|
Name |
Accession |
Description |
Interval |
E-value |
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
82-898 |
0e+00 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 996.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 82 KEVLVKQHSKVAEEAVTGWEKAEAEASALKTHLETITLAKLTVEDRAAHLDGALKECMRQIRSLKEENEQKLHDVIATKT 161
Cdd:pfam05911 1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 162 NQMDNLRAEFESRIGEYEEELLRCGAENDALSRSLQERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVI 241
Cdd:pfam05911 81 KEWEKIKAELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEKEINSLKYELHVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 242 TKELEIRNEEKNMSMRSAEAANKQHLEGVKKIAKLEAECQRLRTLVRKKLPGPAALAQMKMEVESLGFgDHrQDHRQRRS 321
Cdd:pfam05911 161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLVRKKLPGPAALAQMKLEVEMLGR-DS-GETRLRRS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 322 PVRPSSPlmspmsHMSQVSEFSLDNMQKFHKENDLLTERLLAMEEETKMLKEALAKRNSELQVSRNLCAKTANRLQTLEA 401
Cdd:pfam05911 239 PVKNSSP------HLSPDPDFSEDSLQTPHKENEFLTERLLAMEEETKMLKEALAKRNSELQASRNMCAKTASKLSQLEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 402 QMMSKSPTkrgfEMPAEIFSRQN-ASNPPSMASMSEDGNEDARSVAGS----LMSELSQSNKDKANAKIKKTESAN-QLE 475
Cdd:pfam05911 313 QLEELNQG----QVSMELASSQNpASNPPSLTSMSEDGSDDEVSCAESwasaLISELEHFKKEKPKTKSSCKSVGNsDLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 476 LMDDFLEMEKLACLPNGSNANGSTDHS----------------------------SADSDAEIPPATQLKKRISNVLQSL 527
Cdd:pfam05911 389 LMDDFLEMEKLACLSNDKPSNGSHSSSkssnnkkgeesdsekdssestgkelvpvSSKDISLGKSLSWLQSRISVILESH 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 528 PKDAAFEKILAEIQCAVKDAGVKLP-------SKSHGANL---------NGLTEEKVIAMSNETTEEKVTIVEVITQELS 591
Cdd:pfam05911 469 VTQKSIGKILEDIRCALQDINDSLPeadsclsSGHPSTDAscdyitckeNSSVVEKEGSVSGDDKSSEETSKQSIQQDLS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 592 DALSQIYQFVTYLSKEATAC----SENRTFSQKVQEFSTTFEGVLGKEKTLVDFLFDLSRVLVEASELKIDVLGFHTSTV 667
Cdd:pfam05911 549 KAISKIIDFVEGLSKEALDDqdtsSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSLLDVSSMED 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 668 EIHSPDCIDKVALPENKALQKDSSGEHYQNGCsqsSDSEIPDDCNGTSG-YEPKLATCKFTTEEFEGLKLEKEKAESNLA 746
Cdd:pfam05911 629 EIKKHDCIDKVTLSENKVAQVDNGCSEIDNLS---SDPEIPSDGPLVSGsNDLKTEENKRLKEEFEQLKSEKENLEVELA 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 747 SCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGETQLKCMVESYRSLETRSSELEIELTSLKGKIENLEDELHDEK 826
Cdd:pfam05911 706 SCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEK 785
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063684916 827 ENHREALAKCQELEEQLQRN-NQNCPNCSVIEDDPKSKQDNELAAAAEKLAECQETILLLGKQLKSMC-PQTEQ 898
Cdd:pfam05911 786 NCHEELEAKCLELQEQLERNeKKESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGKQLKALAsPQDAS 859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-307 |
6.42e-09 |
|
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: 60.07 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 50 EVKSYEEKVTKLEDQIKDLDLKLSTAnadivakEVLVKQHSKVAEEAVTGWEKAEAEASALKTHLETITLAKLTVEDRAA 129
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 130 HLDGALKECMRQIRSLKEENE-------------QKLHDVIATKTNQMDNLRA---EFESRIGEYEEELLRCGAENDALS 193
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEeaeeelaeaeaeiEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 194 RSLQERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIRNEEKNMSMRSAEAANKQHLEGVKKI 273
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270
....*....|....*....|....*....|....
gi 1063684916 274 AKLEAECQRLRTlvrkklpgpaALAQMKMEVESL 307
Cdd:TIGR02168 911 SELRRELEELRE----------KLAQLELRLEGL 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-843 |
4.32e-07 |
|
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: 54.29 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 56 EKVTKLEDQIKDLDLKLSTAnaDIVAKEVLVKQHSKVAEEAVTGWEKAEAEASALKTHLETITLAKLTVEDRAAHLDGAL 135
Cdd:TIGR02168 213 ERYKELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 136 KECMRQIrslkeeneqklhdviatktnqmdnlrAEFESRIGEYEEELLRCGAENDALSRSLQERSNMLMRISEEKSQAES 215
Cdd:TIGR02168 291 YALANEI--------------------------SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 216 EIEHLKNNIESCEREINTLKYEThvitKELEIRNEEKNMSMRSAEAANKQHLEgvkKIAKLEAECQRLRTLVrkklpgpa 295
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAEL----EELESRLEELEEQLETLRSKVAQLEL---QIASLNNEIERLEARL-------- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 296 alaqmkmeveslgfgdHRQDHRQRRSPVRPSSPLMSPMSHMSQVSEFSLDNMQKfhkENDLLTERLLAMEEETKMLKEAL 375
Cdd:TIGR02168 410 ----------------ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 376 AKRNSELQVSRNLCAKTANRLQTLEAQMMSKSPTKRGFEMPAEIFSRQNASNPPSMASMS-EDGNEDARSVA-GSLMSEL 453
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvDEGYEAAIEAAlGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 454 SQSNKDKANAKI---KKTES--ANQLEL---MDDFLEMEKLACLPNGSNANGSTDhSSADSDAEIPPATQLkkRISNVL- 524
Cdd:TIGR02168 551 VVENLNAAKKAIaflKQNELgrVTFLPLdsiKGTEIQGNDREILKNIEGFLGVAK-DLVKFDPKLRKALSY--LLGGVLv 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 525 -QSLPKDAAFEKILAEIQCAVKDAGVKLpsKSHGANLNG--LTEEKVIAMSNE--TTEEKVTIVEVITQELSDALSQIY- 598
Cdd:TIGR02168 628 vDDLDNALELAKKLRPGYRIVTLDGDLV--RPGGVITGGsaKTNSSILERRREieELEEKIEELEEKIAELEKALAELRk 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 599 QFVTYLSKEATACSENRTFSQKVQEFSTTFEGVLGKEKTLVDFLFDLSRVLVEASElKIDVLGFHTSTVEIHSPDCIDKV 678
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA-EIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 679 AlpENKALQKDSSGEHYQNGCSQSSDSEIPDDCNG-----TSGYEPKLATCKFTTEEFEGLKLEKEKAESNLASCEADLE 753
Cdd:TIGR02168 785 E--ELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 754 atktklqETEKLLAEVKSDLESAQKSNGMGETQLKCMVESYRSLETRSSELEIELTSLKGKIENLEDELHDEKENHREAL 833
Cdd:TIGR02168 863 -------ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
810
....*....|
gi 1063684916 834 AKCQELEEQL 843
Cdd:TIGR02168 936 VRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-291 |
6.40e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 56 EKVTKLEDQIKDLD-----LKLSTANADIVAKEVLVKQHSKVAEEAVTGWEKAEAEASALKTHLETITLAKLTVEDRAAH 130
Cdd:COG1196 213 ERYRELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 131 LDGALKECMRQIRSLKE------ENEQKLHDVIATKTNQMDNLRAEFESRIGEYEEELLRCGAENDALSRSLQERSNMLM 204
Cdd:COG1196 293 LLAELARLEQDIARLEErrreleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 205 RISE----------EKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIRNEEKNMSMRSAEAANKQHLEGVKKIA 274
Cdd:COG1196 373 ELAEaeeeleelaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250
....*....|....*..
gi 1063684916 275 KLEAECQRLRTLVRKKL 291
Cdd:COG1196 453 ELEEEEEALLELLAELL 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-224 |
8.19e-06 |
|
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: 50.06 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 10 KKSSEKTATVTEVVDQENGKKPSYIQISFDQYTNLNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQH 89
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 90 SKVAEEAVTGWEKAEAEASALKTHLETITLAKLTVEDRAAHLDGALKECMRQIRSLKEENEQKLHDViatktNQMDNLRA 169
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-----ASLEEALA 890
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063684916 170 EFESRIGEYEEELLRCGAENDALSRSLQERSNMLMRISEEKSQAESEIEHLKNNI 224
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
732-845 |
2.07e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 732 EGLKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGETQLKcMVESYRSLETrsseLEIELTSL 811
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEYEA----LQKEIESL 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 1063684916 812 KGKIENLED---ELHDEKENHREALAKCQELEEQLQR 845
Cdd:COG1579 102 KRRISDLEDeilELMERIEELEEELAELEAELAELEA 138
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-237 |
3.76e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 47 LKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKE-VLVKQHSKV----AEEAVTGWEKAEAEASALKTHLETItlak 121
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEeDLHKLEEALndleARLSHSRIPEIQAELSKLEEEVSRI---- 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 122 ltvEDRAAHLDGALKECMRQIRSLKEENEQKLHDVIATKTN------QMDNLRA---EFESRIGEYEEELLRCGAENDAL 192
Cdd:TIGR02169 811 ---EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksiekEIENLNGkkeELEEELEELEAALRDLESRLGDL 887
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063684916 193 SRSLQERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLKYE 237
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
44-298 |
3.84e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 44 LNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAEEAVTGWEKAEAEASALKTHLETITLAKLT 123
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 124 VEDRAAHLDGALKECMRQIRSLKEENEQKLHDVIATKTNQMDNL--RAEFESRIGEYEEELLRCGAENDALSRSLQERSN 201
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 202 MLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIR-NEEKNMSMRSAEAANKQHLEGVKKIAKLEAEC 280
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLlEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
250
....*....|....*...
gi 1063684916 281 QRLRTLVRKKLPGPAALA 298
Cdd:COG1196 530 IGVEAAYEAALEAALAAA 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-845 |
5.32e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 705 SEIPDDCNGTSGYEPKLATCKFTTEEFEGLKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGE 784
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063684916 785 TQLKcMVESYRSLETRSSELEIELTSLKGKIENLEDELhDEKENHREALAKCQELEEQLQR 845
Cdd:PRK03918 294 EYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKLKELEK 352
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
734-926 |
6.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 734 LKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGETQLKCMVESYRSLETRSSELEIELTSLKG 813
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 814 KIENLEDELHDEKENHREALAKCQELEEQLQRNNQNcpncsvIEDDPKSKQDNELAAAAEKLAECQETILLLGKQLKSMC 893
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
170 180 190
....*....|....*....|....*....|...
gi 1063684916 894 PQTEQVASSPSQEQQALNPEEEEYATSTNPQDS 926
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
44-199 |
7.62e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 44 LNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAEEAvtgweKAEAEASALKTHLETITLAKLT 123
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063684916 124 VEDRAAHLDGALKEcmrqirslKEENEQKLHDVIATKTNQMDNLRAEFESRIGEYEEELLRCGAENDALSRSLQER 199
Cdd:COG1579 108 LEDEILELMERIEE--------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
29-283 |
8.62e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 29 KKPSYIQISFDQYTNLNGLKDEVKSYEEKVTKLEDQIKDLDLKLstanadivakevlvkqhskvaeEAVTGWEKAEAEAS 108
Cdd:PRK05771 80 SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI----------------------ERLEPWGNFDLDLS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 109 ALKtHLETITLAKLTVEDRAAHLDGALKEcmrqIRSLKEENEQKLHD--VIATKTNQMDNLraefesrigeyEEELLRCG 186
Cdd:PRK05771 138 LLL-GFKYVSVFVGTVPEDKLEELKLESD----VENVEYISTDKGYVyvVVVVLKELSDEV-----------EEELKKLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 187 AENDALSRSlqersnmlMRISEEKSQAESEIEHLKNNIESCEREINTLK---YETHVITKE-LEIRNEEKNMSMRSAEAA 262
Cdd:PRK05771 202 FERLELEEE--------GTPSELIREIKEELEEIEKERESLLEELKELAkkyLEELLALYEyLEIELERAEALSKFLKTD 273
|
250 260
....*....|....*....|....
gi 1063684916 263 NKQHLEG---VKKIAKLEAECQRL 283
Cdd:PRK05771 274 KTFAIEGwvpEDRVKKLKELIDKA 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
39-223 |
2.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 39 DQYTNLNGLKDEVKSYEEKVTKLEdQIKDLDLKLSTANADIVAKEVLVKQHSkvAEEAVTGWEKAEAEASALKTHLETIT 118
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 119 LAKLTVEDRAAHLDGALKECMRQIRS--------LKEENE--QKLHDVIATKTNQMDNL-----------RAEFESRIGE 177
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGnggdrleqLEREIErlERELEERERRRARLEALlaalglplpasAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063684916 178 YEEELLRCGAENDALSRSLQERSNMLMRISEEKSQAESEIEHLKNN 223
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-285 |
5.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 41 YTNLNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAEEAVTGWEKAEAEASALKTHLETITLA 120
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 121 KLTVEDRAAHLdGALKECMRQIRSLKEENEQKLHDvIATKTNQMDNLR--AEFESRIGEYEEELLRCGAENDALSRSLQE 198
Cdd:PRK03918 244 EKELESLEGSK-RKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKekAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 199 RSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLK-----YEThVITKELEIRNEEKNMSMRSAEAANKQHLEGVKKI 273
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhelYEE-AKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250
....*....|..
gi 1063684916 274 AKLEAECQRLRT 285
Cdd:PRK03918 401 EEIEEEISKITA 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
730-916 |
5.34e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 730 EFEGLKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGETQLKCMVESYRSLETRSSELEIELT 809
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 810 SLKGKIENLEDELHDEKENHREALAKCQELEEQ---------------------LQRNNQNcpncsvieddpKSKQDNEL 868
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalrealdelraeLTLLNEE-----------AANLRERL 826
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063684916 869 AAAAEKLAECQETILLLGKQLKSMCPQTEQVASSPSQEQQALNPEEEE 916
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-307 |
6.60e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 49 DEVKSYEEKVTKLEDQIKDLD-LKLSTANADIVAKEVLvKQHSKVAEEAvtgwEKAEaEASALKTHLETITLAKLTVEDR 127
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEeVEENIERLDLIIDEKR-QQLERLRRER----EKAE-RYQALLKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 128 AahLDGALKECMRQIRSLKEENEQ--KLHDVIATKTNQMDNLRAEFESRI---GEYE-----EELLRCGAENDALSRSLQ 197
Cdd:TIGR02169 234 A--LERQKEAIERQLASLEEELEKltEEISELEKRLEEIEQLLEELNKKIkdlGEEEqlrvkEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 198 ERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIRNEEKNMSMRSAEAANKQH----------- 266
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdelkdyr 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1063684916 267 --LEGVK-KIAKLEAECQRLRTLVRKKlpgPAALAQMKMEVESL 307
Cdd:TIGR02169 392 ekLEKLKrEINELKRELDRLQEELQRL---SEELADLNAAIAGI 432
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
44-217 |
6.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 44 LNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQhskvAEEAVTGWEKAEAEASALKTHLETITLAKLT 123
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE----RREELGERARALYRSGGSVSYLDVLLGSESF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 124 VE--DRAAHLD---GALKECMRQIRSLKEENEQKLHDViATKTNQMDNLRAEFESRIGEYEEELLRCGAENDALSRSLQE 198
Cdd:COG3883 115 SDflDRLSALSkiaDADADLLEELKADKAELEAKKAEL-EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
170
....*....|....*....
gi 1063684916 199 RSNMLMRISEEKSQAESEI 217
Cdd:COG3883 194 AEAQLAELEAELAAAEAAA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-226 |
7.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 27 NGKKPsyiQISFDQYTNLNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKV--AEEAVTGWEKAE 104
Cdd:COG4717 62 QGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 105 AEASALKTHLEtitlakltvedraahldgALKECMRQIRSLKEEnEQKLHDVIATKTNQMDNLRAEFESrigEYEEELLR 184
Cdd:COG4717 139 AELAELPERLE------------------ELEERLEELRELEEE-LEELEAELAELQEELEELLEQLSL---ATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063684916 185 CGAENDALSRSLQERSNMLMRISEEKSQAESEIEHLKNNIES 226
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
728-843 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 728 TEEFEGLKLEKEKAESNLASCEADLEATKTKLQE--TEKLLAEVKSDLESAQKSNGMGETQLKCMVESYRSLETRSSELE 805
Cdd:COG1579 51 KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 1063684916 806 IELTSLKGKIENLEDELHDEKENHREALAKCQELEEQL 843
Cdd:COG1579 131 AELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
720-845 |
1.14e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 720 KLATCKFTTEEFEGLKLEKEKAE-----SNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGETQLKCMVESY 794
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063684916 795 RSL-ETRSSELEIELTSLKGKIENLEDELHDEKENHREALAKCQELEEQLQR 845
Cdd:TIGR02169 282 KDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-232 |
1.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 55 EEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAE---------EAVTGWEKAEAEASALKTHLETITLAKLTV- 124
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeysWDEIDVASAEREIAELEAELERLDASSDDLa 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 125 --EDRAAHLDGALKECMRQIRSLKEEnEQKLHDVIATKTNQMDNLRAEFESRIGEYEEELLRCGAE------NDALSRSL 196
Cdd:COG4913 689 alEEQLEELEAELEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalGDAVEREL 767
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063684916 197 QErsnmlmRISEEKSQAESEIEHLKNNIESCEREIN 232
Cdd:COG4913 768 RE------NLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
44-234 |
1.45e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 44 LNGLKDEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAEEAVTGWEKAEAE-----ASALKTHLETIT 118
Cdd:COG4942 43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 119 LAKLTVED------RAAHLDGALKECMRQIRSLKEENEQklhdvIATKTNQMDNLRAEFESRIGEYEEELlrcgaenDAL 192
Cdd:COG4942 123 ALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAE-----LAALRAELEAERAELEALLAELEEER-------AAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063684916 193 SRSLQERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTL 234
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
729-845 |
1.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 729 EEFEGLKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSngMGETQLKCMVESYRSLETRSSELEIEL 808
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE--LEELEKKYSEEEYEELREEYLELSREL 675
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063684916 809 TSLKGKIENLE----------DELHDEKENHREALAKCQELEEQLQR 845
Cdd:PRK03918 676 AGLRAELEELEkrreeikktlEKLKEELEEREKAKKELEKLEKALER 722
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
729-849 |
1.61e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 729 EEFEGLKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGETQLKCMVESYRSLETRSSELEIEL 808
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1063684916 809 TSLKGKIENLEDELHDEKENHREALAKCQELEEQLQRNNQN 849
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
727-848 |
1.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 727 TTEEFEGLKLEKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAQKSNGMGE-----TQLKCMVESYRSLETRS 801
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEEL 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063684916 802 SELEIELTSLKGKIENL--------EDELHDEKENHREALAKCQELEEQLQRNNQ 848
Cdd:COG4717 166 EELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
122-403 |
2.02e-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: 41.80 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 122 LTVEDRAAHLDGALKECMRQIRSLKEENEQKLHDVIATKTN------QMDNLRAEFESRIGEYEEELLRCGAENDALSRS 195
Cdd:pfam07888 23 LLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERykrdreQWERQRRELESRVAELKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 196 LQERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIRNE--EKNMSMRSAEAANKQHLEgvkki 273
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKEraKKAGAQRKEEEAERKQLQ----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 274 AKLEAECQRLRTLvrkklpgpaalaqmkmeveSLGFGDHRQDHRQRRSPVRPSSPLMSPMSHMSQVSEFSLDNMQKFHKE 353
Cdd:pfam07888 178 AKLQQTEEELRSL-------------------SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063684916 354 NDLLTERLLAMEEETKMLKEALA-------KRNSELQVSRNLCAKTANRLQTLEAQM 403
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQARLQAAQLTLQLADASLAL 295
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
737-842 |
2.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 737 EKEKAESNLASCEADLEATKTKLQETEKLLAEVKSDLESAqksngmgETQLKCMVESYRSLETRSSELEIELTSLKGKIE 816
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-------ERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100
....*....|....*....|....*.
gi 1063684916 817 NLEDELHDEKENHREALAKCQELEEQ 842
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQ 119
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-319 |
3.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 49 DEVKSYEEKVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAEEAvtgwEKAEAEASALKTHLETITLAKLTVE--- 125
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE----ERREDLEELIAERRETIEEKRERAEelr 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 126 DRAAHLDGALKECMRQIRSLKEENEQKLHDV------IATKTNQMDNLR--AEFESRIGEYEEELLRCGAENDALSRSLQ 197
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVaelnskLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 198 ERSNMLMRISEEKSQAESEIEhlKNNIESC-EREINTLKYETHVITKELEIRNEEKNMSMRSAEAANK-QHLEGVK-KIA 274
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFD--EARIEEArEDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENElEELEELReRRE 701
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063684916 275 KLEAECQRLRTLVRkklpgpaalaqmkmEVESLG--FGDHRQDHRQR 319
Cdd:PRK02224 702 ALENRVEALEALYD--------------EAEELEsmYGDLRAELRQR 734
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
129-278 |
4.41e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 129 AHLDGALKECMRQIRSLKEENEQKLHDVIATKTNQMDNLRAEFESRIGEYEEELLRcgaendaLSRSLQERSNMLMRISE 208
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-------LEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 209 EKSQAESEIEHLKNNIESCEREINTLKYEthVITKELEIRNEEKNMSMRSAEAANKQHLEGVKKIAKLEA 278
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEE--LEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
57-251 |
5.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 57 KVTKLEDQIKDLDLKLSTANADIVAKEVLVKQHSKVAEEAVTG----WEKAEAEASALKTHLETIT--LAKLTV--EDRA 128
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARkqnkYDELVEEAKTIKAEIEELTdeLLNLVMdiEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 129 AHL----DGALKECMRQIRSLKEENEQKLHDVIATKTNQM---DNLRAEFESRIGEYEEELlrcGAENDALSRsLQERSN 201
Cdd:PHA02562 255 AALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQIsegPDRITKIKDKLKELQHSL---EKLDTAIDE-LEEIMD 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063684916 202 MLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIRNEE 251
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE 380
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
48-277 |
6.41e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 48 KDEVKSYEEKVTKLEDQIKDLDLKLSTA----NADIVAKEVlVKQHSKVAEEAvtgwEKAEAEASALKTHletitlaKLT 123
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNKYSALAIKNKFAktkkDSEIIIKEI-KDAHKKFILEA----EKSEQKIKEIKKE-------KFR 1580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 124 VEDRAAHLDGALKECMrQIRSLKEENEQKLHDVIATKTNQMDNLRaEFES--------RIGEYEEELLRCGAENDALSRS 195
Cdd:TIGR01612 1581 IEDDAAKNDKSNKAAI-DIQLSLENFENKFLKISDIKKKINDCLK-ETESiekkissfSIDSQDTELKENGDNLNSLQEF 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 196 LQERSNMLMRISEEKSqaesEIEHLKNNIESCEREINTLK--YETHVITK--ELEIRNEEKNMSMRSA---------EAA 262
Cdd:TIGR01612 1659 LESLKDQKKNIEDKKK----ELDELDSEIEKIEIDVDQHKknYEIGIIEKikEIAIANKEEIESIKELieptienliSSF 1734
|
250
....*....|....*
gi 1063684916 263 NKQHLEGVKKIAKLE 277
Cdd:TIGR01612 1735 NTNDLEGIDPNEKLE 1749
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-289 |
8.24e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 117 ITLAKLTVEDRAAHLDGALKECMRQIRSLKEENE-QKLHDVIatktNQMDNLRAEFESRIGEYEEELLRCGAENDALSRS 195
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAElQRLRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 196 LQERSNMLMRISEEKSQAESEIEHLKNNIESCEREINTLKYETHVITKELEIRNEEKNmSMRSAEAANKQHLEGvKKIAK 275
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEARLSH-SRIPE 795
|
170
....*....|....
gi 1063684916 276 LEAECQRLRTLVRK 289
Cdd:TIGR02169 796 IQAELSKLEEEVSR 809
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-246 |
8.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 60 KLEDQIKDLDLKLSTANADIVAKEVLVKQhskvAEEAVTGWEKAEAEA--SALKTHLETItLAKLTVEDRAA--HLDGAL 135
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEE----LQELLREAEELEEELqlEELEQEIAAL-LAEAGVEDEEElrAALEQA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063684916 136 KECmRQIRSLKEENEQKLHDVIATKTNQMDNL-RAEFESRIGEYEEELLRCGAENDALSRSLQERSNML--MRISEEKSQ 212
Cdd:COG4717 395 EEY-QELKEELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAE 473
|
170 180 190
....*....|....*....|....*....|....
gi 1063684916 213 AESEIEHLKNNIESCEREINTLKYETHVITKELE 246
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| |
