|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-1038 |
1.12e-129 |
|
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: 422.84 E-value: 1.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 1 MMKPKGQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMF 80
Cdd:pfam02463 149 MMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 81 KKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLE 160
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 161 DVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQK 240
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 241 EKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELK 320
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 321 EKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDIAISSC 400
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 401 CHALDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLfdlvkvkneeirqafyfalrdtl 480
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL----------------------- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 481 vaNNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQ 560
Cdd:pfam02463 606 --AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 561 KVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEK 640
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 641 AGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEIN 720
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 721 DLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQ 800
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 801 KEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSE 880
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 881 RDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEK 960
Cdd:pfam02463 1004 KKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEK 1083
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152066 961 TLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTKS 1038
Cdd:pfam02463 1084 TLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
46-1029 |
2.21e-94 |
|
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: 325.87 E-value: 2.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 46 GEKLNRVKMVEKEK----DALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNV 121
Cdd:TIGR02169 183 EENIERLDLIIDEKrqqlERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 122 LSNEMKAKNSAVKDVEKKLNKVTK-FIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSK 200
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 201 TVINETTTRNNSLEKEREKEEKklkeVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTA 280
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKE----ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 281 VSQLSKAKEAL------ITASETLKERKAA-IKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSS 353
Cdd:TIGR02169 419 SEELADLNAAIagieakINELEEEKEDKALeIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 354 LAMNRSRGKVLDAIIQEKKSGrIPGIYGRLGDLGAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATF 432
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKAS-IQGVHGTVAQLGSVGERYATAIEVAAGNrLNNVVVEDDAVAKEAIELLKRRKAGRATF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 433 IGLDKMTVWAKKMSKIQTPENTPRLFDLVKVkNEEIRQAFYFALRDTLVANNLDQATRVAYQrdrrWRVVTLQGQIIEQS 512
Cdd:TIGR02169 578 LPLNKMRDERRDLSILSEDGVIGFAVDLVEF-DPKYEPAFKYVFGDTLVVEDIEAARRLMGK----YRMVTLEGELFEKS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 513 GTMSGGgSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQ-IQEQKVQHEEAVVKLRHSER---DMRNTLEKFAAS 588
Cdd:TIGR02169 653 GAMTGG-SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSeLRRIENRLDELSQELSDASRkigEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 589 IQGLSEQEEYLCVQIKELEANVltTAPDRKQQKLleenvsvfKKEYDAVAEKAGKVEAEI----KRLHNTIIDINNRKLK 664
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEI--ENVKSELKEL--------EARIEELEEDLHKLEEALndleARLSHSRIPEIQAELS 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 665 AQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAE 744
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 745 TSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQ 824
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 825 EELEAIKNPESItneialleaqcremkpNLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFY 904
Cdd:TIGR02169 962 RVEEEIRALEPV----------------NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFE 1025
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 905 VITNKLKENYQMLTlGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDE 984
Cdd:TIGR02169 1026 AINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDE 1104
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 1907152066 985 IDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1029
Cdd:TIGR02169 1105 VDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-1029 |
1.02e-81 |
|
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: 289.65 E-value: 1.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 55 VEKEKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVK 134
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 135 DVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLE 214
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 215 KErekeekklkevMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITA 294
Cdd:TIGR02168 358 AE-----------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 295 SETLKErkAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE---- 370
Cdd:TIGR02168 427 LKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegf 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 371 --------KKSGRIPGIYGRLGDLGAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVW 441
Cdd:TIGR02168 505 segvkallKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 442 AKKMSKIQTPENTPR----LFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSG 517
Cdd:TIGR02168 585 EIQGNDREILKNIEGflgvAKDLVKFD-PKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITG 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 518 GGSKvmrgrmGSSVIDEISVEevnkmesqLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEE 597
Cdd:TIGR02168 664 GSAK------TNSSILERRRE--------IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 598 YLCVQIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRlhntiidinnrKLKAQQNKLDTINKQL 677
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----------EIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 678 DECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNL 757
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 758 LQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVE-----DNPVETVAVLSQEELEAIKN 832
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevriDNLQERLSEEYSLTLEEAEA 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 833 --------PESITNEIALLEAQCREMKP-NLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGF 903
Cdd:TIGR02168 959 lenkieddEEEARRRLKRLENKIKELGPvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTF 1038
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 904 YVITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMD 983
Cdd:TIGR02168 1039 DQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILD 1118
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1907152066 984 EIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1029
Cdd:TIGR02168 1119 EVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
945-1039 |
1.99e-65 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 219.47 E-value: 1.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 945 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1024
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 1907152066 1025 RLIGIYKTYNSTKSV 1039
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-1029 |
3.36e-44 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 173.97 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 47 EKLNRVK--MVEKEK--DALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEkihedtkEITEKSNVL 122
Cdd:COG1196 186 ENLERLEdiLGELERqlEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELE-------ELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 123 SNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTV 202
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 203 INETTTRNNSLEKEREKEEKKLKEV---MDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNT 279
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAeeaLLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 280 AVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSS----LA 355
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllllLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 356 MNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIG 434
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 435 LDKMTVwAKKMSKIQTPENTPRLFDLVKVKNEEiRQAFYFALRDTLVANNLDQATRvayqRDRRWRVVTLQGQIIEQSGT 514
Cdd:COG1196 579 LDKIRA-RAALAAALARGAIGAAVDLVASDLRE-ADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 515 MSGGGSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSE 594
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 595 QEEYLCVQIKELEANVLTTAPdrkqqklleenvsvfkkEYDAVAEKAGKVEAEIKRLhntiidinnrklkaqqnkldtin 674
Cdd:COG1196 733 EREELLEELLEEEELLEEEAL-----------------EELPEPPDLEELERELERL----------------------- 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 675 kqldecasaitkaqvaiktadrnlkkaqdsvcrtekeikdtEKEINDLktelkniedkaEEVinntktaetslpeiqkeh 754
Cdd:COG1196 773 -----------------------------------------EREIEAL-----------GPV------------------ 782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 755 rNL--LQELKVIQEnehalQKDALSiklklEQIDghisehnskikywqkeiskiklhpveDnpvetvavlsqeeleaikn 832
Cdd:COG1196 783 -NLlaIEEYEELEE-----RYDFLS-----EQRE--------------------------D------------------- 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 833 pesitneiaLLEAqcremkpnlgaiaeykkKEDLyLQRVAELDKITSERdnFRQAYEDLRKQrlnefmagfyvitnkLKE 912
Cdd:COG1196 807 ---------LEEA-----------------RETL-EEAIEEIDRETRER--FLETFDAVNEN---------------FQE 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 913 NYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFK 992
Cdd:COG1196 843 LFPRLFGGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDA 922
|
970 980 990
....*....|....*....|....*....|....*..
gi 1907152066 993 NVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1029
Cdd:COG1196 923 NVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGV 959
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
955-1037 |
1.01e-32 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 125.11 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 955 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKN-AQFIIISLRNNMFEISDRLIGIYKTY 1033
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 1907152066 1034 NSTK 1037
Cdd:cd03239 175 GVST 178
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
377-491 |
5.00e-32 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 120.80 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 377 PGIYGRLGDLGAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTV-----WAKKMSKIQT 450
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGrLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907152066 451 PENTPRLFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRV 491
Cdd:smart00968 81 PGFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
944-1031 |
1.03e-29 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 118.83 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 944 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEI 1022
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*....
gi 1907152066 1023 SDRLIGIYK 1031
Cdd:cd03275 225 ADALVGVYR 233
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
376-492 |
4.17e-28 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 109.66 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 376 IPGIYGRLGDLGAIDEKYDIAISSCC-HALDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTpENT 454
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLK-GGA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907152066 455 PRLFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRVA 492
Cdd:pfam06470 80 GPLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
950-1029 |
8.98e-28 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 111.40 E-value: 8.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 950 KKIFN---LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRL 1026
Cdd:cd03278 106 KKVQRlslLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
...
gi 1907152066 1027 IGI 1029
Cdd:cd03278 186 YGV 188
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
952-1032 |
9.15e-24 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 98.97 E-value: 9.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 952 IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEISDRLIGIY 1030
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
..
gi 1907152066 1031 KT 1032
Cdd:cd03227 155 KV 156
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
950-1029 |
1.09e-16 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 80.77 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 950 KKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1029
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
949-1034 |
1.68e-16 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 80.42 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 949 WKK-IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLi 1027
Cdd:cd03273 160 WKEsLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL- 238
|
....*..
gi 1907152066 1028 giYKTYN 1034
Cdd:cd03273 239 --FRTRF 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
94-353 |
1.82e-09 |
|
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: 61.96 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 94 LQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAK--------NSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVR 165
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnkelKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 166 EKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEvmdsLKQETQGLQKEKEIQ 245
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 246 EKE---LMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKakealitaseTLKERKAAIKDINTKLPQTQQELKEK 322
Cdd:TIGR04523 425 EKEierLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----------QLKVLSRSINKIKQNLEQKQKELKSK 494
|
250 260 270
....*....|....*....|....*....|.
gi 1907152066 323 EKELQKLTQEEINLKSLVHDLFQKVEEAKSS 353
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
952-1031 |
2.33e-08 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 54.17 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 952 IFNLSGGEKTLSSLALVFALhhyKPtPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFE-ISDRLIGI 1029
Cdd:cd00267 78 VPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
..
gi 1907152066 1030 YK 1031
Cdd:cd00267 154 KD 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-352 |
2.49e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 25 GRLNEPIKVLCRRVEILNEHR---GEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEI 101
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 102 TTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKlnkvtkfieQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQ 181
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA---------KGKCPVCGRELTEEHRKELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 182 LQKDKEKVEELKSVPAKSKTVINETTTrnnslekerEKEEKKLKEVMDSLKQETQGLQKEK-EIQEKELMGFNKSVNEAR 260
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESE---------LIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 261 SKMEVAQSELDiylsrhntAVSQLSKAKEALITASETLKERKAAIKDINTKLP-QTQQELKEKEKELQKLTQEEINLKSL 339
Cdd:PRK03918 539 GEIKSLKKELE--------KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDA 610
|
330
....*....|...
gi 1907152066 340 VHDLFQKVEEAKS 352
Cdd:PRK03918 611 EKELEREEKELKK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
96-374 |
8.03e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 96 NRIAE--ITTQKEKIHEDTKEITEksnVLSNEMKAKNSAVKDVEKKLNKvtkFIEQNKekFTQLDLEDVQVREKLKHATS 173
Cdd:COG3206 155 NALAEayLEQNLELRREEARKALE---FLEEQLPELRKELEEAEAALEE---FRQKNG--LVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 174 KAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTrnnslekerekeekklKEVMDSLKQETQGLQKEKEIQEKELMGFN 253
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 254 KSVNEARSKMEVAQSELDiylSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQkltqee 333
Cdd:COG3206 291 PDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE------ 361
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907152066 334 iNLKSLVHDLFQKVEEAKSSLAMNRSRGKVLD-AIIQEKKSG 374
Cdd:COG3206 362 -VARELYESLLQRLEEARLAEALTVGNVRVIDpAVVPLKPVS 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
537-851 |
3.89e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 537 VEEVNKMESQLErHSKQAMQIQEQKVQHEEAVVKLRHSE-RDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAP 615
Cdd:pfam15921 481 VEELTAKKMTLE-SSERTVSDLTASLQEKERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 616 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNtiiDINNRKLKAQQ-----NKLDTINKQLDECASAITKAQVA 690
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEfkilkDKKDAKIRELEARVSDLELEKVK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 691 IKTAD-------RNLKKAQDSVCrteKEIKDTEKEINDLKTEL----KNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQ 759
Cdd:pfam15921 637 LVNAGserlravKDIKQERDQLL---NEVKTSRNELNSLSEDYevlkRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 760 ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKI--KLHPVEdnpvETVAVLSQEELEAIKNPESIT 837
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkEKHFLK----EEKNKLSQELSTVATEKNKMA 789
|
330
....*....|....
gi 1907152066 838 NEIALLEAQCREMK 851
Cdd:pfam15921 790 GELEVLRSQERRLK 803
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
955-1031 |
1.46e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 46.82 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 955 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK---NAQFIIISLRNNMFEISDRLIGIYK 1031
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQDISGLASSDDVKVFR 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-352 |
1.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 105 KEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKkLNKVTKFIEQNKEKFTQLDLEDVQVR-------EKLKHATSKAKK 177
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEK-LEKEVKELEELKEEIEELEKELESLEgskrkleEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 178 LEKQLQKDKEKVEELKSVPAKSKTVInetttrnnslekerekeekKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVN 257
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEYI-------------------KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 258 EARSKMEVAQ------SELDIYLSRHNTAVSQLSKAKeALITASETLKERKA--AIKDINTKLPQTQQELKEKEKELQKL 329
Cdd:PRK03918 332 ELEEKEERLEelkkklKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260
....*....|....*....|...
gi 1907152066 330 TQEEINLKSLVHDLFQKVEEAKS 352
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKK 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
113-806 |
1.98e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 113 KEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQK-------D 185
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKinseiknD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 186 KEKVEELKSVPAKSKTVINETT---TRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSK 262
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKkniDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 263 ---MEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERkaaikdiNTKLPQTQQELKEKEKELQKLTQEEINLKSL 339
Cdd:TIGR04523 196 llkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK-------QQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 340 VHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRL-GDLGAIDEKYDIAISSCCHAldyivVDSIDTAQEC 418
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN-----NKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 419 VNFLKKhnigiatfiglDKMTVWAKKMSK-IQTPENTPRLFDLVKVKNEEIRQAFYFALRDTLVANNLDQATRVAYQRDR 497
Cdd:TIGR04523 344 ISQLKK-----------ELTNSESENSEKqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 498 RWRVVTLQGQIIEQsgtmsgggskvmrgrmgssvideisveEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERD 577
Cdd:TIGR04523 413 QIKKLQQEKELLEK---------------------------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 578 MRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTapdRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIID 657
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL---NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 658 INNRKLKAQQN-KLDTINKQLDECASAITKaqvaIKTADRNLKKAQDSVcrtEKEIKDTEKEINDLKTELKNIEDKAEEV 736
Cdd:TIGR04523 543 LEDELNKDDFElKKENLEKEIDEKNKEIEE----LKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 737 inntktaETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKI 806
Cdd:TIGR04523 616 -------EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-373 |
2.55e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 91 IYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKh 170
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 171 atsKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKqetqglqKEKEIQEKELM 250
Cdd:TIGR04523 402 ---NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-------NTRESLETQLK 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 251 GFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLT 330
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907152066 331 QE--EINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKS 373
Cdd:TIGR04523 552 FElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
556-971 |
2.77e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 556 QIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANV-LTTAPDRKQQKLLEENVSVFKKEy 634
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpNLQNITVRLQDLTEKLSEAEDML- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 635 dAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKL-------DTINKQLDECASAITKAQVAIKTADR-NLKKAQDSVC 706
Cdd:TIGR00618 611 -ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalhalqLTLTQERVREHALSIRVLPKELLASRqLALQKMQSEK 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 707 RTEKEIKDTEKEINDLKTELKNIEDKAEEVIN---------------NTKTAETSLPEIQKEHRNLLQELKVIQENEHAL 771
Cdd:TIGR00618 690 EQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassslgsdlaaREDALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 772 QKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAiKNPESITNEIALLEAQCREMK 851
Cdd:TIGR00618 770 VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSATLGEIT 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 852 PNLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELELVDSL 931
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNAR 928
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907152066 932 DPFSEGIMF------SVRPPKkswkkifNLSGGEKTLSSLALVFAL 971
Cdd:TIGR00618 929 KYQGLALLVadaytgSVRPSA-------TLSGGETFLASLSLALAL 967
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-370 |
2.80e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 147 IEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekerekeekklke 226
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 227 vMDSLKQETQGLQKEKEIQEKELMGFNKSV--NEARSKMEV---AQSELDIYlsRHNTAVSQLSKAKEALITA-SETLKE 300
Cdd:COG4942 85 -LAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllsPEDFLDAV--RRLQYLKYLAPARREQAEElRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 301 RKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE 370
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
538-784 |
4.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 538 EEVNKMESQLERHSKQAM---QIQEQKVQHEEAVVKLRHSERdMRNTLEKFAAsiqglseqeeylcvqikELEANVLtta 614
Cdd:COG4913 235 DDLERAHEALEDAREQIEllePIRELAERYAAARERLAELEY-LRAALRLWFA-----------------QRRLELL--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 615 pdRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTA 694
Cdd:COG4913 294 --EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 695 DRnlkkaqdSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETslpEIQKEHRNLLQELKVIQENEHALQKD 774
Cdd:COG4913 372 GL-------PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRKSNIPAR 441
|
250
....*....|
gi 1907152066 775 ALSIKLKLEQ 784
Cdd:COG4913 442 LLALRDALAE 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
662-895 |
5.98e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 662 KLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEvinntk 741
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 742 tAETSLPEIQKEHRNLLQELKVIQENEHA---LQKDALSIKLKLEQIDGHISEHNskikywQKEISKIKlhpvednpvet 818
Cdd:COG4942 95 -LRAELEAQKEELAELLRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPAR------REQAEELR----------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152066 819 vavLSQEELEAIKnpESITNEIALLEAQCREMKpnlgaiAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQR 895
Cdd:COG4942 157 ---ADLAELAALR--AELEAERAELEALLAELE------EERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
603-900 |
1.13e-04 |
|
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: 46.58 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 603 IKELEaNVLTTAPDrkQQKLLEENVSVFKKEYDavaEKAGKVEAEikrlhNTIIDINNRKLKAQQNKLDTINKQLDECAS 682
Cdd:TIGR00606 697 ISDLQ-SKLRLAPD--KLKSTESELKKKEKRRD---EMLGLAPGR-----QSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 683 AITKAQVAIKTADRNLKKAQDSVC------RTEKEIKDTEKEINDLKTELKNIE---------DKAEEVINNTKTAETSL 747
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVCLTdvtimeRFQMELKDVERKIAQQAAKLQGSDldrtvqqvnQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 748 PEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEEL 827
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 828 EAIKNPESITNEIALLEAQcrEMKPNLGAIAEYKK---------KEDLYLQRVAELDKITSERDNFRQayedlRKQRLNE 898
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVN--DIKEKVKNIHGYMKdienkiqdgKDDYLKQKETELNTVNAQLEECEK-----HQEKINE 998
|
..
gi 1907152066 899 FM 900
Cdd:TIGR00606 999 DM 1000
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
579-897 |
1.32e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 579 RNTLEKFAA--SIQGLSEQEEYLCVQIKE-LEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTI 655
Cdd:pfam12128 305 ELNGELSAAdaAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 656 IDINNRKL----KAQQNKLDTINKQLDECASA------------------ITKAQVAIKTADRNLKKAQDSVCRTEKEIK 713
Cdd:pfam12128 385 KEQNNRDIagikDKLAKIREARDRQLAVAEDDlqaleselreqleagkleFNEEEYRLKSRLGELKLRLNQATATPELLL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 714 DTE---KEINDLKTEL----KNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQID 786
Cdd:pfam12128 465 QLEnfdERIERAREEQeaanAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEA 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 787 GHISEHNSKIkywqkeISKIKLHPVEDNPVETVAVLSQE--------ELEAIKNPESITNEIAlLEAQCREMKPNLGAIA 858
Cdd:pfam12128 545 PDWEQSIGKV------ISPELLHRTDLDPEVWDGSVGGElnlygvklDLKRIDVPEWAASEEE-LRERLDKAEEALQSAR 617
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907152066 859 EYKKKEDLYL-QRVAELDKITSERDNFRQAYE--DLRKQRLN 897
Cdd:pfam12128 618 EKQAAAEEQLvQANGELEKASREETFARTALKnaRLDLRRLF 659
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
589-831 |
1.46e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 589 IQGLSEQEEYLCVQIKELEANVLttapdrKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINnRKLKAQQN 668
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIE------EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLV-MDIEDPSA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 669 KLDTINkqldecaSAITKAQVAIKTADRNLKKAQD-SVCRTEKE-IKDTEKEINDLKTELKNIEDKAEEVinntktaets 746
Cdd:PHA02562 256 ALNKLN-------TAAAKIKSKIEQFQKVIKMYEKgGVCPTCTQqISEGPDRITKIKDKLKELQHSLEKL---------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 747 lpeiqKEHRnllQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNpvETVAVLSQEE 826
Cdd:PHA02562 319 -----DTAI---DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA--EELAKLQDEL 388
|
....*
gi 1907152066 827 LEAIK 831
Cdd:PHA02562 389 DKIVK 393
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
100-359 |
1.61e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 100 EITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHatsKAKKLE 179
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 180 KQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKlkevMDSLKQETQGLQKEKEIQEKELMGFNKSVNEA 259
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN----IEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 260 RSKMEVAQSELDIYLSRHNTAVSQ--------LSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQ 331
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDkkiseeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE 721
|
250 260
....*....|....*....|....*...
gi 1907152066 332 EEINLKSLVHDLFQKVEEAKSSLAMNRS 359
Cdd:pfam05483 722 ERDSELGLYKNKEQEQSSAKAALEIELS 749
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
622-901 |
2.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 622 LLEENVSVFKKEYDAVAEKAGKVEAEIKRLhNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKA 701
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQA-REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 702 QDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 781
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 782 LEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYK 861
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907152066 862 KKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMA 901
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
668-862 |
2.64e-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: 43.76 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 668 NKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNtktaetsl 747
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 748 peiqKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKlhpvednpvetvavlsqEEL 827
Cdd:COG1579 89 ----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK-----------------AEL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907152066 828 EAIKnpESITNEIALLEAQCREMKPNLGA--IAEYKK 862
Cdd:COG1579 148 DEEL--AELEAELEELEAEREELAAKIPPelLALYER 182
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
444-838 |
3.66e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 444 KMSKIQTPENTPRLFDLVKVK-NEEIRQAFYFALRDTLVANN----LDQATRV--AYQRDRRWRVVTLQGQIIEQSGTMS 516
Cdd:NF012221 1438 RVSELDTYTNTSLYQDLSNLTaGEVIALSFDFARRAGLSTNNgievLWNGEVVfaSSGDASAWQQKTLKLTAKAGSNRLE 1517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 517 GGGSKVMRGrMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASiqglseqe 596
Cdd:NF012221 1518 FKGTGHNDG-LGYILDNVVATSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGS-------- 1588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 597 eylcvQiKELEANvlttapdrkQQKLLEENVSVfkkEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNK------- 669
Cdd:NF012221 1589 -----Q-SQLEST---------DQNALETNGQA---QRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGdqwrnpf 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 670 ----LDTINKQLDECASAITKAQVAIKTA-DRNLKKAQDSVC-------RTEKEIKDTEKEINDLKTELKNIEDKAEEVI 737
Cdd:NF012221 1651 agglLDRVQEQLDDAKKISGKQLADAKQRhVDNQQKVKDAVAkseagvaQGEQNQANAEQDIDDAKADAEKRKDDALAKQ 1730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 738 NNTKTAET-SLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIK---YWQKEISKIKLHPVED 813
Cdd:NF012221 1731 NEAQQAESdANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNRQGAAGSGLSgkaYSVEGVAEPGSHINPD 1810
|
410 420
....*....|....*....|....*....
gi 1907152066 814 NPVET----VAVLSQEELEAIKNPESITN 838
Cdd:NF012221 1811 SPAAAdgrfSEGLTEQEQEALEGATNAVN 1839
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
636-883 |
4.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 636 AVAEKAGKVEAEIKRLhntiidinNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDT 715
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 716 EKEINDLKTELKNIEDKAEEVINNT-KTAETSLPEI---QKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISE 791
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALyRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 792 HNSKIKYWQKEISKIKlhpvednpvETVAVLSQEELEAIKNPESITNEIALLEAQcremkpnlgaIAEYKKKEDLYLQRV 871
Cdd:COG4942 169 LEAERAELEALLAELE---------EERAALEALKAERQKLLARLEKELAELAAE----------LAELQQEAEELEALI 229
|
250
....*....|..
gi 1907152066 872 AELDKITSERDN 883
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
646-898 |
4.86e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 646 AEIKRLHNTIIDI---NNRKLKAQQNK--LDTINKQLDECASAITKAQVAIktadRNLKKAQDSVcrtekeikDTEKEIN 720
Cdd:COG3206 148 ELAAAVANALAEAyleQNLELRREEARkaLEFLEEQLPELRKELEEAEAAL----EEFRQKNGLV--------DLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 721 DLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEH--ALQKDALSIKLKLEQIDGHISEHNSKIKY 798
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 799 WQKEISKIKlhpvednpvetvAVLSQEELEAIknpESITNEIALLEAQCREMKpnlGAIAEYKKKEDLYLQRVAELDKIT 878
Cdd:COG3206 296 LRAQIAALR------------AQLQQEAQRIL---ASLEAELEALQAREASLQ---AQLAQLEARLAELPELEAELRRLE 357
|
250 260
....*....|....*....|
gi 1907152066 879 SERDNFRQAYEDLRkQRLNE 898
Cdd:COG3206 358 REVEVARELYESLL-QRLEE 376
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
602-797 |
6.06e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 602 QIKELEANVlttapdrkqQKLLEENvsvFKKEYDAVAEKAGKVEaeiKRLHNTIIDINNRKLKAQQNKLDTINKQLDECA 681
Cdd:pfam06160 212 QLEELKEGY---------REMEEEG---YALEHLNVDKEIQQLE---EQLEENLALLENLELDEAEEALEEIEERIDQLY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 682 SAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEI-----------------NDLKTELKNIEDKAEEVINNTKTAE 744
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELervqqsytlnenelervRGLEKQLEELEKRYDEIVERLEEKE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 745 TSLPEIQKEHRNLLQELKVIQENE-------HALQKDALSIKLKLEQIDGHISEHNSKIK 797
Cdd:pfam06160 357 VAYSELQEELEEILEQLEEIEEEQeefkeslQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
617-893 |
6.79e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 617 RKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTI--IDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTA 694
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIneISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 695 DRNLKKAQDSVCRTEKEIKDTEKEINDLKT---ELKNIEDKAEEVInntktaetslpEIQKEHRNLLQELKVIQENEHAL 771
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAEEYI-----------KLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 772 QKDALSIKLKLEQidghISEHNSKIKYWQKEISKIklhpvednpvetvavlsQEELEAIKNPESITNEIALLEAQCREMK 851
Cdd:PRK03918 320 EEEINGIEERIKE----LEEKEERLEELKKKLKEL-----------------EKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907152066 852 PNLG------AIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRK 893
Cdd:PRK03918 379 KRLTgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
602-747 |
8.12e-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: 42.22 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 602 QIKELEaNVLTTAPDRKQQklLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQnKLDTI--NKQLDE 679
Cdd:COG1579 18 ELDRLE-HRLKELPAELAE--LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVrnNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152066 680 CASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSL 747
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
590-772 |
1.05e-03 |
|
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: 43.20 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 590 QGLSEQEEYLCVQIKEL---EANVLTTAPDRKQQKLLEENVSVfKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKL-KA 665
Cdd:pfam07111 59 QALSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLEAQAM-ELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 666 QQNKLDTINKQLDECASAITKAQ----VAIKTADRNLKKAQDSV----CRTEKEIKDTEKEINDLKTELKNIEDKAEEVI 737
Cdd:pfam07111 138 SQRELEEIQRLHQEQLSSLTQAHeealSSLTSKAEGLEKSLNSLetkrAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907152066 738 NNTKT-----AETSLPEIQK-----EHRNLLQELKVIQENEHALQ 772
Cdd:pfam07111 218 TLVESlrkyvGEQVPPEVHSqtwelERQELLDTMQHLQEDRADLQ 262
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
643-1037 |
1.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 643 KVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQvaiKTADRNLKKAQDSVCRTEKEIKDTEKEINDL 722
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR---KKNGENIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 723 KTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHalqkdALSIKLKLEQIDGHISEHNSKIKYWQKE 802
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGV-----CPTCTQQISEGPDRITKIKDKLKELQHS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 803 ISKIKLHpvednpVETVAVLSQEELEAIKNPESITNEIALLEAQ-CREMKPNLGAIAEYKKKEDLYLQRVAELDKITSER 881
Cdd:PHA02562 315 LEKLDTA------IDELEEIMDEFNEQSKKLLELKNKISTNKQSlITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 882 DNFRQAYEDLRKQRlneFMAGFyvITNKLKE-------------------NYQMLTLGGDAELELVDSldpFSEGImfsv 942
Cdd:PHA02562 389 DKIVKTKSELVKEK---YHRGI--VTDLLKDsgikasiikkyipyfnkqiNHYLQIMEADYNFTLDEE---FNETI---- 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 943 rppKKSWKKIF---NLSGGEKTLSSLALVFA------LHHYKPTPLYFMDEI-DAALDFKNVSIVaFYIYEQTKNAQFII 1012
Cdd:PHA02562 457 ---KSRGREDFsyaSFSQGEKARIDLALLFTwrdvasKVSGVDTNLLILDEVfDGALDAEGTKAL-LSILDSLKDTNVFV 532
|
410 420
....*....|....*....|....*
gi 1907152066 1013 ISLRNNMFEISDRLIGIYKTYNSTK 1037
Cdd:PHA02562 533 ISHKDHDPQKFDRHLKMEKVGRFSV 557
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
116-369 |
1.18e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 116 TEKSNVL----SNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVqvrEKLKHATSKAKKLEKQLQKDKEKVEE 191
Cdd:PRK01156 464 EEKSNHIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 192 LKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETqgLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD 271
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 272 IYLSRHNTAVSQLSKAK---EALITASETL--------------KERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEI 334
Cdd:PRK01156 619 KSIREIENEANNLNNKYneiQENKILIEKLrgkidnykkqiaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
250 260 270
....*....|....*....|....*....|....*
gi 1907152066 335 NLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQ 369
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
651-868 |
1.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 651 LHNTIIDINNRKLKAQQNKLDTINKQLDE-CASAITKAQVAIKTAD---RNLKKAQDSVCRTEKEIKDTEKEINDLKTEL 726
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 727 KNIED--KAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHalqkdalsiklKLEQIDGHISEHNSKIKYWQKEIS 804
Cdd:COG4717 119 EKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152066 805 KIKLHPVEDNpVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYL 868
Cdd:COG4717 188 LATEEELQDL-AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
654-728 |
2.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907152066 654 TIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKN 728
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
45-372 |
2.29e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 45 RGEKLNRVKMVEKEKDALEgEKNIAIEFLTlENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSN 124
Cdd:TIGR00606 507 QNEKADLDRKLRKLDQEME-QLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 125 EMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHA------TSKAKKLEKQLQKDKEKVEELKSVPAK 198
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEKSSKQRAMLAGATAV 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 199 SKTVINETTTRNNS---LEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIY-- 273
Cdd:TIGR00606 665 YSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKek 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 274 --------LSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTK---LPQTQQELKEKEKELQKLTQE--EINLKSLV 340
Cdd:TIGR00606 745 eipelrnkLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKlqGSDLDRTV 824
|
330 340 350
....*....|....*....|....*....|..
gi 1907152066 341 HDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKK 372
Cdd:TIGR00606 825 QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
545-753 |
2.34e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 545 SQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTapdRKQQKLLE 624
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 625 ENVSVFKKEYD---AVAEKAGKVEAEIKRLHNTIIDINNRKL-------KAQQNKLDTINKQLDECASAITKAQVAIKTA 694
Cdd:COG4942 97 AELEAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152066 695 DRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKE 753
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
547-807 |
2.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 547 LERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQglseqEEYLCVQIKELEanvlttapdRKQQKLLEEN 626
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE---------EKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 627 VSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDIN--NRKLKAQQNKLDTINKQLDECASAITKAQV-AIKTADRNLKKAQD 703
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEP 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 704 ------SVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNllQELKVIQENEHALQKDALS 777
Cdd:PRK03918 600 fyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAG 677
|
250 260 270
....*....|....*....|....*....|
gi 1907152066 778 IKLKLEQIDGHISEHNSKIKYWQKEISKIK 807
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
537-911 |
2.50e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 537 VEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSE-RDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVlttAP 615
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL---SL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 616 DRKQQKLLEE-------NVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKqldecasaITKAQ 688
Cdd:pfam15921 396 EKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK--------VSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 689 VAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEdKAEEVINNTKTAETSLPEIQKEHrnlLQELKVIQENE 768
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKLQE---LQHLKNEGDHL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 769 HALQKDALSIKLKLEQIDGHISEHNSKIKYWQK------------EISKIKLHP-VEDNPVE--TVAVLSQEELEAIKNP 833
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKeINDRRLElqEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152066 834 ESITNEIALLEAQ-CREMKPNLGAIAEYKKKEDlylQRVAELDKITSERDNFRQAYEDLRKQRLNEfMAGFYVITNKLK 911
Cdd:pfam15921 624 EARVSDLELEKVKlVNAGSERLRAVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRNFRNK-SEEMETTTNKLK 698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
93-332 |
2.53e-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: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 93 DLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEkftqldledvqvreklkhat 172
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 173 sKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEiqekelmgf 252
Cdd:COG4942 91 -EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 253 nkSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKealitasetlKERKAAIKDINTKLPQTQQELKEKEKELQKLTQE 332
Cdd:COG4942 161 --ELAALRAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
534-892 |
4.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 534 EISVEEVNKMESQLERHSKQAMQIQEQkvqhEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTT 613
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 614 APDRK----QQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQqNKLDTINKQLDECASAITKAQV 689
Cdd:PRK02224 306 DADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR-EEAAELESELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 690 AIKTadrnlkkaqdsvcrTEKEIKDTEKEINDLKTELKNIEDKAEEVINN-------TKTAETSLPEIQK---EHRNLLQ 759
Cdd:PRK02224 385 EIEE--------------LEEEIEELRERFGDAPVDLGNAEDFLEELREErdelrerEAELEATLRTARErveEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 760 ELKV------IQENEHA------------LQKDALSIKLKLEQIDGHIsEHNSKIKYWQKEISKIKlhpvedNPVETVav 821
Cdd:PRK02224 451 AGKCpecgqpVEGSPHVetieedrerveeLEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLE------ERREDL-- 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152066 822 lsqEELEAIKnpESITNEIALLEAQCREMKPNLGAIAEYKKKE--------DLYLQRVAELDKITSERDNFRQAYEDLR 892
Cdd:PRK02224 522 ---EELIAER--RETIEEKRERAEELRERAAELEAEAEEKREAaaeaeeeaEEAREEVAELNSKLAELKERIESLERIR 595
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
36-325 |
4.52e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 36 RRVEILNEHRGEKLNRVKMVEKEKDAL--EGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITtqKEKIHEDTK 113
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLT--KEKVEKLNA 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 114 EITEKSNVLSnemKAKNSAVKDVEKK-LNKVTKFIEQNKEKftqlDLEDVQVREKLKHATS-KAKKLEKQLQKDKEKVEE 191
Cdd:PTZ00108 1110 ELEKKEKELE---KLKNTTPKDMWLEdLDKFEEALEEQEEV----EEKEIAKEQRLKSKTKgKASKLRKPKLKKKEKKKK 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 192 LKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD 271
Cdd:PTZ00108 1183 KSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSS 1262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152066 272 IYLSRHN---TAVSQLSKAKEALITASETLKERK-------AAIKDINTKLPQTQQELKEKEKE 325
Cdd:PTZ00108 1263 DDLSKEGkpkNAPKRVSAVQYSPPPPSKRPDGESnggskpsSPTKKKVKKRLEGSLAALKKKKK 1326
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
54-335 |
4.95e-03 |
|
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: 40.71 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 54 MVEKEKDALEGEKNIAIEFLTLENEMFKKKNHIcqyyiydLQNRIAEITTQKEKIHEDTKEIteksnvlsnEMKAKNSAV 133
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN-------ANNLIKQFENTKEKIAEYTKSI---------DIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 134 KDVEKKLNKVTKFIEQNKEKFTQLDledvQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSL 213
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQ----NLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 214 EKEREKEEKKLKEVMDSLKQetqgLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD-----IYLSRHNTAVSQLSKAK 288
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILAT----LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeliseLNKVMREADEESQSRLE 466
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907152066 289 EALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEIN 335
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLE 513
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
545-787 |
5.75e-03 |
|
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: 40.49 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 545 SQLERHSKQamQIQEQKVQHEEAVVKLRHSERDMRNTLEK---FAASIQGLSEQEEylcvqikELEANVLTTAPDRKQQK 621
Cdd:pfam05557 12 SQLQNEKKQ--MELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREA-------EAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 622 LLEENVSVFKKEYDAVAEKAGKVEAEIK---RLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKtadrNL 698
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKnelSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 699 KKAQDSVCRTEKEIKDTEKEI---NDLKTELKNIEDKAEevinntktaetSLPEIQKEHRNLLQE---LKVIQENEHALQ 772
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELEFEIqsqEQDSEIVKNSKSELA-----------RIPELEKELERLREHnkhLNENIENKLLLK 227
|
250
....*....|....*
gi 1907152066 773 KDALSIKLKLEQIDG 787
Cdd:pfam05557 228 EEVEDLKRKLEREEK 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
170-355 |
5.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 170 HATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekerekeekklkevMDSLKQETQGLQKEKEIQEKEL 249
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE------------------YNELQAELEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 250 MGFNKSVNEARSKME----------VAQSELDIYLSRHN--------TAVSQLSKAKEALI----TASETLKERKAAIKD 307
Cdd:COG3883 75 AEAEAEIEERREELGeraralyrsgGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLeelkADKAELEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907152066 308 INTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLA 355
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
602-735 |
7.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 602 QIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAE------KAGKVEAEIKRLHNTIidinnRKLKAQQNKLDTINK 675
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAEL-----ERLDASSDDLAALEE 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 676 QLDEcasaitkAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEE 735
Cdd:COG4913 693 QLEE-------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
8-376 |
7.98e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 8 TEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKL-NRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKnhi 86
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLiQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER--- 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 87 cqyYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMkaknsaVKDVEKKLNKVTKfIEQNKEKftqLDLEDVQVRE 166
Cdd:COG5022 883 ---QLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDL------IENLEFKTELIAR-LKKLLNN---IDLEEGPSIE 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 167 klKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSlekerekeekklkevMDSLKQETQGLQKEKEIQE 246
Cdd:COG5022 950 --YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSE---------------LKNFKKELAELSKQYGALQ 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 247 KELmgfnKSVNEARSKMEVAQSELDIYLSRHnTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEK-E 325
Cdd:COG5022 1013 EST----KQLKELPVEVAELQSASKIISSES-TELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQlE 1087
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907152066 326 LQKLTQEEINLKSLvhdLFQKVEEAKSS--LAMNRSRGKVLDAIIQEKKSGRI 376
Cdd:COG5022 1088 STENLLKTINVKDL---EVTNRNLVKPAnvLQFIVAQMIKLNLLQEISKFLSQ 1137
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
26-827 |
8.07e-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: 40.42 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 26 RLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEgEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAeITTQK 105
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQ-EHIRARDSLIQSLATRLELDGFERGPFSERQIKNF-HTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 106 EKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLekqLQKD 185
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI---LELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 186 KEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDslkQETQGLQKEKEIQEKELMgfnksvnEARSKMEV 265
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD---QEMEQLNHHTTTRTQMEM-------LTKDKMDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 266 AQSELDIYLSRHNTAVSQL------SKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSL 339
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 340 VHD-------------LFQKVEEAKSSLAMNRSRGKVLDAIIQE---KKSGRIPgiygrlgdLGAIDEKYDIAISSCCHA 403
Cdd:TIGR00606 628 LFDvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVYSQFITQltdENQSCCP--------VCQRVFQTEAELQEFISD 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 404 LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRL----FDLVKVKNEEIRQAFYFALRDT 479
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqkvnRDIQRLKNDIEEQETLLGTIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 480 LVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEisVEEVNKMESQLERHSKqAMQIQE 559
Cdd:TIGR00606 780 EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK--QHELDTVVSKIELNRK-LIQDQQ 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 560 QKVQHEEAVVKLRHSERdmrNTLEKFAASIQGLSEQEEYLCVQIKEL---------EANVLTTAPDRKQQKLLE------ 624
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEK---LQIGTNLQRRQQFEEQLVELSTEVQSLireikdakeQDSPLETFLEKDQQEKEElisske 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 625 ENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNL--KKAQ 702
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQ 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 703 DSVCRTEKEIKDTEKEINDLKTELKNiedkaeeviNNTKTAETSLPEIQKEHRNLLQELKVIQENEhalqkdalsiklkl 782
Cdd:TIGR00606 1014 ERWLQDNLTLRKRENELKEVEEELKQ---------HLKEMGQMQVLQMKQEHQKLEENIDLIKRNH-------------- 1070
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1907152066 783 EQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEEL 827
Cdd:TIGR00606 1071 VLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
583-1037 |
8.40e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 583 EKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFK-KEYDAVAEKAGKVEAEIKRLHNTIIDINNR 661
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELKDK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 662 KLKAQQnkldtinkqLDECASAITKAQVAIKTADRNLKKAQdsvcRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTK 741
Cdd:PRK01156 545 HDKYEE---------IKNRYKSLKLEDLDSKRTSWLNALAV----ISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFP 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 742 TAET----SLPEIQKEHRNLLQELKVIQENehalqkdalsiKLKLEQIDGhisehnsKIKYWQKEISKIKlhPVEDNPVE 817
Cdd:PRK01156 612 DDKSyidkSIREIENEANNLNNKYNEIQEN-----------KILIEKLRG-------KIDNYKKQIAEID--SIIPDLKE 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 818 TVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKkkedlylQRVAELDKITSERDNFRQAYEDLRKQRLN 897
Cdd:PRK01156 672 ITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS-------DRINDINETLESMKKIKKAIGDLKRLREA 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 898 EFMAGFYVITNKLKENYqMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSW-KKIFNLSGGEKTLSSLALVFALHHY-- 974
Cdd:PRK01156 745 FDKSGVPAMIRKSASQA-MTSLTRKYLFEFNLDFDDIDVDQDFNITVSRGGMvEGIDSLSGGEKTAVAFALRVAVAQFln 823
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152066 975 KPTPLYFMDEIDAALDFKNVS----IVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTK 1037
Cdd:PRK01156 824 NDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSK 890
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
545-888 |
9.47e-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: 40.01 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 545 SQLERHSKQAMQIQEQKVQHEEAVVKLRHSERD---------MRNTLEKFAASIQGLSEQEEYLCVQIKELeANVLTTAP 615
Cdd:pfam05667 207 SLLERNAAELAAAQEWEEEWNSQGLASRLTPEEyrkrkrtklLKRIAEQLRSAALAGTEATSGASRSAQDL-AELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 616 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIkrLHNTIIDINNRKLKaQQNKLDTINKQLDECASAITKAqvaiktad 695
Cdd:pfam05667 286 GSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSS--PPTKVETEEELQQQ-REEELEELQEQLEDLESSIQEL-------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 696 rnlkkaqdsvcrtekeikdtEKEINDLKTELKNIEDKAEEvinnTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDA 775
Cdd:pfam05667 355 --------------------EKEIKKLESSIKQVEEELEE----LKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 776 LSIKLKLEQIDGHISEHNSKIkywqkeISKIKLHPVEdnpvetvavLSQEELEAiknpESITNEIALLEAQCREMkpnlg 855
Cdd:pfam05667 411 DASAQRLVELAGQWEKHRVPL------IEEYRALKEA---------KSNKEDES----QRKLEEIKELREKIKEV----- 466
|
330 340 350
....*....|....*....|....*....|...
gi 1907152066 856 aIAEYKKKEDLYLQRVAELDKITseRDNFRQAY 888
Cdd:pfam05667 467 -AEEAKQKEELYKQLVAEYERLP--KDVSRSAY 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
669-903 |
9.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 669 KLDTINKQLDECASAITKAQVAIktadrnlkkaqdsvcrteKEIKDTEKEINDLKTELKNIEDKAEEVInNTKTAETSLP 748
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERL------------------EALEAELDALQERREALQRLAEYSWDEI-DVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 749 EIQKEHRNLLQ---ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEI--SKIKLHPVEDNPVETVAVLS 823
Cdd:COG4913 672 ELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152066 824 QEELEAIKNP-------ESITNEIALLEAQCREMKPNL-GAIAEYKKKEDLYLQRV-----------AELDKITSER-DN 883
Cdd:COG4913 752 EERFAAALGDaverelrENLEERIDALRARLNRAEEELeRAMRAFNREWPAETADLdadleslpeylALLDRLEEDGlPE 831
|
250 260
....*....|....*....|
gi 1907152066 884 FRQAYEDLRKQRLNEFMAGF 903
Cdd:COG4913 832 YEERFKELLNENSIEFVADL 851
|
|
| |
