVLKEMAAEM 928
Cdd:PRK12704 106 --------EKREEELEKKEKELEQKQQELEKKEEELE---ELIEEQLQELE-RISGLTAE-EAKEILLEKVEEEA 167
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
559-916 |
8.75e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 559 ENQIRTEQQAAlqrlrEEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAAlraekeaEKEAALLQ-LREQLEGER 637
Cdd:PRK10929 25 EKQITQELEQA-----KAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVI-------DNFPKLSAeLRQQLNNER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 638 KEAVAGLEKKHSAELEQlcSSLEAKHQEVISSLQkkiegAQQKEEA--QLQESLGWAEQRAHQKVHQVTEYEQELSSLlr 715
Cdd:PRK10929 93 DEPRSVPPNMSTDALEQ--EILQVSSQLLEKSRQ-----AQQEQDRarEISDSLSQLPQQQTEARRQLNEIERRLQTL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 716 DKRQEVEREHERKMDKMkeehwqemadareryEAEERKQRADLLghltgELERLRRAHERELESMR--------QEQDQQ 787
Cdd:PRK10929 164 GTPNTPLAQAQLTALQA---------------ESAALKALVDEL-----ELAQLSANNRQELARLRselakkrsQQLDAY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 788 LEDLR-----RRHRDHERKLQ----------DLEVELSSRTKDVKARLAQLNVQEENIrkekQLLLDAQRQAA---LERE 849
Cdd:PRK10929 224 LQALRnqlnsQRQREAERALEstellaeqsgDLPKSIVAQFKINRELSQALNQQAQRM----DLIASQQRQAAsqtLQVR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 850 EATATHQHLEEAKKEHTHLLET-------------KQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQR 916
Cdd:PRK10929 300 QALNTLREQSQWLGVSNALGEAlraqvarlpempkPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNR 379
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
555-780 |
9.12e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 555 TEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKeaekeaallQLREQLE 634
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE---------QAAKQAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 635 GERKEAVaglEKKHSAELEQlcssleAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVteyEQElssll 714
Cdd:TIGR02794 116 EKQKQAE---EAKAKQAAEA------KAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA---EAE----- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160420304 715 RDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADllghltgELERLRRAHERELESM 780
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAA-------AAEAERKADEAELGDI 237
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
556-675 |
9.32e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.95 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 556 EAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRaekeaekeaallQLREQLE 634
Cdd:cd16269 180 EAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEqQRELEQKLEDQERSYEEHLR------------QLKEKME 247
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 160420304 635 GERKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIE 675
Cdd:cd16269 248 EERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
571-854 |
9.72e-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: 43.56 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 571 QRLREEAETLQKAErasleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQlegerkeavaglekKHSA 650
Cdd:pfam05483 530 ERMLKQIENLEEKE-----MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE--------------KQMK 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 651 ELEQLCSSLEAKhqevISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVhQVTEYEQELSSLlRDKRQEVEREHERKMD 730
Cdd:pfam05483 591 ILENKCNNLKKQ----IENKNKNIEELHQENKALKKKGSAENKQLNAYEI-KVNKLELELASA-KQKFEEIIDNYQKEIE 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 731 --KMKEEHWQEMADARERYEAEERKQRADL---LGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDL 805
Cdd:pfam05483 665 dkKISEEKLLEEVEKAKAIADEAVKLQKEIdkrCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL 744
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 160420304 806 EVELSsrtkDVKARLAQLNVQEENIRKEKQLLldaqrqaALEREEATAT 854
Cdd:pfam05483 745 EIELS----NIKAELLSLKKQLEIEKEEKEKL-------KMEAKENTAI 782
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
738-924 |
1.01e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 738 QEMAdARERYEAEERKQRADLLGHLtgelerlrraherelesmrQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVK 817
Cdd:PRK11637 54 QDIA-AKEKSVRQQQQQRASLLAQL-------------------KKQEEAISQASRKLRETQNTLNQLNKQIDELNASIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 818 ARLAQLNVQ--------------------------EENIRKEKQL----LLDAQRQAALE-----REEATATHQHLEEAK 862
Cdd:PRK11637 114 KLEQQQAAQerllaaqldaafrqgehtglqlilsgEESQRGERILayfgYLNQARQETIAelkqtREELAAQKAELEEKQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 863 KEHTHLLETKQQlrrtiddlrvrrveleSQVDLLQAQSQRlQKHLSSLEAEVQRKQDVLKEM 924
Cdd:PRK11637 194 SQQKTLLYEQQA----------------QQQKLEQARNER-KKTLTGLESSLQKDQQQLSEL 238
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
547-690 |
1.20e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 547 LRAQVQSRTEAFENQIRTEQQAalqrLREEAETLQKAERASLEQKSR-----RALEQLREQLEAEERSAQAALRaEKEAE 621
Cdd:pfam04012 9 VRANIHEGLDKAEDPEKMLEQA----IRDMQSELVKARQALAQTIARqkqleRRLEQQTEQAKKLEEKAQAALT-KGNEE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 622 KEAALLQLREQLEG--ERKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQK-KIEGAQQKEEAQLQESLG 690
Cdd:pfam04012 84 LAREALAEKKSLEKqaEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLlKARLKAAKAQEAVQTSLG 155
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
312-687 |
1.21e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 312 QKENENSDPKASSSQMAPELDPGGDQPSRASK-KQQAEDPVQA---GKEGECRR--ESAAKEPKEASALENTSDVSEESE 385
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKAeeaKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAK 1496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 386 ihghlKDARHSGSEASGPKSFLGLDLGFRSRISEHLLDGDtlspvlggghwEAQGLDQEEQDDSKSSiAEPQSKHTQGSE 465
Cdd:PTZ00121 1497 -----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-----------EAKKADEAKKAEEKKK-ADELKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 466 REHLQSSLHSQATEEGPLQTLEGQPEWKEAEgpgKDSVASPAPLSLLQSLLKAQLQKATAEEKEKEEETKIREEESRRLV 545
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 546 CLRAQV--------QSRTEAFENQIRTEQQA---------ALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEER 608
Cdd:PTZ00121 1637 QLKKKEaeekkkaeELKKAEEENKIKAAEEAkkaeedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 609 SAQAALRAEKEAEKEAALLQlREQLEGERKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKI-EGAQQKEEAQLQE 687
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAK-KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeEELDEEDEKRRME 1795
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
559-769 |
1.24e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 559 ENQIRTEQQAALQRLREEAETLQ------KAERASLEQKSRRALEQLRE-QLEAEERSAQaalraekeaekeaalLQLRE 631
Cdd:pfam05667 326 EEELQQQREEELEELQEQLEDLEssiqelEKEIKKLESSIKQVEEELEElKEQNEELEKQ---------------YKVKK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 632 QLEGERKEAVAGLEKkhsaeLEQLCSSleakhqevisSLQKKIEGAQQKEEAQlqeslgwaeqrahqkVHQVTEYEQels 711
Cdd:pfam05667 391 KTLDLLPDAEENIAK-----LQALVDA----------SAQRLVELAGQWEKHR---------------VPLIEEYRA--- 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 160420304 712 slLRDKRQEVEREHERKMDKMKEEHwQEMADAreryeAEERKQRADLLGHLTGELERL 769
Cdd:pfam05667 438 --LKEAKSNKEDESQRKLEEIKELR-EKIKEV-----AEEAKQKEELYKQLVAEYERL 487
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
770-1076 |
1.26e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 770 RRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENI-------RKEKQLLLDAQR 842
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDhnrasmqRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 843 QAALEREEATATHQhLEEakkehthLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLK 922
Cdd:PLN02939 116 QTNSKDGEQLSDFQ-LED-------LVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 923 eMAAEMNAspHPE-PGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVR-----QFLSAEGVAVRNAKEFLVRqtr 996
Cdd:PLN02939 188 -LAAQEKI--HVEiLEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLlkddiQFLKAELIEVAETEERVFK--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 997 sMRRRQTALKAAQQHWRHELASAQE---------VDEDLPGTEVLGNMrknLNEETRHLDEMKSAMRKGHDLLKKKEEkl 1067
Cdd:PLN02939 262 -LEKERSLLDASLRELESKFIVAQEdvsklsplqYDCWWEKVENLQDL---LDRATNQVEKAALVLDQNQDLRDKVDK-- 335
|
....*....
gi 160420304 1068 iqLESSLQE 1076
Cdd:PLN02939 336 --LEASLKE 342
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
649-922 |
1.39e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 649 SAELEQLCSSLEA----KHQEVISSLQKKIEgAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKrQEVERE 724
Cdd:TIGR04523 287 EKQLNQLKSEISDlnnqKEQDWNKELKSELK-NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN-SEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 725 HERKMDKMKeehwqemadaRERYEAEERKQRADLLGHLTGELERlrraHERELESMRQEQDQQLEDLRRRHRDHERKLQD 804
Cdd:TIGR04523 365 LEEKQNEIE----------KLKKENQSYKQEIKNLESQINDLES----KIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 805 LEVE---LSSRTKDVKARLAQLNVQEEN----IRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRR 877
Cdd:TIGR04523 431 LKETiikNNSEIKDLTNQDSVKELIIKNldntRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 160420304 878 TIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLK 922
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
775-931 |
1.53e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 775 RELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKdvKARLAqLNVQEENIRKEKqllldAQRQAALErEEATAT 854
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEE--KARLA-LEKGREDLAREA-----LERKAELE-AQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 855 HQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQsQRLQKHLSSLEAE--------VQRKQDvlkEMAA 926
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEALSGIDSDdatsalerMEEKIE---EMEA 179
|
....*
gi 160420304 927 EMNAS 931
Cdd:COG1842 180 RAEAA 184
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
746-927 |
1.72e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 746 RYEAEERKQRAD------LLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKAR 819
Cdd:pfam15709 283 KYDAEESQVSIDgrssptQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 820 LAQlNVQEENIRKEKQLLLDAQRQAalerEEATATHQHLEEAKKEHTHLlETKQQLRRTIDDLRVRRVELESQVDLLQAQ 899
Cdd:pfam15709 363 LQQ-EQLERAEKMREELELEQQRRF----EEIRLRKQRLEEERQRQEEE-ERKQRLQLQAAQERARQQQEEFRRKLQELQ 436
|
170 180
....*....|....*....|....*...
gi 160420304 900 SQRLQKHLSSLEAEVQRKQDVLKEMAAE 927
Cdd:pfam15709 437 RKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
720-916 |
1.91e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 41.29 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 720 EVEREHERKMDKMKEEHWQEMADAREryEAEERKQR-ADLLGHLTGELERLRRAHERELESMRQEQdQQLEDLRRRHRDH 798
Cdd:pfam14988 7 EYLAKKTEEKQKKIEKLWNQYVQECE--EIERRRQElASRYTQQTAELQTQLLQKEKEQASLKKEL-QALRPFAKLKESQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 799 ERKLQDLEVELSSRTKDVKARLAQLNVQeenIRKEKQLLldaQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRT 878
Cdd:pfam14988 84 EREIQDLEEEKEKVRAETAEKDREAHLQ---FLKEKALL---EKQLQELRILELGERATRELKRKAQALKLAAKQALSEF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 160420304 879 IDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQR 916
Cdd:pfam14988 158 CRSIKRENRQLQKELLQLIQETQALEAIKSKLENRKQR 195
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
709-927 |
2.00e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 709 ELSSLLRDKRQEVEREheRKMDKMKEEHWQEMADARERYEAEERKQRADllghltgELERLRRAHERELESMRQEQdQQL 788
Cdd:PHA02562 167 EMDKLNKDKIRELNQQ--IQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE-------NIARKQNKYDELVEEAKTIK-AEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 789 EDLRRRHRDHERKLQDLevelSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQrqaalereEATATHQHLEEAKKEHTHL 868
Cdd:PHA02562 237 EELTDELLNLVMDIEDP----SAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG--------VCPTCTQQISEGPDRITKI 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 869 LETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQ----------KHLSSLEAEVQRKQDVLKEMAAE 927
Cdd:PHA02562 305 KDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLelknkistnkQSLITLVDKAKKVKAAIEELQAE 373
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
547-1090 |
2.30e-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: 42.50 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 547 LRAQVQSRTEAFENQIRTEQQAaLQRLREEAETLQKaeraslEQKSRRALEQLreqLEAEERSAQAALRAEKEAEKEAAL 626
Cdd:pfam10174 47 LRKEEAARISVLKEQYRVTQEE-NQHLQLTIQALQD------ELRAQRDLNQL---LQQDFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 627 LQLREQLEGERKEAVAGLEKKHSAELEqlcSSLEAKHQEVIS---SLQKKIEGAQQKEEAQLQESLGWAEQRahqkvhQV 703
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEME---LRIETQKQTLGArdeSIKKLLEMLQSKGLPKKSGEEDWERTR------RI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 704 TEYE---QELSSLLRDKrqEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRAdllghlTGELERLRRAHERELESM 780
Cdd:pfam10174 188 AEAEmqlGHLEVLLDQK--EKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTK------ISSLERNIRDLEDEVQML 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 781 RQEQDQQLEDlrrrhrdHERKLQDLEVeLSSRTKDVKARLAQLNvQEENiRKEKQLLLDAQRQAALEREEATaTHQHLEE 860
Cdd:pfam10174 260 KTNGLLHTED-------REEEIKQMEV-YKSHSKFMKNKIDQLK-QELS-KKESELLALQTKLETLTNQNSD-CKQHIEV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 861 AKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNasphpepGLH- 939
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN-------VLQk 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 940 -IEDLrksldtnknQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRSMRRRQTALKAAQQHWRHELAS 1018
Cdd:pfam10174 402 kIENL---------QEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELES 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 1019 AQEVDEDLpgTEVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEEVSDEDTLKGSSIK 1090
Cdd:pfam10174 473 LKKENKDL--KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKK 542
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
516-924 |
2.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 516 LKAQLQKATAEEKEKEEETKIREEESRRLvclrAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERaSLEQKSRRA 595
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRL----EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK-ELEELEKAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 596 LEQLREQLEAEERSAQAalraekeaekeaallqlrEQLEGERKEAVAGLEKKHS------AEL-EQLCSSLEAKHQEVIS 668
Cdd:PRK03918 401 EEIEEEISKITARIGEL------------------KKEIKELKKAIEELKKAKGkcpvcgRELtEEHRKELLEEYTAELK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 669 SLQKKIEGAQQKEEaQLQESLgwaeqrahQKVHQVTEYEQELSSLLRDKRQEVEREherkmDKMKEEHWQEMADARERYE 748
Cdd:PRK03918 463 RIEKELKEIEEKER-KLRKEL--------RELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEELEKKAEEYE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 749 AEERKqradlLGHLTGELERLrrahERELESMrQEQDQQLEDLRRRHRDHERKLQDLEVELSSR----TKDVKARLAQLN 824
Cdd:PRK03918 529 KLKEK-----LIKLKGEIKSL----KKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 825 ------VQEENIRKEKQLLLDAQrqaALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDD-----LRVRRVELESQV 893
Cdd:PRK03918 599 pfyneyLELKDAEKELEREEKEL---KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSREL 675
|
410 420 430
....*....|....*....|....*....|.
gi 160420304 894 DLLQAQSQRLQKHLSSLEAEVQRKQDVLKEM 924
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
702-864 |
2.39e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 702 QVTEYEQE---LSSLLRDKRQEV-------EREHERKMDKMKEEHWQEMADARERYEAE-ERKQRADLlghlTGELERLR 770
Cdd:COG2268 175 AITDLEDEnnyLDALGRRKIAEIirdariaEAEAERETEIAIAQANREAEEAELEQEREiETARIAEA----EAELAKKK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 771 RAHERELESMRQEQDQQLEDLRrrhrdhERKLQDLE--VELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALER 848
Cdd:COG2268 251 AEERREAETARAEAEAAYEIAE------ANAEREVQrqLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
|
170
....*....|....*.
gi 160420304 849 EEATATHQhLEEAKKE 864
Cdd:COG2268 325 AEAEAEAI-RAKGLAE 339
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
559-806 |
2.44e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 559 ENQIRTEQQAALQRLREEAETLQKA----ERASLEQKSRRALEQLREQLeAEERSAQAALRAEKEAEKEAALLQLREQLE 634
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRlhlqQCSQELALKLTALHALQLTL-TQERVREHALSIRVLPKELLASRQLALQKM 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 635 GERKEAVAG----LEKKHSAELEQLCSSLEAKH-----QEVISSLQKKIEGaqqkEEAQLQESLGWAE-QRAHQKVHQVT 704
Cdd:TIGR00618 686 QSEKEQLTYwkemLAQCQTLLRELETHIEEYDRefneiENASSSLGSDLAA----REDALNQSLKELMhQARTVLKARTE 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 705 EYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHErELESMRQEQ 784
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE-QFLSRLEEK 840
|
250 260
....*....|....*....|..
gi 160420304 785 DQQLEDLRRRHRDHERKLQDLE 806
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLA 862
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
548-904 |
2.52e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTEQQAALQRLREEA---ETLQKAE--RASLEQKSRRALEQLReqleAEERSAQAALRAEKEAEK 622
Cdd:NF041483 116 RLQAELHTEAVQRRQQLDQELAERRQTVEShvnENVAWAEqlRARTESQARRLLDESR----AEAEQALAAARAEAERLA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 623 EAALLQLREQLEGERKEAVAGLeKKHSAELEQLCSSLEAKHQEVIS-SLQKKIEGAQQKEEA--QLQESLGWAEQRAhqk 699
Cdd:NF041483 192 EEARQRLGSEAESARAEAEAIL-RRARKDAERLLNAASTQAQEATDhAEQLRSSTAAESDQArrQAAELSRAAEQRM--- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 700 vhqvteyeQELSSLLRDKRQEVerehERKMDKMKEEHWQEMADARERYEAEER---KQRADLLGHLTGELERLRRAHERE 776
Cdd:NF041483 268 --------QEAEEALREARAEA----EKVVAEAKEAAAKQLASAESANEQRTRtakEEIARLVGEATKEAEALKAEAEQA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 777 LESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRT---------KDVKARLAQLNVQEENIRKEkqllldAQRQAALE 847
Cdd:NF041483 336 LADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTaeevltkasEDAKATTRAAAEEAERIRRE------AEAEADRL 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 160420304 848 REEATATHQHLEEAKKEHThlletkqqlrrtiDDLRVRRVELESQVDLLQAQSQRLQ 904
Cdd:NF041483 410 RGEAADQAEQLKGAAKDDT-------------KEYRAKTVELQEEARRLRGEAEQLR 453
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
565-790 |
2.57e-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: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQKAERASLEQkSRRALEQLREQLEAEERS------------AQAALRAEKEAEKEAALLQLREQ 632
Cdd:pfam10174 447 EKERIIERLKEQREREDRERLEELES-LKKENKDLKEKVSALQPEltekesslidlkEHASSLASSGLKKDSKLKSLEIA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 633 LEGERKEAVA---GLEKKHSAELEQLCS---SLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEY 706
Cdd:pfam10174 526 VEQKKEECSKlenQLKKAHNAEEAVRTNpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 707 EQELSSLLRDKRQEVeREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRA-------------- 772
Cdd:pfam10174 606 ESLTLRQMKEQNKKV-ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEldatkarlsstqqs 684
|
250 260
....*....|....*....|.
gi 160420304 773 -HERE--LESMRQEQDQQLED 790
Cdd:pfam10174 685 lAEKDghLTNLRAERRKQLEE 705
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
577-861 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 577 AETLQKAERASLEQKSRRALEQLREQL-EAEERSAQAALRaekeaekeaaLLQLREQlegerkEAVAGLEKKHSAELEQL 655
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLpELRKELEEAEAA----------LEEFRQK------NGLVDLSEEAKLLLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 656 cSSLEAKhqevISSLQKKIEGAQQKEEaQLQESLGWAEQRAhQKVHQVTEYEQelsslLRDKRQEVEREHERKMDKMKEE 735
Cdd:COG3206 222 -SELESQ----LAEARAELAEAEARLA-ALRAQLGSGPDAL-PELLQSPVIQQ-----LRAQLAELEAELAELSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 736 HwQEMADAREryeaeerkQRADLLGHLTGELERLRRAHERELESMRQeQDQQLEDLRRRHRDHERKLQDLEVELSSRTKD 815
Cdd:COG3206 290 H-PDVIALRA--------QIAALRAQLQQEAQRILASLEAELEALQA-REASLQAQLAQLEARLAELPELEAELRRLERE 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 160420304 816 VKARLAQLnvqeenirkekQLLLDAQRQAALEREEATATHQHLEEA 861
Cdd:COG3206 360 VEVARELY-----------ESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
567-723 |
2.70e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 567 QAALQRLREEAETLQ-KAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAekeaaLLQLREQLEGER-KEAVAGL 644
Cdd:pfam00529 64 EAQLAKAQAQVARLQaELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQ-----LAQAQIDLARRRvLAPIGGI 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 645 EKKHSAELEQLCSSLEAKHQEVISSLQKkiegAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQEVER 723
Cdd:pfam00529 139 SRESLVTAGALVAQAQANLLATVAQLDQ----IYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
554-860 |
2.86e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 554 RTEAFE--NQIRTEQQAALQRLREEaetlqkAERASLEQKSRRALEQLREQLEAEERSAQAalraekeaekEAALLQLRE 631
Cdd:NF041483 537 RAEAEEqaEEVRAAAERAARELREE------TERAIAARQAEAAEELTRLHTEAEERLTAA----------EEALADARA 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 632 QLEGERKEAVAGLEKkhsaeleqlcssLEAKHQEVISSLQkkiegAQQKEEAQLQESLGWAEQRAHQkvhqvTEYEQELS 711
Cdd:NF041483 601 EAERIRREAAEETER------------LRTEAAERIRTLQ-----AQAEQEAERLRTEAAADASAAR-----AEGENVAV 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 712 SLLRDKRQEVER---EHERKMDKMKeehwQEMADARERYEAEErkqrADLLGHLTGELERLRRAHERELESMRQEQDQQl 788
Cdd:NF041483 659 RLRSEAAAEAERlksEAQESADRVR----AEAAAAAERVGTEA----AEALAAAQEEAARRRREAEETLGSARAEADQE- 729
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 789 edlRRRHRDherklQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEE 860
Cdd:NF041483 730 ---RERARE-----QSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEE 793
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
565-920 |
3.12e-03 |
|
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: 42.25 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALqrLREEAETL--QKAERASLEQKSRRALEQLREQL------------EAEERSAQAALR--AEKEAEKEAALLQ 628
Cdd:COG3096 784 EKRLEE--LRAERDELaeQYAKASFDVQKLQRLHQAFSQFVgghlavafapdpEAELAALRQRRSelERELAQHRAQEQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 629 LREQLEgERKEAVAGLEKKhsaeLEQLCSSLEAKHQEVISSLQKKIEGAQQKEeaqlqeslgwAEQRAHQKvhQVTEYEQ 708
Cdd:COG3096 862 LRQQLD-QLKEQLQLLNKL----LPQANLLADETLADRLEELREELDAAQEAQ----------AFIQQHGK--ALAQLEP 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 709 ELSSLLRDKRQ--EVEREHERKMDKMKEEHWQ--EMADARERYEAEERKQRADLLGHLTGELERLRrAHERELESMRQEQ 784
Cdd:COG3096 925 LVAVLQSDPEQfeQLQADYLQAKEQQRRLKQQifALSEVVQRRPHFSYEDAVGLLGENSDLNEKLR-ARLEQAEEARREA 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 785 DQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKA---RLAQLNVQEENirkekqlllDAQRQAALEREEatathqhleea 861
Cdd:COG3096 1004 REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQEleqELEELGVQADA---------EAEERARIRRDE----------- 1063
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160420304 862 kkehthlleTKQQLRRTiddlRVRRVELESQVDLLQAQSQRLQKHLSSLEAE--VQRKQDV 920
Cdd:COG3096 1064 ---------LHEELSQN----RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDykQEREQVV 1111
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
629-921 |
3.15e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 629 LREQLEGERKEAVAGLEKKHSAELEQLcSSLEAKhqevISSLQKKIEGAQQKEEAQLQEslgwaeQRAHQKvhqvtEYEQ 708
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTL-ESAELR----LSHLHFGYKSDETLIASRQEE------RQETSA-----ELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 709 ELSSLLRDKRQEVEREHERKmdKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRraherELESMRQEQDQQL 788
Cdd:pfam12128 291 LLRTLDDQWKEKRDELNGEL--SAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLP-----SWQSELENLEERL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 789 EDLRRRHRDHERKLQDLEVELSSRTKDVkarLAQLNVQEENIRKEKQLLLDAQRqAALEREEATATHQHlEEAKKEhthL 868
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRD---IAGIKDKLAKIREARDRQLAVAE-DDLQALESELREQL-EAGKLE---F 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 869 LETKQQLRRTIDDLRVR--RVELESQVDLLQAQSQ----RLQKHLSSLEAEVQRKQDVL 921
Cdd:pfam12128 436 NEEEYRLKSRLGELKLRlnQATATPELLLQLENFDerieRAREEQEAANAEVERLQSEL 494
|
|
| AmyAc_MTSase |
cd11336 |
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ... |
721-793 |
3.23e-03 |
|
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
Pssm-ID: 200475 [Multi-domain] Cd Length: 660 Bit Score: 41.71 E-value: 3.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160420304 721 VEREHERKMDKMkeehWQEMADARERYEAEERKQRADLL-GHLTGELERLRRAHERELESMRQEQDQQLEDLRR 793
Cdd:cd11336 291 VDPAGEAALTRL----YRRFTGDPGDFAELVREAKRLVLdTSLAGELNRLARLLGRIAEADRRTRDFTLNALRR 360
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
517-1082 |
3.50e-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: 41.88 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 517 KAQLQKATAEEKEKEEETKIREEESRRlvclraqvqsRTEAFENQI---RTEQQAALQRLREEAETLQKAERASLEQKSR 593
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEI----------KREAEEEEEeelEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 594 RALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEavAGLEKKHSAELEQLCSSLEAKHQEVISSLQK- 672
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES--IELKQGKLTEEKEELEKQELKLLKDELELKKs 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 673 -KIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAD--ARERYEA 749
Cdd:pfam02463 471 eDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvAISTAVI 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 750 EER---KQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLnvq 826
Cdd:pfam02463 551 VEVsatADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG--- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 827 eenIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKH 906
Cdd:pfam02463 628 ---ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 907 LSSLEAEVQRKQDVLKEMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRN 986
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 987 AKEFLVRQTRSMRRRQTALKAAQQHWRHE---LASAQEVDEDLPGTEVLGNMRKNLNEETRHLDEMKSAMRKghDLLKKK 1063
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEaelLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL--ERLEEE 862
|
570
....*....|....*....
gi 160420304 1064 EEKLIQLESSLQEEVSDED 1082
Cdd:pfam02463 863 ITKEELLQELLLKEEELEE 881
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
593-913 |
3.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 593 RRALEQLREQLEAEersaqaalraekeaekeaallqlREQLEGERKEAVAGLEKKHSaeLEQLCSSLEAKHQEVisSLQK 672
Cdd:PRK04863 781 RAAREKRIEQLRAE-----------------------REELAERYATLSFDVQKLQR--LHQAFSRFIGSHLAV--AFEA 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 673 KIEGAQQKEEAQLQEslgwaeqrAHQKVHQVTEYEQELSSLLRDKRQEVE--REHERKMDKMKEEHWQEMADA--RERYE 748
Cdd:PRK04863 834 DPEAELRQLNRRRVE--------LERALADHESQEQQQRSQLEQAKEGLSalNRLLPRLNLLADETLADRVEEirEQLDE 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 749 AEERKQRADLLGHLTGELER--------------LRRAHErELESMRQEQDQQLEDL-----RRRHRDHERKLQDL--EV 807
Cdd:PRK04863 906 AEEAKRFVQQHGNALAQLEPivsvlqsdpeqfeqLKQDYQ-QAQQTQRDAKQQAFALtevvqRRAHFSYEDAAEMLakNS 984
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 808 ELSSRtkdVKARLAQLNVQEENIRkekqlllDAQRQAaleREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDL----- 882
Cdd:PRK04863 985 DLNEK---LRQRLEQAEQERTRAR-------EQLRQA---QAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpad 1051
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 160420304 883 -------RVRRVELESQvdLLQAQSQR--LQKHLSSLEAE 913
Cdd:PRK04863 1052 sgaeeraRARRDELHAR--LSANRSRRnqLEKQLTFCEAE 1089
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
722-867 |
3.70e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.25 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 722 EREHERKMDKMKEEHWQEMADAREryEAEERKQRADLLGHltGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERK 801
Cdd:pfam12072 22 KSIAEAKIGSAEELAKRIIEEAKK--EAETKKKEALLEAK--EEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRK 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160420304 802 LQDL---EVELSSRTKDVKARLAQLNVQEEN----IRKEKQLLldaQRQAALEREEATAthQHLEEAKKEHTH 867
Cdd:pfam12072 98 DESLekkEESLEKKEKELEAQQQQLEEKEEEleelIEEQRQEL---ERISGLTSEEAKE--ILLDEVEEELRH 165
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
565-786 |
4.12e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 565 EQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRaekeaekeaaLLQLREQLEGERKEAvagl 644
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIR----------LRKQRLEEERQRQEE---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 645 EKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESlgwAEQRAHQKVHQVTEYEQELSSLLRDKRQEVERE 724
Cdd:pfam15709 406 EERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEA---EKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160420304 725 herkmdkmKEEhwqemADARERYEAEERKQRADllghltgelERLRRAHErelESMRQEQDQ 786
Cdd:pfam15709 483 --------KQE-----AEEKARLEAEERRQKEE---------EAARLALE---EAMKQAQEQ 519
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
547-755 |
4.52e-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: 41.50 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 547 LRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSR-----RALEQLREQLEAEERSAQAALRAEKEAE 621
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERleeeiTKEELLQELLLKEEELEEQKLKDELESK 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 622 KEAALLQLREQLEGERKEAVagLEKKHSAELEQlcSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVH 701
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNL--LEEKENEIEER--IKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 160420304 702 QVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwQEMADARERYEAEERKQR 755
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLE--EEKKKLIRAIIEETCQRL 1019
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
548-686 |
4.96e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTE---QQAALQRLREEAETLQKAERASLEQ-KSRRALEQLREQLEAEERSAQAALRAEKEAEKE 623
Cdd:COG2268 194 IAEIIRDARIAEAEAEREteiAIAQANREAEEAELEQEREIETARIaEAEAELAKKKAEERREAETARAEAEAAYEIAEA 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160420304 624 AALLQLREQLEGERKEAVAGLEKKhSAELEQlcssleakhQEVISSLQKKIEG----AQQKEEAQLQ 686
Cdd:COG2268 274 NAEREVQRQLEIAEREREIELQEK-EAEREE---------AELEADVRKPAEAekqaAEAEAEAEAE 330
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
808-1027 |
5.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 808 ELSSRTKDVKARLAQLNVQEENIRKEKQ---LLLDAqRQAALEREEATATHQHLEEAKKEHTHLLETK--QQLRRTIDDL 882
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqieLLEPI-RELAERYAAARERLAELEYLRAALRLWFAQRrlELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 883 RVRRVELESQVDLLQAQSQRLQKHLSSLEA-------------------------EVQRKQDVLKEMAAEMnasphpepG 937
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAqirgnggdrleqlereierlereleERERRRARLEALLAAL--------G 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 938 LHIEDLRKSLDTNKnQEVSSSLSLSKEEIDLSMESVRQFLSAEgVAVRNAKEFLVRQTRSMRRRQTALKAAQQHWRHELA 1017
Cdd:COG4913 373 LPLPASAEEFAALR-AEAAALLEALEEELEALEEALAEAEAAL-RDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
250
....*....|.
gi 160420304 1018 SAQEVDE-DLP 1027
Cdd:COG4913 451 EALGLDEaELP 461
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
547-685 |
5.43e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 547 LRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAE-----ERSAQAALRAEKEAE 621
Cdd:PRK12705 38 ILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEER-LVQKEEQLDARaekldNLENQLEEREKALSA 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160420304 622 KEAALLQLREQLEGERKEaVAGLEKKHSaeLEQLCSSLEAKHQEvisslQKKIEGAQQKEEAQL 685
Cdd:PRK12705 117 RELELEELEKQLDNELYR-VAGLTPEQA--RKLLLKLLDAELEE-----EKAQRVKKIEEEADL 172
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
548-801 |
5.47e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 548 RAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALL 627
Cdd:pfam02029 61 EEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 628 QLREQLEGERKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYE 707
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 708 QELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEE------RKQRADL-LGHLTGELERLRRAHERELESM 780
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEfeklrqKQQEAELeLEELKKKREERRKLLEEEEQRR 300
|
250 260
....*....|....*....|....*
gi 160420304 781 RQEQDQQL----EDLRRRHRDHERK 801
Cdd:pfam02029 301 KQEEAERKlreeEEKRRMKEEIERR 325
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
639-777 |
5.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 639 EAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIEgAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKR 718
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 719 QEVEREHE-RKMDKMKEEHWQEMADARERYEaeerkqradllgHLTGELERLRRAHEREL 777
Cdd:COG2433 459 REIRKDREiSRLDREIERLERELEEERERIE------------ELKRKLERLKELWKLEH 506
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
677-818 |
5.77e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.16 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 677 AQQKEEAQLQESLGWAEQrahQKVHQVTEYEQELSSLLR--DKRQEVEREHerkmdkmkeehwQEMADARERYEAEERKQ 754
Cdd:PTZ00491 668 ARHQAELLEQEARGRLER---QKMHDKAKAEEQRTKLLElqAESAAVESSG------------QSRAEALAEAEARLIEA 732
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160420304 755 RADLlghltgELERLR-RAH----ERELESMRQEQDQQLEdlrrrhrdHERKLQDLEVELSSRTKDVKA 818
Cdd:PTZ00491 733 EAEV------EQAELRaKALrieaEAELEKLRKRQELELE--------YEQAQNELEIAKAKELADIEA 787
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
764-927 |
6.11e-03 |
|
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: 40.65 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 764 GELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDV---KARLAQLNVQEENIRKEKQLLLDA 840
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHeelEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 841 -----QRQAALEREEATATHQHLEeakkEHTHLLETKQQLRRTIDDLRvrrvELESQVDLLQAQSQRLQKHLSSLEAEVQ 915
Cdd:pfam07888 124 raaheARIRELEEDIKTLTQRVLE----RETELERMKERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170
....*....|..
gi 160420304 916 RKQDVLKEMAAE 927
Cdd:pfam07888 196 ELRNSLAQRDTQ 207
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
693-1082 |
6.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 693 EQRAHQKVHQVTEYEQELSSLLRDK--RQEVEREHERKMDKMKEEHWQEMADARERYEaEERKQRADLLGHLTG------ 764
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQitSKEAQLESSREIVKSYENELDPLKNRLKEIE-HNLSKIMKLDNEIKAlksrkk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 765 ELERLRRAHERELESMRQEQDQQLEDLRRRH----RDHERKLQDLEVELSSRTKDVKaRLAQLNVQEENIRKEKQLLLDA 840
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQGTDEQLNDLYHNHqrtvREKERELVDCQRELEKLNKERR-LLNQEKTELLVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 841 QRQAALERE---EATATHQHLE----------EAKKEHTHLLETKQQLRRTIDDLRVrrvELESQVDLLQAQSQRLQKHL 907
Cdd:TIGR00606 359 HQEHIRARDsliQSLATRLELDgfergpfserQIKNFHTLVIERQEDEAKTAAQLCA---DLQSKERLKQEQADEIRDEK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 908 SSLEAEVQRKQDVLKEMAAEM--------NASPHPEPGLHIED-LRKSL-DTNKNQEVSSSLSLSKEEIDLSMESVRQFL 977
Cdd:TIGR00606 436 KGLGRTIELKKEILEKKQEELkfvikelqQLEGSSDRILELDQeLRKAErELSKAEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 978 S----AEGVAVRNAKEFLVRQTRSMRRRQTAL--KAAQQHWRHELASAQEVDeDLPGTEVLGN-----------MRKNL- 1039
Cdd:TIGR00606 516 KlrklDQEMEQLNHHTTTRTQMEMLTKDKMDKdeQIRKIKSRHSDELTSLLG-YFPNKKQLEDwlhskskeinqTRDRLa 594
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 160420304 1040 --NEETRHLDEMKSAMRKGhdlLKKKEEKLIQLESSLQEEVSDED 1082
Cdd:TIGR00606 595 klNKELASLEQNKNHINNE---LESKEEQLSSYEDKLFDVCGSQD 636
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
745-978 |
7.21e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 745 ERYEAEERKQRADLLghltgELERLRraheRELESMRQEQDQQLEDLRRRhrdHERKLQDLEVELSSRTKDVKARLAQln 824
Cdd:PRK00409 523 ASLEELERELEQKAE-----EAEALL----KEAEKLKEELEEKKEKLQEE---EDKLLEEAEKEAQQAIKEAKKEADE-- 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 825 vqeenIRKEKQLLLDAQrQAALEREEATATHQHLEEAKKEhthlLETKQQLRRTIDDL-----RVRRVELESQVDLLQAQ 899
Cdd:PRK00409 589 -----IIKELRQLQKGG-YASVKAHELIEARKRLNKANEK----KEKKKKKQKEKQEElkvgdEVKYLSLGQKGEVLSIP 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 900 SQRlqkhlsslEAEVQrkQDVLKemaaeMNasphpepgLHIEDLRKSLDTNKNQEVSSSLSLSKE-----EIDL------ 968
Cdd:PRK00409 659 DDK--------EAIVQ--AGIMK-----MK--------VPLSDLEKIQKPKKKKKKKPKTVKPKPrtvslELDLrgmrye 715
|
250
....*....|.
gi 160420304 969 -SMESVRQFLS 978
Cdd:PRK00409 716 eALERLDKYLD 726
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
758-916 |
7.40e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.44 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 758 LLGHLTGELERLRRAHER--ELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKdvKARLAQLNVQEENIRKEKQ 835
Cdd:pfam19220 32 LIEPIEAILRELPQAKSRllELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVA--RLAKLEAALREAEAAKEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 836 LLLDAQRQAALEREE--ATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAE 913
Cdd:pfam19220 110 RIELRDKTAQAEALErqLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAE 189
|
...
gi 160420304 914 VQR 916
Cdd:pfam19220 190 LAE 192
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
698-805 |
7.84e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 38.31 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 698 QKVHQVTEYEQELSSLLRDKRQEVE---REHERKMDKMKEEHWQEMADA--RERYEAEER--------KQRADLlghLTG 764
Cdd:pfam12474 4 QKEQQKDRFEQERQQLKKRYEKELEqleRQQKQQIEKLEQRQTQELRRLpkRIRAEQKKRlkmfreslKQEKKE---LKQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 160420304 765 ELERLRRAHERELESMRQEQ------DQQLEDLRRRHRDHERKLQDL 805
Cdd:pfam12474 81 EVEKLPKFQRKEAKRQRKEEleleqkHEELEFLQAQSEALERELQQL 127
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
626-1081 |
7.97e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 626 LLQLREQLEGERKEAVAGLEKKHSAELEQLCSSLE------AKHQEVISSLQKKIEGAQQK------EEAQLQESLGWAE 693
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEeiqnqiSQNNKIISQLNEQISQLKKEltnsesENSEKQRELEEKQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 694 QRAHQKVHQVTEYEQELSSL------LRDKRQEVEREHERKMDKMK--EEHWQEMADARERYEAEERKQrADLLGHLTGE 765
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLesqindLESKIQNQEKLNQQKDEQIKklQQEKELLEKEIERLKETIIKN-NSEIKDLTNQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 766 LERLRRAHErELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKarlaQLNVQEENIRKEKQLLldAQRQAA 845
Cdd:TIGR04523 449 DSVKELIIK-NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK----KLNEEKKELEEKVKDL--TKKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 846 LEREEatathQHLEEAKKEhthlLETK-QQLRRTI--DDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLK 922
Cdd:TIGR04523 522 LKEKI-----EKLESEKKE----KESKiSDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 923 EMAAEmnasphpepglhIEDLRKSLDTNknqevSSSLSLSKEEIDLSMESVRQfLSAEGVAVRNAKEFLVRQTRSMrrrQ 1002
Cdd:TIGR04523 593 QKEKE------------KKDLIKEIEEK-----EKKISSLEKELEKAKKENEK-LSSIIKNIKSKKNKLKQEVKQI---K 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160420304 1003 TALKAAQQHWRHELASAQEVDEDLpgTEVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEE-KLIQLESSLQEEVSDE 1081
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKyKEIEKELKKLDEFSKE 729
|
|
| |
