|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-135 |
4.02e-42 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 149.33 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 2 KAYLKSADGFFVLN-KSTTIGKHaDSDLVLQdhlvrgqhhpqwpgpstsiinqehapppglctcrsdaeSADIDNHHALI 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQ--------------------------------------SPGVEEQHAVI 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 81 EFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGSAGMTYELVIEN 135
Cdd:cd22700 42 EYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGDVLRFGFGGLPYELVVDN 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-1011 |
1.75e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.96 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 323 DDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAItsgmvtsLQKDMSARNEQVQQLQEEVN 402
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 403 RLRIENREKEYQLEALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 478
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 479 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDK-----PITDQQRQH 553
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 554 LRACIPPHRARTCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQR---KWTLQRE--THLHPKQEETMHS 628
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSglSGILGVLSELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 629 VEKLR-------------VLLDKCQACMRDscssIDLKKEVELLQHLPLsPLVSGLQKTVVNILRVSLSWLEETEQLLGD 695
Cdd:TIGR02168 532 DEGYEaaieaalggrlqaVVVENLNAAKKA----IAFLKQNELGRVTFL-PLDSIKGTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 696 LDielsDSDKGFSLCLIYLLEHYKKIMS--QSQDLQAQMNAS---------------RETQKSLRQEH--LAEKEKLAEK 756
Cdd:TIGR02168 607 LV----KFDPKLRKALSYLLGGVLVVDDldNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSsiLERRREIEEL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 757 LEQEEKLKAKIQQLTEEKAALEesigQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMREMLEAERRKAQ 836
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 837 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI-----ELKEQKENVLN--NKLKDALVMVEDAQ 909
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraELTLLNEEAANlrERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 910 QMKTTESQRAETLAL---KLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 986
Cdd:TIGR02168 838 RRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740
....*....|....*....|....*
gi 1720409130 987 VSLEERLCQVTQYYQKIEGEITTLK 1011
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-981 |
7.93e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 265 EVNRLSDFEMESKYKDA--LIMNLQAEVADLSQRL---------SETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESM 333
Cdd:TIGR02168 270 EELRLEVSELEEEIEELqkELYALANEISRLEQQKqilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 334 KSQINALQKGYSqVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENRE--- 410
Cdd:TIGR02168 350 KEELESLEAELE-ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllk 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 411 --KEYQLEALSSRCSVMKEELRKEEAQKDRREAQ----EKELKLCRSQMQDMEKEVRKLR------EELKKNYMGQNIIS 478
Cdd:TIGR02168 429 klEEAELKELQAELEELEEELEELQEELERLEEAleelREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGV 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 479 KTLREKNK--------VEEKLQEDSR-RKLLQLQEMGNRENLIKINLERAVGQLENFR-NQVIKATF-------GKTKPF 541
Cdd:TIGR02168 509 KALLKNQSglsgilgvLSELISVDEGyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKqNELGRVTFlpldsikGTEIQG 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 542 RDKPITDQQRQHLRACIPPhraRTCAPTLQSLprragcleTSYCLSSGQLIEKIIQVTED--NLSFQQRKWTLQREThLH 619
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDL---VKFDPKLRKA--------LSYLLGGVLVVDDLDNALELakKLRPGYRIVTLDGDL-VR 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 620 P------KQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKevellqhlplsplvsglqkTVVNILRVSLSWLEETEQLL 693
Cdd:TIGR02168 657 PggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELE-------------------KALAELRKELEELEEELEQL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 694 GDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEE 773
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 774 KAALeesigqeksrsEEALEKAQARVRELENHLASQKEALENSVAQekrkmremLEAERRKAQDLENQLTQQKEISENNT 853
Cdd:TIGR02168 798 LKAL-----------REALDELRAELTLLNEEAANLRERLESLERR--------IAATERRLEDLEEQIEELSEDIESLA 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 854 YEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAEL 933
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1720409130 934 ETTKTKMiltDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 981
Cdd:TIGR02168 939 DNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
724-1216 |
1.05e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 724 QSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEksrsEEALEKAQARVRELE 803
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 804 NHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENntyeklkmRDTLEKEKRKIQDLENRLTKQKEE 883
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 884 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKmILTDDRLKLQQQSMKALQDERES 963
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA-LAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 964 QKHGFEEEISEYKEQIKQHSQTIV-------------SLEERLCQVTQYY-----QKIEGEITTLKNNDTG-----PKEE 1020
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAvavligveaayeaALEAALAAALQNIvveddEVAAAAIEYLKAAKAGratflPLDK 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1021 ASQDLTAGPPLDSGDKEIACDhLIDDLLMAQKEILSQQEIIMKLRT----DLGEAHSRMSDLRGELSEK---QKMELERQ 1093
Cdd:COG1196 582 IRARAALAAALARGAIGAAVD-LVASDLREADARYYVLGDTLLGRTlvaaRLEAALRRAVTLAGRLREVtleGEGGSAGG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1094 VALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSF 1173
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1720409130 1174 QEEQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEKAN 1216
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN 783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
252-1110 |
4.02e-15 |
|
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: 81.17 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 252 QQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRlsetaavaAARQSNRCDPKLQGVDEGDDLRQKEIE 331
Cdd:pfam02463 183 ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--------YLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 332 SMKSQINALQKGYSQVLsQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIE-NRE 410
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVL-KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKElKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 411 KEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymGQNIISKTLREKNKVE-- 488
Cdd:pfam02463 334 KEEIEELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS---AAKLKEEELELKSEEEke 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 489 -EKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRA---CIPPHRAR 564
Cdd:pfam02463 407 aQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKetqLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 565 TCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQRKWTLQ-----RETHLHPKQEETMHSVEKLRVLLDKC 639
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGvavenYKVAISTAVIVEVSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 640 QACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGdldiELSDSDKGFSLCLIYLLEHYK 719
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR----AKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 720 KIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE----EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 795
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEkaesELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 796 QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ--KEISENNTYEKLKMRDTLEKEKRKIQDL 873
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKekELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 874 ENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQS 953
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 954 MKalqDERESQKHGFEEEISEYKEQIKQHSQTIVSLEErlcqvtqyyqKIEGEITTLKNNDTGPKEEasqdltagPPLDS 1033
Cdd:pfam02463 883 KL---KDELESKEEKEKEEKKELEEESQKLNLLEEKEN----------EIEERIKEEAEILLKYEEE--------PEELL 941
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 1034 GDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRgELSEKQKMELERQVALVRQQSGELSMLKAK 1110
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE-ERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-941 |
2.89e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 262 LGREVNRLSDFEMeskykdaliMNLQAEVADLS--QRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINA 339
Cdd:TIGR02169 277 LNKKIKDLGEEEQ---------LRVKEKIGELEaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 340 LQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLE--- 416
Cdd:TIGR02169 348 ERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAdln 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 417 -----------ALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTL 481
Cdd:TIGR02169 427 aaiagieakinELEEEKEDKALEIKKQEWKleqlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 482 REKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGqleNFRNQVIKATFGKTKpfrdKPIT-DQQRQHLRACIPP 560
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAK----EAIElLKRRKAGRATFLP 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 561 HRARTCAPTLQSLPRRAGCLETSYCLSS-GQLIEKII-QVTEDNLSFQQ-----------RKWTLQREThlhpkqeetmh 627
Cdd:TIGR02169 580 LNKMRDERRDLSILSEDGVIGFAVDLVEfDPKYEPAFkYVFGDTLVVEDieaarrlmgkyRMVTLEGEL----------- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 628 sVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHL--PLSPLVSGLQKTvvnilrvslswLEETEQLLGDLDIELSDSDK 705
Cdd:TIGR02169 649 -FEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERleGLKRELSSLQSE-----------LRRIENRLDELSQELSDASR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 706 GFSLcliyllehykkIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ-E 784
Cdd:TIGR02169 717 KIGE-----------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 785 KSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRK--MREMLEAERRKAQDLENQLTQQK-----EISENNTyEKL 857
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlEKEYLEKEIQELQEQRIDLKEQIksiekEIENLNG-KKE 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 858 KMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAEtlalkLKETLAELETT 936
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrKRLSELKAKLEA-----LEEELSEIEDP 939
|
....*
gi 1720409130 937 KTKMI 941
Cdd:TIGR02169 940 KGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-1132 |
7.06e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 330 IESMKSQINALQKgysqvlsQtlAERNTEIESLKNEGENLkrDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENR 409
Cdd:TIGR02168 195 LNELERQLKSLER-------Q--AEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 410 EKEYQLEALSSRCSVMKEELrkeeaqkdrrEAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEE 489
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEI----------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 490 KLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRAcipphRARTCAPT 569
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-----EIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 570 LQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSfqqrkwTLQRETH-LHPKQEETMHSVEKLRVLLDKCQACMRDSCS 648
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELE------ELEEELEeLQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 649 SID-LKKEVELLQHLPLSplVSGLQKTVVNILRvSLSWLEETEQLLGDLdIElsdSDKGFSLCL-IYLLEHYKKIMS--- 723
Cdd:TIGR02168 483 ELAqLQARLDSLERLQEN--LEGFSEGVKALLK-NQSGLSGILGVLSEL-IS---VDEGYEAAIeAALGGRLQAVVVenl 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 724 ----QSQDLQAQMNASRETQKSLRQEHLAEKE-KLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRS------EEAL 792
Cdd:TIGR02168 556 naakKAIAFLKQNELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddlDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 793 EKA-----QARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEklkMRD 861
Cdd:TIGR02168 636 ELAkklrpGYRIVTLDGDLVRpggvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE---LEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 862 TLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmi 941
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE------ 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 942 ltddrlklQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNdtgpKEEA 1021
Cdd:TIGR02168 787 --------LEAQIEQLKEELKAL----REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1022 SQDLtAGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLR-------TDLGEAHSRMSDLRGELSEKQ----KMEL 1090
Cdd:TIGR02168 851 SEDI-ESLAAEIEELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRELEELReklaQLEL 929
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 1091 ERQVALVR----------QQSGELSMLKAKVAQTTGLMEKKDRELKVLREAL 1132
Cdd:TIGR02168 930 RLEGLEVRidnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
752-993 |
1.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 752 KLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEAlENSVAQEKRKMREMLEAE 831
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEA----ELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 832 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQM 911
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----EEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 912 KTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 991
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
..
gi 1720409130 992 RL 993
Cdd:COG1196 464 LL 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
736-1023 |
1.95e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 736 RETQKSLR--QEHLA-------EKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG----QEKSRSEEALEKAQARVREL 802
Cdd:TIGR02168 175 KETERKLErtRENLDrledilnELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 803 ENHLASQKEALENSVAQEKRKMREM----------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD 872
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 873 LENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 952
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 953 SMKALQDERESQKHGFEE-EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 1023
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
754-1028 |
2.94e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 754 AEKLEQEEKLKAKIQQLTEEKAALE--------ESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMR 825
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 826 EMLEAERRKAQdLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 905
Cdd:COG1196 289 EEYELLAELAR-LEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 906 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQT 985
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720409130 986 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAG 1028
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-877 |
3.85e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 287 QAEVA----DLSQRLSETAAVAAARQsnrcdpklqgvdegDDLRQKEIESMKSQINALQKGySQVLSQTLAERNTEIESL 362
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK--------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 363 KNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQ 442
Cdd:COG1196 273 RLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 443 EKELKLCRSQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQ 522
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 523 LENFRNQVIKAtfgktkpfRDKPITDQQRQHLRACippHRARTCAPTLQSLPRRAGCLEtsyclSSGQLIEKIIQVTEDN 602
Cdd:COG1196 423 LEELEEALAEL--------EEEEEEEEEALEEAAE---EEAELEEEEEALLELLAELLE-----EAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 603 LSFQQRKWTLQREthlhpkQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTV------- 675
Cdd:COG1196 487 AEAAARLLLLLEA------EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVeddevaa 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 676 ------------------VNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRE 737
Cdd:COG1196 561 aaieylkaakagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 738 TQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsv 817
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL--- 717
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 818 aQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRL 877
Cdd:COG1196 718 -EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
735-1011 |
6.46e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 735 SRETQKSLR-QEHLAEKEKLA--EKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKE 811
Cdd:TIGR02169 204 RREREKAERyQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 812 ALENSVAQEKRKMREmLEAERRKAQD----LENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK 887
Cdd:TIGR02169 284 LGEEEQLRVKEKIGE-LEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 888 EQKENVLNNKLKDalvMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHG 967
Cdd:TIGR02169 363 KEELEDLRAELEE---VDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 968 FEE-------EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 1011
Cdd:TIGR02169 439 LEEekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
749-1148 |
6.57e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 749 EKEKLAEKLEQEEKLKAKIQQL---TEEKAALEESI--GQEKSRSEEALEKAQARvRELENhlaSQKEALENSVAQEKRK 823
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKkkAEEAKKADEAKKKAEEA-KKAEE---AKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 824 MREmleaERRKAQDLENQLTQQKEISEN--NTYEKLKMRDTLEK--EKRKIQDLENRLTKQKEEiELKEQKENVLNNKLK 899
Cdd:PTZ00121 1478 KAE----EAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 900 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 979
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 980 KQHSQTIVSLEERLCQVTQYyqKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQK-EILSQQ 1058
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaEELKKK 1710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1059 EIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGElsmlKAKVAQTTGLMEKKDRELK-----VLREALR 1133
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRkekeaVIEEELD 1786
|
410
....*....|....*
gi 1720409130 1134 ASQEKPRPHLSTEQK 1148
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-131 |
1.45e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.90 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 12 FVLNKS-TTIGKHADSDLVLQDHLVrgqhhpqwpgpstsiinqehapppglctcrsdaeSAdidnHHALIEFNEaeGTFV 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTV----------------------------------SR----RHARIRRDG--GGWV 55
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720409130 91 LQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYEL 131
Cdd:COG1716 56 LEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELRFRL 95
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-122 |
3.00e-11 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 60.28 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 18 TTIGKHADSDLVLQDhlvrgqhhpqwpgpstsiinqehapppglctcrsdaesADIDNHHALIEFNEaEGTFVLQDFNSR 97
Cdd:pfam00498 1 VTIGRSPDCDIVLDD--------------------------------------PSVSRRHAEIRYDG-GGRFYLEDLGST 41
|
90 100
....*....|....*....|....*
gi 1720409130 98 NGTFVNECHIQNVAVKLIPGDILRF 122
Cdd:pfam00498 42 NGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-130 |
3.38e-11 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 60.75 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 11 FFVLNKSTTIGKHADSDLVLQDHLVRGqhhpqwpgpstsiinqehapppglctcrsdaesadidnHHALIEFNEaeGTFV 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSR--------------------------------------RHARIEVDG--GGVY 53
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720409130 91 LQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYE 130
Cdd:cd00060 54 LEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFRFE 92
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
677-1111 |
3.80e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 677 NILRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEK 756
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 757 LEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaqarvrELENHLASQKEALENSVAQekrkmremLEAERRKAQ 836
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK------ELKSELKNQEKKLEEIQNQ--------ISQNNKIIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 837 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLEN----------RLTKQKEEIELKEQKENVLNNKLKDALVMVE 906
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKenqsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 907 DAQQMKTTESQRAETLALKLKETLAELETTKTKMILT----DDRLKLQQQSMKALQDERESQKHGFEE----------EI 972
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 973 SEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIACDHL---IDDLLM 1049
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE---LKKENLEKEIDEKnkeIEELKQ 575
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 1050 AQKEILSQQEiimKLRTDLGEAHSRMSDLRGELSEK--QKMELERQVALVRQQSGELSMLKAKV 1111
Cdd:TIGR04523 576 TQKSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKekKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-884 |
4.34e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 251 SQQDKDEIILLLGREVNRLSDFEMESKYKDAL---IMNLQAEVADLSQRLSETAAVAAARqsnrcdpklqgVDEGDDlRQ 327
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAET-----------RDELKD-YR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 328 KEIESMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIE 407
Cdd:TIGR02169 392 EKLEKLKREINELKRELDR-LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 408 NREKEYQLEALSSRCSVMKEELRKEEAQkdrreaqekelklcRSQMQDMEKEVRKLREELKKNYMGqniISKTLREKNKV 487
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQ--------------ARASEERVRGGRAVEEVLKASIQG---VHGTVAQLGSV 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 488 EEKLQ----------------ED----------------SRRKLLQLQEM-GNRENLIKINLERAVGQLEN-------FR 527
Cdd:TIGR02169 534 GERYAtaievaagnrlnnvvvEDdavakeaiellkrrkaGRATFLPLNKMrDERRDLSILSEDGVIGFAVDlvefdpkYE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 528 NqVIKATFGKTKPFRD----KPITDQQRQ-----------------HLRACIPPHRARTCAPTLQSLPRRAGCL--ETSY 584
Cdd:TIGR02169 614 P-AFKYVFGDTLVVEDieaaRRLMGKYRMvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLkrELSS 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 585 CLSSGQLIEKIIQVTEDNLSFQQRKW-TLQRETHLHPKQEETMHS-VEKLRVLLDKCQACMRDSCSSI-DLKKEVELLQ- 660
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELkELEARIEELEe 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 661 -----HLPLSPLVSGLQKTVVNILRVSLSWLEET----EQLLGDLDIELSDSDkgfslcliyLLEHYKKimSQSQDLQAQ 731
Cdd:TIGR02169 773 dlhklEEALNDLEARLSHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLT---------LEKEYLE--KEIQELQEQ 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 732 MNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENHLAS 808
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSE 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 809 QKEALENSVAQEK----------------------RKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE 866
Cdd:TIGR02169 922 LKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
730
....*....|....*...
gi 1720409130 867 KRKIQDLENRLTKQKEEI 884
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
682-1137 |
9.27e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 682 SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKsLRQEHLAEKEKLAEKLEQEE 761
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK-KLKELEKRLEELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 762 KLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQ 841
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCPVCGRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 842 LTQQKEISENNTYeKLKMRDtLEKEKRKIQDLENRLTKQKEEIELKEQKENVLnnklkdaLVMVEDAQQMKTTESQRAET 921
Cdd:PRK03918 445 LTEEHRKELLEEY-TAELKR-IEKELKEIEEKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 922 LALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD------ERESQKHGFEEEISEYKEQIKQHS-QTIVSLEERLC 994
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 995 QVTQYYQkiegEITTLKNndtGPKEeasqdltagppLDSGDKEIacDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSR 1074
Cdd:PRK03918 596 ELEPFYN----EYLELKD---AEKE-----------LEREEKEL--KKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1075 MSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQT-------TGLMEKKDRELKVLREALRASQE 1137
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTleklkeeLEEREKAKKELEKLEKALERVEE 725
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
716-1075 |
1.14e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 716 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ--EEKLKAK-IQQLTEEKAALEESI--GQEKSRSEE 790
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEeAKKKAEEAKKADEAKkkAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 791 ALEKAQ---ARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK-- 865
Cdd:PTZ00121 1488 AKKKAEeakKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKae 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 866 EKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVE------------DAQQMKTTESQRAETLALKLKETLAEL 933
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeakkaeeakiKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 934 ETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYK-EQIKQHSQTIVSLEERLCQVTQYYQKIEG-----EI 1007
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaeEE 1727
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 1008 TTLKNNDTGPKEEASQDLTAGPPLDSGDKEiACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRM 1075
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
70-131 |
7.31e-10 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 57.33 E-value: 7.31e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409130 70 SADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGMTYEL 131
Cdd:cd22704 32 SRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-1092 |
1.16e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 292 DLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLK 370
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 371 RDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsvMKEELRKEEAQKDRREAQEKELKLCR 450
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 451 SQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKveekLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQV 530
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDY---REKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 531 ------IKATFGKTKPFRDKpITDQQRQHLRacipphrartcaptlqslprragcletsyclssgqlIEKIIQVTEDNLS 604
Cdd:TIGR02169 444 edkaleIKKQEWKLEQLAAD-LSKYEQELYD------------------------------------LKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 605 FQQRKWTlQRETHLHPKQEETMHSVEKLRVLldkcqacmRDSCSSI-----DLKKEVELLQHLPLSPLVSGLQKTVV--- 676
Cdd:TIGR02169 487 KLQRELA-EAEAQARASEERVRGGRAVEEVL--------KASIQGVhgtvaQLGSVGERYATAIEVAAGNRLNNVVVedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 677 -------------NILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQsqdlqaqmnASRETQkslr 743
Cdd:TIGR02169 558 avakeaiellkrrKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKY---------VFGDTL---- 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 744 qehlaekekLAEKLEQEEKLKAKIQQLTEEKAALEES-----------IGQEKSRSEEA-LEKAQARVRELENHLAS--- 808
Cdd:TIGR02169 625 ---------VVEDIEAARRLMGKYRMVTLEGELFEKSgamtggsraprGGILFSRSEPAeLQRLRERLEGLKRELSSlqs 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 809 QKEALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE 885
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 886 LKEQKENVLNNKLKDALVmvedaqQMKTTESQRAETLALKLKETLAELET-----TKTKMILTDDR---------LKLQQ 951
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRI------PEIQAELSKLEEEVSRIEARLREIEQklnrlTLEKEYLEKEIqelqeqridLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 952 QSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSL-------EERLCQVTQYYQKIEGEITTLKNND---TGPKEEA 1021
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkerdelEAQLRELERKIEELEAQIEKKRKRLselKAKLEAL 929
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 1022 SQDLTA-GPPLDSGDKEIACDHLIDDLLMA----QKEILSQQEIIMKLRTDLGEAHSRMSDLRgelSEKQKMELER 1092
Cdd:TIGR02169 930 EEELSEiEDPKGEDEEIPEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDELK---EKRAKLEEER 1002
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
737-1023 |
1.38e-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: 62.73 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEAlekaQARVRELEnhlaSQKEALEn 815
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKEnQSYKQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQ----QEKELLE- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 816 svaQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 895
Cdd:TIGR04523 426 ---KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 896 NK----------LKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTD---------DRLKLQQQSMKA 956
Cdd:TIGR04523 503 EEkkeleekvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeiEELKQTQKSLKK 582
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 957 LQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 1023
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
748-1100 |
1.81e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 748 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEkAQARVRELENHLasqkealensVAQEKRKMREM 827
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYE----------LLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 828 LEAERRKAQDLENQLTQ-QKEISENNTyEKLKMRDTLEKEKRKIQDL-ENRLTKQKEEIELKEQKENVLNNKLKDALVMV 905
Cdd:TIGR02169 239 KEAIERQLASLEEELEKlTEEISELEK-RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 906 EDAQ-QMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQ 981
Cdd:TIGR02169 318 EDAEeRLAKLEAEIDKLLA-EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 982 HSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltagppldsgdkeiacdhLIDDLLMAQKEILSQQEII 1061
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-------------------LEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1720409130 1062 MKLRTDLGEAHSRMSDLRGELS--EKQKMELERQVALVRQQ 1100
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDrvEKELSKLQRELAEAEAQ 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
740-1232 |
1.99e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 740 KSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENH------LASQK 810
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEELkeeieeLEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 811 EALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKEISEN-NTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIE 885
Cdd:PRK03918 248 ESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKaEEYIKLsEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 886 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKM-ILTDDRLKLQQQSMKALQDERESQ 964
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 965 KHGFEEEISEYKEQIKQHSQTIVSLE--ERLCQV-----------------TQYYQKIEGEITTLKNNDTGPKEEASQdl 1025
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKkaKGKCPVcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1026 tagppldsgdkeiacdhlIDDLLMAQKEILSQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELS 1105
Cdd:PRK03918 485 ------------------LEKVLKKESELIKLKELAEQLK----ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1106 MLKAKVAQTTGLMEKKDRELKVLREAlrasqEKPRPHLSTEQKPRTLSQKCDISLQI---EPAHPDSFSSFQEEQSFSDL 1182
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLkelEPFYNEYLELKDAEKELERE 617
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 1183 GVKCKGSRHE-----ETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELR 1232
Cdd:PRK03918 618 EKELKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS 672
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
716-1334 |
2.98e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 716 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ-EEKLKAKIQQLTEEKAALEES--IGQEKSRSEEAL 792
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 793 EKAQ---ARVRELENHLASQKEALE-NSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENNTYEKLKMRdtlEKEKR 868
Cdd:PTZ00121 1398 KKAEedkKKADELKKAAAAKKKADEaKKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 869 KIQDLENRLTKQKEEIELKEQKENVLN--NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDR 946
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 947 LKLQQQSMKALQDERESQKHGFEEEiseyKEQIKQHSQTIVSLEERlcqvtqyyqKIEGEITTLKNNDTGPKEEASQDLT 1026
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEA---------RIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1027 AGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEiimKLRTDLGEAHSRMSDL-RGELSEKQKMELERQVALVRQQSGELS 1105
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1106 MLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSF-QEEQSFSDLGV 1184
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLkKEEEKKAEEIR 1774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1185 KCKGSRHEETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELRTLR-MEKNVQKILLDAKpdltTLARVEIRPPQ 1263
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKeMEDSAIKEVADSK----NMQLEEADAFE 1850
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 1264 NSPFNSGSTLVMEKSVKTDAGEALELSEK-----LYTDMIKTLgslmNIKDMSSHTSLKHLSPKEREKVNHLRQKD 1334
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDdeeeiEEADEIEKI----DKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
723-934 |
6.50e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 723 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVREL 802
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 803 ENHLASQKEALENSVA---QEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 879
Cdd:COG4942 96 RAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 880 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETL---ALKLKETLAELE 934
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLE 233
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
747-1011 |
7.75e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 747 LAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEES-IGQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMR 825
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYeLLKEKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 826 EMLEAERRKAQDL--ENQLTQQKEISENnTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENVLN-----NK 897
Cdd:TIGR02169 272 QLLEELNKKIKDLgeEEQLRVKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDkLLAEIEELEReieeeRK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 898 LKDALV-MVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYK 976
Cdd:TIGR02169 351 RRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270
....*....|....*....|....*....|....*
gi 1720409130 977 EQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 1011
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-530 |
1.07e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 252 QQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAvaaarQSNRCDPKLQGVDEGDDLRQKEIE 331
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-----RLEEAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 332 SMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREK 411
Cdd:TIGR02168 793 QLKEELKALREALDE-LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 412 EYQLEALSSRCSVMKEELrkeEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIsktlreKNKVEEKL 491
Cdd:TIGR02168 872 ESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL------EVRIDNLQ 942
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720409130 492 QEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQV 530
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
716-1409 |
1.49e-08 |
|
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: 59.75 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 716 EHYKKIMS----QSQDLQAQMNASREtqkslrqehLAEKEKLAEKlEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA 791
Cdd:pfam15921 74 EHIERVLEeyshQVKDLQRRLNESNE---------LHEKQKFYLR-QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 792 LEKAQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTlekekrKIQ 871
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 872 DLENRLTKQKEEIELKEqkenvlnNKLKDALVMVEDAQQMKTTESQRAETLAL-----KLKETLAELETTKTKMILTDDR 946
Cdd:pfam15921 217 SLGSAISKILRELDTEI-------SYLKGRIFPVEDQLEALKSESQNKIELLLqqhqdRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 947 LKLQQQSmkaLQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ----KIEGEITTLKNNDTGPKEEAS 1022
Cdd:pfam15921 290 ARSQANS---IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdkieELEKQLVLANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1023 QDltagpPLDSGDKEIACDHLIDDLLMAQKEILSQQE--------------IIMKLRTDLGEAH---SRMSDLRGELSEK 1085
Cdd:pfam15921 367 QF-----SQESGNLDDQLQKLLADLHKREKELSLEKEqnkrlwdrdtgnsiTIDHLRRELDDRNmevQRLEALLKAMKSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1086 QKMELERQVALVRQQSGEL---SMLKAKVAQTTGLMEKKDRELKVLREALRAS-----------QEKPRPHLSTEQKPRT 1151
Cdd:pfam15921 442 CQGQMERQMAAIQGKNESLekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSertvsdltaslQEKERAIEATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1152 LSQKCDISLQiEPAHPDSfssfqEEQSFSDLGVKCKGSRHE--------ETIQRQRKALSEL-----RTR-VRELEKANS 1217
Cdd:pfam15921 522 LRSRVDLKLQ-ELQHLKN-----EGDHLRNVQTECEALKLQmaekdkviEILRQQIENMTQLvgqhgRTAgAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1218 CNHKDHVNESFLELRTLRMEKNVQKILLDAKPDLTTLARVEIRPPQNSPFNSGSTLVMEK-----SVKTDAGEALELSEK 1292
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERdqllnEVKTSRNELNSLSED 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1293 LYT----------DMIKTLGSL-MNIKDMSSHTSLKHLSPKERE-------KVNHLRQKDLDLVFDKITQLKTRLQRKEE 1354
Cdd:pfam15921 676 YEVlkrnfrnkseEMETTTNKLkMQLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 1355 LLKGYEQELEQLRIEERIRSRETCPTAPSKTMRSRDACLLRWSRARCRTQVSRLE 1409
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
734-964 |
1.58e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 734 ASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLAS---QK 810
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAElekEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 811 EALENSVAQEKRKMREMLeaerRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 890
Cdd:COG4942 93 AELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 891 ENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQ 964
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
715-981 |
2.55e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNasRETQKSLRQEHLA-EKEKLAEKLEQEEKlKAKIQQLTEEKAALE--------------- 778
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMD--RQAAIYAEQERMAmERERELERIRQEER-KRELERIRQEEIAMEisrmrelerlqmerq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 779 ---ESIGQE-------KSRSEEALEKAQARVRELENHLASQKEALENSVAQ-EKRKMREMleaERRKAQDLENQltQQKE 847
Cdd:pfam17380 389 qknERVRQEleaarkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREM---ERVRLEEQERQ--QQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 848 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENVLNNKLKDALV--MVEDAQQMKTTESQRAETlalk 925
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLekEMEERQKAIYEEERRREA---- 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 926 lketlaelETTKTKMILTDDRLKLQQQSMKAlqDERESQKHGFEEEiSEYKEQIKQ 981
Cdd:pfam17380 539 --------EEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMERE-REMMRQIVE 583
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
686-978 |
2.70e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 57.77 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 686 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkiMSQSQDLQAQMNASRETQKSLRQE--HLAEKEKLAEKLEQE--- 760
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEEnkALREEAQAAEKALQRaeg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 761 ------------EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQ--------- 819
Cdd:pfam19220 161 elatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 820 -EKRKMREMLEAERRKAQDLENQLTQQkeisenntyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKL 898
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEA--------------RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 899 KDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRlklqqqsMKALQDERESQKHGFEEEISEYKEQ 978
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDR-------IAELTKRFEVERAALEQANRRLKEE 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
715-1154 |
8.53e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAKIQQ---LTEEKAALEESIGQEKSRSE 789
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKLLQllpLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 790 EaLEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRK 869
Cdd:COG4717 150 E-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 870 IQDLENRLTKQKEEIELKEQKE----------------NVLNNKLKDA--------LVMVEDAQQMKTTESQRAETLALK 925
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 926 LKETLAELETTKTKMILTDDRLK-----------------LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSqtIVS 988
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPpdlspeellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEAGVED--EEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 989 LEERLCQVTQyYQKIEGEITTLKNNdtgpkeeasqdltagppLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL 1068
Cdd:COG4717 387 LRAALEQAEE-YQELKEELEELEEQ-----------------LEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1069 GEAHSRMSDLRGELSEkqkMELERQVALVRQqsgELSMLKAKVAQttglMEKKDRELKVLREALRASQEkprpHLSTEQK 1148
Cdd:COG4717 449 EELREELAELEAELEQ---LEEDGELAELLQ---ELEELKAELRE----LAEEWAALKLALELLEEARE----EYREERL 514
|
....*.
gi 1720409130 1149 PRTLSQ 1154
Cdd:COG4717 515 PPVLER 520
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
73-130 |
9.52e-08 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 51.08 E-value: 9.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 73 IDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAGMTYE 130
Cdd:cd22665 40 VSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVKCQYV 97
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-991 |
1.23e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 404 LRIENREKEYQ-----LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniIS 478
Cdd:PRK03918 155 LGLDDYENAYKnlgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 479 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIK-----IN--------LERAVGQLENFRNQviKATFGKTKPFRDKP 545
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIReleerIEelkkeieeLEEKVKELKELKEK--AEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 546 ITDQQRQHLRACIPPHRARTCAPTLQ---SLPRRAGCLETSYclssGQLIEKIIQVTEDNLSFQQRKWTLQRETHLhpKQ 622
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKeleEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKEELERL--KK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 623 EETMHSVEKLRVLLDKCQacmrdscssiDLKKEVElLQHLPLSPLVSGLqKTVVNILRVSLSWLEETEQLLGDLDIELSD 702
Cdd:PRK03918 380 RLTGLTPEKLEKELEELE----------KAKEEIE-EEISKITARIGEL-KKEIKELKKAIEELKKAKGKCPVCGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 703 SDKGfslcliYLLEHYKKIMSqsqDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG 782
Cdd:PRK03918 448 EHRK------ELLEEYTAELK---RIEKELKEIEEKERKLRKE-LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 783 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRK---MREMLEAERRKAqDLENQLTQQKEISENNTYEKLKM 859
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELA-ELLKELEELGFESVEELEERLKE 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 860 RDTLEKE-------KRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTES-QRAETLALKLKETLA 931
Cdd:PRK03918 597 LEPFYNEylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 932 ELETTKtkmiltdDRLKLQQQSMKALQDERESQKhgfeEEISEYKEQIKQHSQTIVSLEE 991
Cdd:PRK03918 677 GLRAEL-------EELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEE 725
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
737-1214 |
1.46e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHlASQKEALENS 816
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA-EEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 817 VAQEKRKMREMLEA--ERRKAQDLENQLTQQKEISE--NNTYEKLKMRDTLEK---EKRKIQDLENRLTKQKEEIELKEQ 889
Cdd:PTZ00121 1373 KEEAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEAKKkaeEKKKADEAKKKAEEAKKADEAKKK 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 890 KENvlNNKLKDALVMVEDAQqmKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFE 969
Cdd:PTZ00121 1453 AEE--AKKAEEAKKKAEEAK--KADEAKKKAEEAKKADEAKKKAEEAKKKA----DEAKKAAEAKKKADEAKKAEEAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 970 EEISEYKEQIKQHsqtivslEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltagpplDSGDKEIAcdhliddllM 1049
Cdd:PTZ00121 1525 DEAKKAEEAKKAD-------EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK--------AEEDKNMA---------L 1580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1050 AQKEILSQQE---IIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELK 1126
Cdd:PTZ00121 1581 RKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1127 VLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahpdsfssfqEEQSFSDLGVKCKGSRHEETIQRQRKALSELR 1206
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
....*...
gi 1720409130 1207 TRVRELEK 1214
Cdd:PTZ00121 1730 IKAEEAKK 1737
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
737-1001 |
1.60e-07 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 55.84 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRqehlAEKEKLAEKLEQEEKL-KAKIQQLTEEKAALEEsigqEKsrseealEKAQARVRELENHLASQKEALEN 815
Cdd:pfam15070 4 ESLKQLQ----TERDQYAENLKEEGAVwQQKMQQLSEQVRTLRE----EK-------ERSVSQVQELETSLAELKNQAAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 816 SVAQEKRKMREMLEAERRKAQDLEnQLTQQKEISENNTYEKLKMRDTL-----EKEKRkIQDLENRLTKQKEEIELKEQk 890
Cdd:pfam15070 69 PPAEEEQPPAGPSEEEQRLQEEAE-QLQKELEALAGQLQAQVQDNEQLsrlnqEQEQR-LLELERAAERWGEQAEDRKQ- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 891 envlnnklkdalvMVEDAQQMKTTESqRAETLALKLKETLAELETTKTKmiLTDDRLKLqqqsMKALQDERESQKH---- 966
Cdd:pfam15070 146 -------------ILEDMQSDRATIS-RALSQNRELKEQLAELQNGFVK--LTNENMEL----TSALQSEQHVKKElakk 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720409130 967 --GFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 1001
Cdd:pfam15070 206 lgQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQ 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
789-943 |
2.14e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 789 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAE----RRKAQDLENQLTQQKEISENNTyeklkmrDTLE 864
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRKL-------ELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 865 KEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV-----EDAQQM---KTTESQRAETLAL-KLKETLAELET 935
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEA 186
|
....*....
gi 1720409130 936 TKT-KMILT 943
Cdd:PRK12704 187 DKKaKEILA 195
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
737-1214 |
2.57e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQqltEEKAALEESIGQEKSRSEEALEKAQARvRELENHLASQKEALENS 816
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFAR-RQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 817 VAQEKRKMREMLEA-ERRKAQDLENQLTQQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 895
Cdd:PTZ00121 1285 KAEEKKKADEAKKAeEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 896 NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiltddrlklqqqsmKALQDERESQKHGFEEEISEY 975
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK-----------------KAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 976 KEQIKQHSQTIVSLEErlcqvtqyyqkiegeiTTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQKEIL 1055
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADE----------------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1056 SQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLME--KKDRELKVLREALR 1133
Cdd:PTZ00121 1484 KADEAKKKAE----EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1134 ASQEKPRPHLSTEQKPRTLS-QKCDISLQIEPAHPDSFSSFQEEQSFSDlGVKCKGSRHEETIQRQRKALSELRTRVREL 1212
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEEKKMK-AEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
..
gi 1720409130 1213 EK 1214
Cdd:PTZ00121 1639 KK 1640
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
728-924 |
2.61e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 728 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLA 807
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE----ELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 808 -----SQKEALENSVAQEKRKMREMLEAE------RRKAQDLENQLTQ-QKEISENNTYEKLKMRDTLEKEKRKIQDLEN 875
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLeelrelEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720409130 876 RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAL 924
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
346-955 |
2.80e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 346 QVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKE---------YQLE 416
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhihtlqQQKT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 417 ALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKlreELKKNYMGQNIISKTLREKNKVEEKLQEDSR 496
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 497 RKLLQLQEMGNRENLIKinLERAVGQLENFRNQVIKatfgktkpfrdkpitDQQRQHLRACIPPHRARTCAPTLQSLPRR 576
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHL--QETRKKAVVLARLLELQ---------------EEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 577 AGCLETSYclssGQLIEKIIQVTEDNLSFQQRKWTLQREthlhpkQEETMHSVEKLRVLLDkcqacmRDSCSSIDLKKEV 656
Cdd:TIGR00618 530 MQRGEQTY----AQLETSEEDVYHQLTSERKQRASLKEQ------MQEIQQSFSILTQCDN------RSKEDIPNLQNIT 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 657 ELLQHlpLSPLVSGLQKTVVNILRVSlswLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkimsqsqDLQAQMNASR 736
Cdd:TIGR00618 594 VRLQD--LTEKLSEAEDMLACEQHAL---LRKLQPEQDLQDVRLHLQQCSQELALKLTALH---------ALQLTLTQER 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHLaEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESigQEKSRSEEALEKAQAR-VRELENHLASQKEALEn 815
Cdd:TIGR00618 660 VREHALSIRVL-PKELLASRQLALQKMQSEKEQLTYWKEMLAQC--QTLLRELETHIEEYDReFNEIENASSSLGSDLA- 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 816 svaQEKRKMREMLEAERRKAQDlenQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 895
Cdd:TIGR00618 736 ---AREDALNQSLKELMHQART---VLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 896 NKLKDALVMVEDAQQmktTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK 955
Cdd:TIGR00618 810 QEIPSDEDILNLQCE---TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
714-1068 |
3.13e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 714 LLEHYKKIMSQSQDLQAQMNASRETQK----SLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRS 788
Cdd:pfam02463 131 SPEAYNFLVQGGKIEIIAMMKPERRLEieeeAAGSRLKRKKKEALKKLIEEtENLAELIIDLEELKLQELKLKEQAKKAL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 789 EEALEKAQARVREL-------ENHLASQKEALE---NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLK 858
Cdd:pfam02463 211 EYYQLKEKLELEEEyllyldyLKLNEERIDLLQellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 859 MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKT 938
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 939 KMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIkQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPK 1018
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL-ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1019 EEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL 1068
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
727-901 |
3.76e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 727 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA---LEKAQARVRELE 803
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 804 NH-----LASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyeklkmrdTLEKEKRKIQDLENRLT 878
Cdd:COG3206 289 NHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA--------------QLEARLAELPELEAELR 354
|
170 180
....*....|....*....|...
gi 1720409130 879 KQKEEIELKEQKENVLNNKLKDA 901
Cdd:COG3206 355 RLEREVEVARELYESLLQRLEEA 377
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
723-890 |
3.99e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 723 SQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL 802
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 803 ENH------------------LASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 864
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 1720409130 865 KEKRKIQDLENRLTKQKEEIELKEQK 890
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-124 |
4.15e-07 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 49.22 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 12 FVLNKST-TIGKHADSDLVLQDHLVRGqhhpqwpgpstsiinqehapppglctcrsdaesadidnHHALIEFNEaeGTFV 90
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSS--------------------------------------RHARIYLQG--SSWY 52
|
90 100 110
....*....|....*....|....*....|....
gi 1720409130 91 LQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 124
Cdd:cd22693 53 LEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
723-1370 |
4.21e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 723 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkakiqqltEEKAALEESIGQEKSRSEEALEKAQARV--R 800
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK----------EEEKEKKLQEEELKLLAKEEEELKSELLklE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 801 ELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKiqdLENRLTKQ 880
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL---EEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 881 KEEIELKEQKENVLNNKLKDALVMvEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 960
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 961 RESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIAC 1040
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ-----KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1041 DHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSmlkakVAQTTGLMEK 1120
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE-----IDPILNLAQL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1121 KDRELKVLREALRAsqekprphlsteqKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQRK 1200
Cdd:pfam02463 609 DKATLEADEDDKRA-------------KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1201 ALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPDLTTLARVEIrPPQNSPFNSGSTLVMEKSVK 1280
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-NEELKLLKQKIDEEEEEEEK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1281 T--DAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLdlvfDKITQLKTRLQRKEELLKG 1358
Cdd:pfam02463 755 SrlKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK----EEAELLEEEQLLIEQEEKI 830
|
650
....*....|..
gi 1720409130 1359 YEQELEQLRIEE 1370
Cdd:pfam02463 831 KEEELEELALEL 842
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
353-977 |
5.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 353 AERNTEIESLKNEGENLKR-DHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRK 431
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 432 EEAQKDRREAQEK----ELKLCRSQMQDMEKEVRKLREELKKNYMGQNI---ISKTLREKNKVEEKLQEDSRRKllQLQE 504
Cdd:PTZ00121 1378 KKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAKK--KAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 505 MGNRENLIKINLE-RAVGQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRACIPPHRARTCAPTlqslpRRAGCLETS 583
Cdd:PTZ00121 1456 AKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-----KKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 584 yclssgqliEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQACMRdscssIDLKKEVELLQHLP 663
Cdd:PTZ00121 1531 ---------EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEE 1596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 664 LSPLVSGLQKTVVNILRVSLSWLEETEQLLGDldielsdsdkgfslcliyllEHYKKIMSQSQDLQAQMNASRETQKSLR 743
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--------------------EEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 744 QEHLAEKEKLAEKLEQEEKlkaKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQ---KEALENSVAQE 820
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIKAE 1733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 821 KRKMREmlEAERRKAQDL------ENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 894
Cdd:PTZ00121 1734 EAKKEA--EEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 895 NNKLKDALVmVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiLTDDRLKLQQQSMKALQDERESQKHGFEEEISE 974
Cdd:PTZ00121 1812 EGGKEGNLV-INDSKEMEDSAIKEVADSKNMQLEEADAFEKHK----FNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
...
gi 1720409130 975 YKE 977
Cdd:PTZ00121 1887 ADE 1889
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
755-991 |
6.39e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 755 EKLEQ-EEKLKAKIQQLTEEKAALEEsIGQEKSRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMLEAE 831
Cdd:pfam05483 370 QRLEKnEDQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 832 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD---------LENRLTKQKEE---IELKEQKENVLNNKlK 899
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQEASdmtLELKKHQEDIINCK-K 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 900 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 979
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250
....*....|..
gi 1720409130 980 KQHSQTIVSLEE 991
Cdd:pfam05483 604 ENKNKNIEELHQ 615
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
388-983 |
7.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 388 SARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKlcrsQMQDMEKEVRKLREEL 467
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 468 KKNYMGQNIISKTL----REKNKVEEKLQEDSRRKlLQLQEMGNRENLIKINLERAVGQLENFrnqvikatfgktkpfrd 543
Cdd:PRK03918 303 EEYLDELREIEKRLsrleEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELY----------------- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 544 kpitdqqrqhlracippHRARTCAPTLQSLPRRAGCLETsyclssGQLIEKIIQVTEDNLSFQ-QRKWTLQRETHLHPKQ 622
Cdd:PRK03918 365 -----------------EEAKAKKEELERLKKRLTGLTP------EKLEKELEELEKAKEEIEeEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 623 EETMHSVEKLRVLLDKCQACMRDscssIDLKKEVELLQHLPLSplvsglqktvvniLRVSLSWLEETEQLLGDLDIELSD 702
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPVCGRE----LTEEHRKELLEEYTAE-------------LKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 703 SDKgfslcliyLLEHYKKIMSQsQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESi 781
Cdd:PRK03918 485 LEK--------VLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEIKSLKKELEKLEEL- 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 782 gqeKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLENQLTQQKEisenntyEKLKM 859
Cdd:PRK03918 555 ---KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEK-------ELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 860 RDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN-NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKT 938
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1720409130 939 KMILTDDRLKLQQQSMKALQDEResqkhgfeEEISEYKEQIKQHS 983
Cdd:PRK03918 705 EREKAKKELEKLEKALERVEELR--------EKVKKYKALLKERA 741
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
359-469 |
1.02e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.32 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 359 IESLKNEGENLKRDHAITsgMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL---RKEEAQ 435
Cdd:COG2433 382 LEELIEKELPEEEPEAER--EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseaRSEERR 459
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720409130 436 KDRREAQ----EKELKLCRSQMQDMEKEVRKLREELKK 469
Cdd:COG2433 460 EIRKDREisrlDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
736-963 |
1.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 736 RETQKSLRQEHLAEKEKLAEKLEQEEKLK---AKIQQLTEEKAALEESIGQEKSRSEEALEKAQArvrelenhLASQKEA 812
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEELIAERRETIEEKRERAEE--------LRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 813 LEnSVAQEKR----KMREMLEAERRKAQDLENQLTQQKEISEN-NTYEKL-----KMRDTLEKEKRKIQDLENRLTKQKE 882
Cdd:PRK02224 549 LE-AEAEEKReaaaEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLlaaiaDAEDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 883 EIELKEQKENVLNNKLKDAlvMVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 962
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEA--RIEEAREDK----ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE 701
|
.
gi 1720409130 963 S 963
Cdd:PRK02224 702 A 702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
731-1371 |
1.54e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 731 QMNASRETQKSLRQEHLAEKEKLAE--KLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS 808
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 809 QKEALENSVAQEKRKMREMLEAER-RKAQDLEnQLTQQKEISENNTYEKLKMRDTLEK--EKRKIQDLEnRLTKQKEEIE 885
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEvRKAEELR-KAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVK-KAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 886 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAEtlalklkETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQK 965
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-------EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 966 HGFEEEISEYKEQIKQHSQTIVSLEERlcqvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLid 1045
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1046 dllmaqKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMlKAKVAQTTGLMEKKDREL 1125
Cdd:PTZ00121 1384 ------KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1126 KVLREALRASQEKPRPHlSTEQKPRTLSQKCDISLQIEPA--HPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRqrkalS 1203
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAkkKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----A 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1204 ELRTRVRELEKANSCNHKDHVNESfLELRTLRMEKNVQKILLDAKPDLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDA 1283
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKA-EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1284 GEAL-ELSEKLYTDMIKtlgslmniKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITqlKTRLQRKEELLKGYEQE 1362
Cdd:PTZ00121 1610 EEAKkAEEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEE 1679
|
....*....
gi 1720409130 1363 LEQLRIEER 1371
Cdd:PTZ00121 1680 AKKAEEDEK 1688
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
715-991 |
1.89e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.60 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNA-SRETQKSLRQEHLAEKEKLAEKL--EQEEKLKAKIQQLTEEKAALEESIGQEKS--RSE 789
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINIlEMRLSETDARIKLAAQEKIHVEIleEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 790 EALEKAQARVreLENHLASQKEALENSVAQEKRkmREMLEAERRkaqDLENQL-TQQKEISENNTYEKlkmrDTLEKEKR 868
Cdd:PLN02939 235 NMLLKDDIQF--LKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 869 KIQDLENRLTKQKEEIELKEQKENVLNNKLKdalvmvedaqqmkttesqraetlalKLKETLAELETTKtkmiLTDDRLK 948
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVE 354
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720409130 949 LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 991
Cdd:PLN02939 355 LLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
49-219 |
2.16e-06 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 51.69 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 49 SIINQEHAPPPGLCTCRSDAESADI----DNH-------------HALIEFneAEGTFVLQDfNSRNGTFVNECHI---Q 108
Cdd:COG3456 6 RIINSPDLESGSAASATFGRGGGTIgrsaDCDwvlpdpdrsvsrrHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 109 NVAVKLIPGDILRFGSagmtYEL---VIENPSPVSCPWVRGPAPWPSPQPHLS--SSPPDMPFHHGIQPATVQRSWSQGC 183
Cdd:COG3456 83 GRPVRLRDGDRLRIGD----YEIrveISGEDEGADDPLAAAPEPAVSSPSNLSdtEAAPDAALAFSFSLDPLEALDEAAT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720409130 184 PRPTMVPPAPHQRPMSASGKMFSFVMDPKSPVINQV 219
Cdd:COG3456 159 EAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQL 194
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
748-934 |
2.79e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 748 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREM 827
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 828 LEAERR--------KAQDLE---NQLTQQKEISENNTyeklKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKenvLNN 896
Cdd:COG3883 96 YRSGGSvsyldvllGSESFSdflDRLSALSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALKAE---LEA 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720409130 897 KLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 934
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
729-992 |
2.79e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 729 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESIGQEKSRSEEALEKAQA--RVRELENH 805
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 806 LASQKEALE--NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK---EKRKIQDLENRLTKQ 880
Cdd:PTZ00121 1324 AEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 881 KEEI-ELK---EQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKET--LAELETTKTKMILTDDRLKLQQQSM 954
Cdd:PTZ00121 1404 KKKAdELKkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720409130 955 KALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEER 992
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
721-856 |
3.93e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.56 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 721 IMSQSQDLQAQMNASRETQKSlrQEHLaEKEKLAEKLEQEEKlKAKIQQLTEEKAALE---ESIGQEKSRSEEALEKAQA 797
Cdd:PTZ00491 659 ITTKSQEAAARHQAELLEQEA--RGRL-ERQKMHDKAKAEEQ-RTKLLELQAESAAVEssgQSRAEALAEAEARLIEAEA 734
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 798 RVRELEnhLASQKEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEIS--ENNTYEK 856
Cdd:PTZ00491 735 EVEQAE--LRAKALRIEAEAELEKLRKRQELELEYEQAQN-ELEIAKAKELAdiEATKFER 792
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
320-1136 |
4.44e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 320 DEGDDL--RQKEIESMKSQINALQ---------KGYSQVLSQTLAERNTEI-----ESLKNEGENLKRDHAITSGMVTSL 383
Cdd:TIGR00606 245 NELDPLknRLKEIEHNLSKIMKLDneikalksrKKQMEKDNSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDC 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 384 QKDMSARNEQVQQLQEEvnRLRIENREKEYQLEALSSRCSVMKEELRKEEAQ----------------------KDRREA 441
Cdd:TIGR00606 325 QRELEKLNKERRLLNQE--KTELLVEQGRLQLQADRHQEHIRARDSLIQSLAtrleldgfergpfserqiknfhTLVIER 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 442 QEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEM-GNRENLIKinLERAV 520
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLeGSSDRILE--LDQEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 521 GQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRacipphRARTCAPTLQSLPRRAGCLETSYCLS-----SGQLIEKI 595
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNEKADLDR------KLRKLDQEMEQLNHHTTTRTQMEMLTkdkmdKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 596 IQVTEDNLSFQ--QRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQAC--MRDSCSSIDLKKEVELLQHLPLSPLVSGL 671
Cdd:TIGR00606 555 KSRHSDELTSLlgYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLeqNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 672 QKTVVNILRV---------SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSL 742
Cdd:TIGR00606 635 QDEESDLERLkeeieksskQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 743 rqehlaekEKLAEKLEQEEKLkakIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEK- 821
Cdd:TIGR00606 715 --------ESELKKKEKRRDE---MLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEs 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 822 ------------RKMREMLEAERRKAQdlenQLTQQKEISENNTYEKLKmrdtlekekRKIQDLENRLTKQKEEIEL--- 886
Cdd:TIGR00606 784 akvcltdvtimeRFQMELKDVERKIAQ----QAAKLQGSDLDRTVQQVN---------QEKQEKQHELDTVVSKIELnrk 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 887 --KEQKENVLN-----NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD 959
Cdd:TIGR00606 851 liQDQQEQIQHlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 960 ERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQK-IEGEITTLK---NNDTGPKEEASQDL-TAGPPLDSG 1034
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNaqlEECEKHQEKINEDMrLMRQDIDTQ 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1035 DKeiacdhliddllmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQqsgELSMLKAKVAQT 1114
Cdd:TIGR00606 1011 KI--------------QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEE---NIDLIKRNHVLA 1073
|
890 900
....*....|....*....|..
gi 1720409130 1115 TGLMEKKDRELKVLREALRASQ 1136
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKELREPQ 1095
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
246-505 |
5.43e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 246 MDHDLSQQDKDEiillLGREVNRLSDFEMESKYKDALiMNLQAEVADLSQRLsetaavaaARQSNRCDPKLQGVD---EG 322
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM--------AMERERELERIRQEErkrEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 323 DDLRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDHAITSGMVTSLQKDMSARNEQVQQL 397
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 398 QEE----VNRLRIENREKEYQLEAL--------SSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLRE 465
Cdd:pfam17380 441 EEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720409130 466 ELKKNymgQNIISKTLREKNKVEE--KLQEDSRRKLLQLQEM 505
Cdd:pfam17380 521 EMEER---QKAIYEEERRREAEEErrKQQEMEERRRIQEQMR 559
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-539 |
5.52e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 326 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR 405
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 406 --IENREKEY--QLEAL--SSRCSVMKEELRKE----------------EAQKDRREAQEKELKLCRSQMQDMEKEVRKL 463
Cdd:COG4942 97 aeLEAQKEELaeLLRALyrLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 464 REELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTK 539
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
325-801 |
6.39e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 325 LRQKEIESMKSQINALQKGYSQV--LSQTLAERNTEIESLKNEGENLKRDHAITSGMVT--SLQKDMSARNEQVQQLQEE 400
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYaeLQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 401 VNRLRIEN---REKEYQLEALSSRCSVMKEELrkEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNymgQNII 477
Cdd:COG4717 148 LEELEERLeelRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA---QEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 478 SKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATF--------GKTKPFRDKPITDQ 549
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 550 QRQHLRAciPPHRARTCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEetmhsv 629
Cdd:COG4717 303 EAEELQA--LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA------ 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 630 eklrvLLDKCQACMRDscssiDLKKEVELLQHLplsplvsglqktvvnilrvslswlEETEQLLGDLDIELSDSDKGFSL 709
Cdd:COG4717 375 -----LLAEAGVEDEE-----ELRAALEQAEEY------------------------QELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 710 CLIYLLEHykKIMSQSQDLQAQMNASRETQKSLRQE---------HLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALees 780
Cdd:COG4717 421 LLEALDEE--ELEEELEELEEELEELEEELEELREElaeleaeleQLEEDGELAELLQELEELKAELRELAEEWAAL--- 495
|
490 500
....*....|....*....|.
gi 1720409130 781 igqekSRSEEALEKAQARVRE 801
Cdd:COG4717 496 -----KLALELLEEAREEYRE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
353-962 |
7.69e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 353 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALssrcsvmkeELRKE 432
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV---------EARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 433 EAQKDRREAQEkELKLCRSQMQDMEKEVRKLREELKKnymgQNIISKTLREKNKVEEKLQEDSRRKLlqlqemGNRENLI 512
Cdd:PRK02224 318 ELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADD----LEERAEELREEAAELESELEEAREAV------EDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 513 KInLERAVGQLEnfrnqvikatfgktKPFRDKPITDQQRQHLRACIPPHRARtcaptlqslprragcletsyclssgqli 592
Cdd:PRK02224 387 EE-LEEEIEELR--------------ERFGDAPVDLGNAEDFLEELREERDE---------------------------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 593 ekiiqvtednlsfqqrkwTLQRETHLHPKQEETMHSVEKLRVLLD--KCQACMrdscssidlkkevellQHLPLSPLVSG 670
Cdd:PRK02224 424 ------------------LREREAELEATLRTARERVEEAEALLEagKCPECG----------------QPVEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 671 lqktvvnilrvslswLEETEQLLGDLDIELSDsdkgfslcliyllehykkIMSQSQDLQAQMNASRETQKSLRQ-EHLAE 749
Cdd:PRK02224 470 ---------------IEEDRERVEELEAELED------------------LEEEVEEVEERLERAEDLVEAEDRiERLEE 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 750 KEKLAEKL--EQEEKLKAK---IQQLTEEKAALEESiGQEK----SRSEEALEKAQARVRELENHLASQKEALENSvaqe 820
Cdd:PRK02224 517 RREDLEELiaERRETIEEKrerAEELRERAAELEAE-AEEKreaaAEAEEEAEEAREEVAELNSKLAELKERIESL---- 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 821 kRKMREMLEAERRKAQDLENQLTQQKEISENNTYEklkmRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENvlnnkLKD 900
Cdd:PRK02224 592 -ERIRTLLAAIADAEDEIERLREKREALAELNDER----RERLAEKRERKRELEAEFDEARIE-EAREDKER-----AEE 660
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 901 ALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERE 962
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR----EALENRVEALEALYDEAE 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
714-900 |
8.08e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 714 LLEHYKKIMS---------QSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE------EKLKAKIQQLTEEKAALE 778
Cdd:COG4913 230 LVEHFDDLERahealedarEQIELLEPIRELAERYAAARER-LAELEYLRAALRLWfaqrrlELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 779 EsigqEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENN-- 852
Cdd:COG4913 309 A----ELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720409130 853 TYEKLK--MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKD 900
Cdd:COG4913 381 EFAALRaeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
734-920 |
1.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 734 ASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLASQKEA 812
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 813 LENSVAQEKRKMR---------------------EMLEAERRKAQDLENQLTQQKEISENntyEKLKMRDTLEKEKRKIQ 871
Cdd:COG3883 88 LGERARALYRSGGsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720409130 872 DLEnrltKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 920
Cdd:COG3883 165 ELE----AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
726-866 |
1.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 726 QDLQAQMNASRETQKSLRQEHLAEKEKLAE-KLEQEEKLKAKIQQLTEEKAALE----------ESIGQEKSRSEEALEK 794
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 795 AQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNtyekLKMRDTLEKE 866
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL----LALRDALAEA 452
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
69-123 |
1.18e-05 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 45.17 E-value: 1.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 69 ESADIDNHHALIEFnEAEGTFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 123
Cdd:cd22683 36 SDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
734-1237 |
1.30e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 734 ASRETQKSLRQEHLAEKEKLAEkLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELE------NHL 806
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 807 ASQKEALENsvaqEKRKMREMLEAERRKAQDLENQ---LTQQKEISENNTYEKLKMRDTLEKEkrkIQDLENRLTKQKEE 883
Cdd:PRK02224 313 EARREELED----RDEELRDRLEECRVAAQAHNEEaesLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 884 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmilTDDRLKLQQQsmkaLQDERES 963
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT-------ARERVEEAEA----LLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 964 QKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNndtgpkeeasqdltagppLDSGDKEIacDHL 1043
Cdd:PRK02224 455 PECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED------------------LVEAEDRI--ERL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1044 IDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQK--MELERQVALVRQQSGELSMLKA----------KV 1111
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaAEAEEEAEEAREEVAELNSKLAelkeriesleRI 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1112 AQTTGLMEKKDRELKVLREALRASQEKprphlsTEQKPRTLSQKCDISLQIEPAHPDsfSSFQEEQSfsdlgvkcKGSRH 1191
Cdd:PRK02224 595 RTLLAAIADAEDEIERLREKREALAEL------NDERRERLAEKRERKRELEAEFDE--ARIEEARE--------DKERA 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720409130 1192 EETIQRQRKALSELRTRVRELEKANSCnhkdhVNESFLELRTLRME 1237
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGA-----VENELEELEELRER 699
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
674-804 |
1.33e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.86 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 674 TVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLqaqMNASRETQKSLRQEHLAEKEKL 753
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE---LDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 754 AEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA-------LEKAQARVRELEN 804
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKLLQS 285
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
741-964 |
1.35e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 741 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQ---------LTEEKAALEESiGQEKSRSEEALEKAQARVRELEN---HLAS 808
Cdd:pfam09787 4 SAKQELADYKQKAARILQSKEKLIASLKEgsgvegldsSTALTLELEEL-RQERDLLREEIQKLRGQIQQLRTelqELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 809 QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLekeKRKIQDLENRLTKQKEEIELKE 888
Cdd:pfam09787 83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 889 QkenvlnnklkdalvmvEDAQQMKTTESQRAETLALKLKETLAE-LETTKTKMILTDDRLklqQQSMKALQDERESQ 964
Cdd:pfam09787 160 Q----------------SSSSQSELENRLHQLTETLIQKQTMLEaLSTEKNSLVLQLERM---EQQIKELQGEGSNG 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
719-893 |
1.44e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 719 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG------QEKSRSE--- 789
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralYRSGGSVsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 790 ----------------EALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEisennt 853
Cdd:COG3883 106 dvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEAQQA------ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720409130 854 yEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENV 893
Cdd:COG3883 179 -EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
743-1237 |
1.60e-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: 49.58 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 743 RQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLA--------------- 807
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqerinrarka 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 808 -------------SQKEALENSVAQEKRKMREML----------EAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 864
Cdd:TIGR00618 293 aplaahikavtqiEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 865 KEKrkiqDLENRLTKQKEEIELKEQKENVLNNKLKdalvmVEDAQQmKTTESQRAETLALKLKETLAELETTKTKMILTD 944
Cdd:TIGR00618 373 QQH----TLTQHIHTLQQQKTTLTQKLQSLCKELD-----ILQREQ-ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 945 DRLKLQQQSMKALQDERESQKhgFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQD 1024
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1025 LTAGPpldsgdkeiacdhLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGEL 1104
Cdd:TIGR00618 521 DNPGP-------------LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ-SFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1105 SMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLsQKCDISLQIEPAHPDSFSS--FQEEQSFSDL 1182
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL-QQCSQELALKLTALHALQLtlTQERVREHAL 665
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 1183 GVKCKGSRHEETIQRQRKAL-SELRTRVRELEKANSCNHKDH-VNESFLELRTLRME 1237
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLReLETHIEEYDREFNE 722
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
747-874 |
1.70e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 48.44 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 747 LAEKEKLAEKLEQEE----KLKAKIQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHLASQ 809
Cdd:pfam02841 154 LEERDKLEAKYNQVPrkgvKAEEVLQEFLQSKEAVEEAILQtdqaltakekaieAERAKAEAAEAEQELLREKQKEEEQM 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 810 KEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLE 874
Cdd:pfam02841 234 MEAQERSYQEHVKQLIEKMEAEREQLLA-EQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
729-836 |
1.79e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 729 QAQMNASRETQKSLRQehLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlas 808
Cdd:COG2268 223 AEEAELEQEREIETAR--IAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQ----- 295
|
90 100
....*....|....*....|....*...
gi 1720409130 809 QKEAlENSVAQEKRKMREMLEAERRKAQ 836
Cdd:COG2268 296 EKEA-EREEAELEADVRKPAEAEKQAAE 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
297-509 |
1.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 297 LSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRD 372
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 373 HAITSGMVTSLQKDMSARNE-----QVQQLQEEVNRLRIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELK 447
Cdd:COG3883 85 REELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 448 LCRSQMQDMEKEVRKLREELkknymgQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRE 509
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
64-123 |
1.85e-05 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 44.96 E-value: 1.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 64 CRSDAESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 123
Cdd:cd22724 30 CELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
686-847 |
1.89e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 686 LEETEQLLGDLDIELSDsdkgfslcLIYLLEHYKKIMSQSQDLQAQMNASRETQkSLRQEHLAEKEKLAEKLEQEEKLKA 765
Cdd:COG3206 221 LSELESQLAEARAELAE--------AEARLAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 766 KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRK--AQDLENQLT 843
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevARELYESLL 371
|
....
gi 1720409130 844 QQKE 847
Cdd:COG3206 372 QRLE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
700-1218 |
2.56e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 700 LSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK-----------IQ 768
Cdd:pfam15921 403 LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQlestkemlrkvVE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 769 QLTEEKAALEESIG---------QEKSRSEEA----LEKAQARV----RELEnHLASQKEALENSVAQ---------EKR 822
Cdd:pfam15921 483 ELTAKKMTLESSERtvsdltaslQEKERAIEAtnaeITKLRSRVdlklQELQ-HLKNEGDHLRNVQTEcealklqmaEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 823 KMREMLeaeRRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLenRLTKQKEEIELKEQKENV--------- 893
Cdd:pfam15921 562 KVIEIL---RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF--KILKDKKDAKIRELEARVsdlelekvk 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 894 LNNKLKDALVMVEDAQQ--------MKTTE------SQRAETLALKLKETLAELETT--KTKMILTDDRLKLQQ-----Q 952
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQerdqllneVKTSRnelnslSEDYEVLKRNFRNKSEEMETTtnKLKMQLKSAQSELEQtrntlK 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 953 SMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE---------------------RLCQVTQYYQKIEGEITTLK 1011
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtnankekhflkeeknklsqELSTVATEKNKMAGELEVLR 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1012 NNDTGPKEEASQDLTAgppLDSGDKEIA-CDHLIddllmaQKEilSQQEIIMKLRTDL------GEAHSRMSDLRGELSe 1084
Cdd:pfam15921 797 SQERRLKEKVANMEVA---LDKASLQFAeCQDII------QRQ--EQESVRLKLQHTLdvkelqGPGYTSNSSMKPRLL- 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1085 kQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRAS-QEKPRPHLS-TEQKPRTLS--------Q 1154
Cdd:pfam15921 865 -QPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSViNEEPTVQLSkAEDKGRAPSlgalddrvR 943
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 1155 KCDISLQIEPAHPDSFSSFqeeqsfsdlgVKCKGSRHEETIQRQRKALselrtRVRELEKANSC 1218
Cdd:pfam15921 944 DCIIESSLRSDICHSSSNS----------LQTEGSKSSETCSREPVLL-----HAGELEDPSSC 992
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
719-981 |
2.58e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 719 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 798
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 799 VrelenhlASQKEALENSVAQEKrkmremlEAERRKAQDLENQLTQQKEISENntyeklkmrdtlEKEKRKIQDLENRLT 878
Cdd:TIGR02794 123 E-------AKAKQAAEAKAKAEA-------EAERKAKEEAAKQAEEEAKAKAA------------AEAKKKAEEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 879 KQKEEIELKEQKENVLNNKLKdalvmvedAQQMKTTESQRAETLALKLKETLAELETTKTKMILT-DDRLKLQQQSMKAL 957
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAEEAKAK--------AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAElGDIFGLASGSNAEK 248
|
250 260
....*....|....*....|....
gi 1720409130 958 QDERESQKHGfeEEISEYKEQIKQ 981
Cdd:TIGR02794 249 QGGARGAAAG--SEVDKYAAIIQQ 270
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
719-981 |
2.80e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 719 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 798
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 799 VRELENHLASQKEalENSVAQEKRKMREMLEAERRKAQ------DLENQLTQQ-KEISenntyEKLKMRDTLEKEKRKIQ 871
Cdd:COG1340 91 REELDELRKELAE--LNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELVEKiKELE-----KELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 872 DLENRLTKQKEEI-ELKEQKENVLN--NKLKDALV-MVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRL 947
Cdd:COG1340 164 ELRAELKELRKEAeEIHKKIKELAEeaQELHEEMIeLYKEADELR----KEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1720409130 948 -KLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 981
Cdd:COG1340 240 rELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
672-933 |
3.13e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 672 QKTVVNILRVSLSWLEETEQLLGDLDielsdsdkgfslcliylleHYKKIMSQ----SQDLQAQMNASRETQKSLRqEHL 747
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAK-------------------QYQQVIDNfpklSAELRQQLNNERDEPRSVP-PNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 748 AEKEklaekLEQeEKLKAKIQQLTEEKAALEEsigQEKSR----SEEALEKAQARVRELENHLASQKEALENS---VAQE 820
Cdd:PRK10929 103 STDA-----LEQ-EILQVSSQLLEKSRQAQQE---QDRAReisdSLSQLPQQQTEARRQLNEIERRLQTLGTPntpLAQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 821 KRKMREMlEAERRKAQDLENQLTQqkeISENNTYEKLKMRDTLEKEKR-----KIQDLENRLTKQ-KEEIE--------L 886
Cdd:PRK10929 174 QLTALQA-ESAALKALVDELELAQ---LSANNRQELARLRSELAKKRSqqldaYLQALRNQLNSQrQREAEralestelL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 887 KEQKENV---------LNNKLKDALvmVEDAQQMKTTESQR--AETLALKLKETLAEL 933
Cdd:PRK10929 250 AEQSGDLpksivaqfkINRELSQAL--NQQAQRMDLIASQQrqAASQTLQVRQALNTL 305
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
76-123 |
3.40e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 43.86 E-value: 3.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1720409130 76 HHALIEFneAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 123
Cdd:cd22694 38 RHALLEF--DGDGWVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
76-123 |
3.44e-05 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 44.95 E-value: 3.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720409130 76 HHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDILRFG 123
Cdd:cd22679 52 NHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDIVQFG 102
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
67-131 |
3.94e-05 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 44.21 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 67 DAESADI--DNH-----HALIEF----NEAEGTFVLQ------DFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGMT 128
Cdd:cd22676 28 DRRVADIplDHPscskqHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLSTRE 107
|
...
gi 1720409130 129 YEL 131
Cdd:cd22676 108 YVL 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
745-995 |
4.00e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 745 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG-QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRk 823
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 824 mremLEAERRKAQDLENQLTQQkeISENNTyeklkmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDA-L 902
Cdd:COG4913 314 ----LEARLDALREELDELEAQ--IRGNGG--------------DRLEQLEREIERLERELEERERRRARLEALLAALgL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 903 VMVEDAQQMKTTESQRAETLAlKLKETLAELETTKtkmiltdDRLKLQQQsmkALQDERESQkhgfEEEISEYKEQIKQH 982
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE-ALEEELEALEEAL-------AEAEAALR---DLRRELREL----EAEIASLERRKSNI 438
|
250
....*....|...
gi 1720409130 983 SQTIVSLEERLCQ 995
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
751-952 |
4.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 751 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlaSQKEALENSVAQEKRKMREMLEA 830
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 831 ERRKAQDLENQLTQQKEISENNTYEKLKMR-DTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKDALVMVEDA 908
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERlEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720409130 909 QQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 952
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
727-1012 |
4.32e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.29 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 727 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESIGQE----------------KS 786
Cdd:PTZ00440 956 NLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILNKKIDDLikkqhddiielidkliKE 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 787 RSEEALEKAQARVRELEN--------HLASQKEALENSVAQEK-RKMREMLEAERRKAQDLENQLTQQKEISENNTY--- 854
Cdd:PTZ00440 1036 KGKEIEEKVDQYISLLEKmktklssfHFNIDIKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnad 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 855 -EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN----KLKDALVMVEDAQQMKTTESQRAETLALKLKET 929
Cdd:PTZ00440 1116 kEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESY 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 930 LAELETTKTKMILTD----DRLKLQQQSMKALQDERE----SQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 1001
Cdd:PTZ00440 1196 KKDIDQVKKNMSKERndhlTTFEYNAYYDKATASYENieelTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENN 1275
|
330
....*....|.
gi 1720409130 1002 KIEGEITTLKN 1012
Cdd:PTZ00440 1276 KMENALHEIKN 1286
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
726-907 |
4.53e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 726 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRsEEALEKAQARV---REL 802
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 803 ENhLASQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQKEISEnntyeklKMRDTLEKEKRKIQDLENRLTK 879
Cdd:COG1579 92 EA-LQKEIESLKRRISDLEDEILELmerIEELEEELAELEAELAELEAELE-------EKKAELDEELAELEAELEELEA 163
|
170 180 190
....*....|....*....|....*....|....
gi 1720409130 880 QKEEI------ELKEQKENVLNNKLKDALVMVED 907
Cdd:COG1579 164 EREELaakippELLALYERIRKRKNGLAVVPVEG 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
750-978 |
4.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 750 KEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqeksrseEALEKAQARVRELENHLASQKEalensvaqekrkmremLE 829
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEL--------DALQERREALQRLAEYSWDEID----------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 830 AERRKAQDLENQLTQqkeISENNtyeklkmrDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQ 909
Cdd:COG4913 665 SAEREIAELEAELER---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 910 -QMKTTESQRAETLALKLKETLAELETTKtkmILTDDRLKLQQQsMKALQDERESQKHGFEEEISEYKEQ 978
Cdd:COG4913 734 dRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-471 |
5.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 286 LQAEVADLSQRLSETAAVAAA---------RQSNRCDpKLQGVDEGD-DLR--QKEIESMKSQINALQKGYSQV--LSQT 351
Cdd:COG4913 615 LEAELAELEEELAEAEERLEAleaeldalqERREALQ-RLAEYSWDEiDVAsaEREIAELEAELERLDASSDDLaaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 352 LAERNTEIESLKNEGENLKRDHAitsgmvtSLQKDMSARNEQVQQLQEEVNrlRIENREKEYQLEALSSRCsvmkEELRK 431
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERF----AAALG 760
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720409130 432 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNY 471
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFNREW 800
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
76-129 |
5.75e-05 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 43.85 E-value: 5.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 76 HHALI-----EFNEAEG----TFVLQDFnSRNGTFVNECHIQNVA-VKLIPGDILRFGSAGMTY 129
Cdd:cd22667 42 KHATLtvlhpEANLSDPdtrpELTLKDL-SKYGTFVNGEKLKGGSeVTLKDGDVITFGVLGSKF 104
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
745-890 |
5.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 745 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR---SEEALEKAQARVRELENHLASQKEALENSVAQ-- 819
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARleaAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 820 EKRKMREM------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 890
Cdd:COG1579 84 NVRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
808-1030 |
6.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 808 SQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ-QKEIsenntyeklkmrDTLEKEkrkIQDLENRLTKQKEEIE- 885
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEAlQAEI------------DKLQAE---IAEAEAEIEERREELGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 886 -LKEQKENVLNNKLKDALVMVED-------AQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKAL 957
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESfsdfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409130 958 QDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 1030
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
45-133 |
6.71e-05 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 43.97 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 45 GPSTSIINQEHAPPPGLCTCRSDAESADIDNHHALIEFNEAEGTFV--LQDFNSRNGTFVNECHI-QNVAVKLIPGDILR 121
Cdd:cd22681 38 SPSCYLIGREKGESTEIVVADIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDVIT 117
|
90
....*....|..
gi 1720409130 122 FgSAGMTYELVI 133
Cdd:cd22681 118 F-SKSNDYELVF 128
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
736-886 |
6.93e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 736 RETQKSLRQEHLAEKEKLAEKLEQE-----EKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQK 810
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEE----EERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 811 EALENSVAQEKrkmREMLEAERRKAQDLENQLT-QQKEISENNTYEKLK-MRDTLEKEKRKIQDLENRLTKQKEEIEL 886
Cdd:pfam15709 433 QELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
64-131 |
7.29e-05 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438777 [Multi-domain] Cd Length: 106 Bit Score: 43.38 E-value: 7.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 64 CRSDAESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGMTYEL 131
Cdd:cd22725 30 CELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
441-873 |
7.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 441 AQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAV 520
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 521 GQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRACIPPHRARtcaptLQSLPRRAGCLETsyclssgqliekiiQVTE 600
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-----LKALREALDELRA--------------ELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 601 DNLSFQQRKWTLQREthlhpkqEETMHSVEKLRVLLDKcqacmrdscSSIDLKKEVELLQHLplsplvsglqktvvnilr 680
Cdd:TIGR02168 815 LNEEAANLRERLESL-------ERRIAATERRLEDLEE---------QIEELSEDIESLAAE------------------ 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 681 vslswLEETEQLLGDLDIELSDSDKGFSlcliYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE 760
Cdd:TIGR02168 861 -----IEELEELIEELESELEALLNERA----SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 761 EKLKAKIQQ----LTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKmrEMLEAER 832
Cdd:TIGR02168 932 EGLEVRIDNlqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERY--DFLTAQK 1009
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1720409130 833 RKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDL 873
Cdd:TIGR02168 1010 EDLTEAKETL--EEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-837 |
8.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 383 LQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALS--SRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEV 460
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 461 RKLREELKknymgqniisktlREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVikatfgktKP 540
Cdd:COG4717 173 AELQEELE-------------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL--------EQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 541 FRDKPITDQQRQHLRACipphRARTCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQRKwtlqrethlHP 620
Cdd:COG4717 232 LENELEAAALEERLKEA----RLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE---------KA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 621 KQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNI--LRVSLSWLEETEQLLGDLDI 698
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeeLEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 699 ELSDSDKGFSLCLIyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAE--KEKLAEKLEQEEKLKAKIQQLTEEKAA 776
Cdd:COG4717 379 AGVEDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 777 LEESIgqEKSRSEEALEKAQARVRELENHLASQKEAlensvAQEKRKMREMLEAERRKAQD 837
Cdd:COG4717 458 LEAEL--EQLEEDGELAELLQELEELKAELRELAEE-----WAALKLALELLEEAREEYRE 511
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
716-908 |
9.08e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 716 EHYKKimsQSQDLQAQMNASRETQKSLRQEH----LAEKEKLAEkleQEEKLKAKIQQLTEEKAALEESIGQEKSRSEE- 790
Cdd:PRK10929 211 ELAKK---RSQQLDAYLQALRNQLNSQRQREaeraLESTELLAE---QSGDLPKSIVAQFKINRELSQALNQQAQRMDLi 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 791 ALEKAQA-----RVRELENHLASQK----------EALENSVAQ--EKRKM----REM--LEAERRKAQDLENQLTQQKE 847
Cdd:PRK10929 285 ASQQRQAasqtlQVRQALNTLREQSqwlgvsnalgEALRAQVARlpEMPKPqqldTEMaqLRVQRLRYEDLLNKQPQLRQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 848 ISENNTYeklkmrdTLEKEKRKIqdLENRLTKQKEEIE----------LKEQKENVLNNKLKDALVMVEDA 908
Cdd:PRK10929 365 IRQADGQ-------PLTAEQNRI--LDAQLRTQRELLNsllsggdtliLELTKLKVANSQLEDALKEVNEA 426
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
717-1248 |
9.57e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 717 HYKKIMSQSqDLQAQMNASRETQKSLRQEHLAEKEKL---AEKLEQEEKLKAKIQQLTEEKAALEE-SIGQEKS--RSEE 790
Cdd:pfam05483 60 HYQEGLKDS-DFENSEGLSRLYSKLYKEAEKIKKWKVsieAELKQKENKLQENRKIIEAQRKAIQElQFENEKVslKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 791 ALEKAQARVRE--LENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ----KEISENNTYEKLKMRDTLE 864
Cdd:pfam05483 139 EIQENKDLIKEnnATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafEELRVQAENARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 865 KEKRKIQDLENrltKQKEEIELKEQKENVL-------NNKLKDALVMVEDAQQMKTTESQRAETLALKLKETL------- 930
Cdd:pfam05483 219 EDHEKIQHLEE---EYKKEINDKEKQVSLLliqitekENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIekkdhlt 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 931 AELETTKTKMILT-------DDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 1003
Cdd:pfam05483 296 KELEDIKMSLQRSmstqkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1004 EG-----------------EITTLKNNDTGPKEEASQDLTAGPPLDSGDKEI--------ACDHLIDDLLMAQKEILSQQ 1058
Cdd:pfam05483 376 EDqlkiitmelqkksseleEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFekiaeelkGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1059 EIIMKLRTDLGEAHSR-MSDLRGELSEKQ-----------KMELERQvALVRQQSGELSMLKAKVAQTTGLMEKKDRELK 1126
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKeVEDLKTELEKEKlknieltahcdKLLLENK-ELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1127 VLrEALRASQEKPRPHLST---EQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEetIQRQRKALS 1203
Cdd:pfam05483 535 QI-ENLEEKEMNLRDELESvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--IENKNKNIE 611
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 1204 ELRTRVRELEKANSCNHKD------HVNESFLELRTLR-----MEKNVQKILLDAK 1248
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQlnayeiKVNKLELELASAKqkfeeIIDNYQKEIEDKK 667
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
392-1176 |
1.09e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 392 EQVQQLQEEVnrlRIENREKEYQLEALSSRCSVMKEEL-RKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKn 470
Cdd:TIGR00618 176 DQYTQLALME---FAKKKSLHGKAELLTLRSQLLTLCTpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 471 ymgqniisktLREKNKVEEKLQEDSRR-KLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQ 549
Cdd:TIGR00618 252 ----------QEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 550 QRQHLRACIPPHRARTcaptlQSLPRRAGCLETSYclssGQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSV 629
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQ-----SSIEEQRRLLQTLH----SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 630 EKLRVLldkcqacmrdscSSIDLKKEVELLQHLPlsplvsglQKTVVNILRVSLSWLEETEQLlgdldielsdSDKGFSL 709
Cdd:TIGR00618 393 QKLQSL------------CKELDILQREQATIDT--------RTSAFRDLQGQLAHAKKQQEL----------QQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 710 CLIYllehykkIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAK-IQQLTEEKAALEESIGQEKS 786
Cdd:TIGR00618 443 CAAA-------ITCTAQCEKLEKIHLQESAQSLKEreQQLQTKEQIHLQETRKKAVVLArLLELQEEPCPLCGSCIHPNP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 787 RSEEALEKA--QARVRELENHLASQKEALENSVAQ--EKRKMREMLEAERRKAQDLENQLTQQ----KEISENNTYEKLK 858
Cdd:TIGR00618 516 ARQDIDNPGplTRRMQRGEQTYAQLETSEEDVYHQltSERKQRASLKEQMQEIQQSFSILTQCdnrsKEDIPNLQNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 859 MRDTLEKEkrkiqdLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvedAQQMKTTESQRAETLALKLKETLAELETTKT 938
Cdd:TIGR00618 596 LQDLTEKL------SEAEDMLACEQHALLRKLQPEQDLQDVRL------HLQQCSQELALKLTALHALQLTLTQERVREH 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 939 KMILTDDRLKLQQQSMKALQDE--RESQKHGFEEEISEYKE---QIKQHSQTIVSLEERLCQVTQYY-QKIEGEITTLKN 1012
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMqsEKEQLTYWKEMLAQCQTllrELETHIEEYDREFNEIENASSSLgSDLAAREDALNQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1013 NDTGPKEEASQDLTAgpplDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRtDLGEAHSRMSDLRGELSEKQKMELER 1092
Cdd:TIGR00618 744 SLKELMHQARTVLKA----RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR-LREEDTHLLKTLEAEIGQEIPSDEDI 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1093 QVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahPDSFSS 1172
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD---GDALIK 895
|
....
gi 1720409130 1173 FQEE 1176
Cdd:TIGR00618 896 FLHE 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-880 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 257 EIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAaarqsnrcdPKLQGVDEGDDLRQKEIESMKSQ 336
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------PELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 337 INALQKGYSQVLSQ--TLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMsarnEQVQQLQEEVNRLRIENREKEYQ 414
Cdd:PRK03918 240 IEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 415 LEALSSRCSVMKEELRKEEAQKDRREAQEKELKlcrsqmqDMEKEVRKLREEL--------KKNYMGQNIISKTLREKNK 486
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLK-------ELEKRLEELEERHelyeeakaKKEELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 487 VEEKLQEDSRRKlLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATfgKTKPFRDKPITDQQRQHLRAcipphrartc 566
Cdd:PRK03918 389 LEKELEELEKAK-EEIEEEISKITARIGELKKEIKELKKAIEELKKAK--GKCPVCGRELTEEHRKELLE---------- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 567 aptlqslprragcletSYCLSSGQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKqeetmhsVEKLRVLLDKCQAcMRDS 646
Cdd:PRK03918 456 ----------------EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE-------LIKLKELAEQLKE-LEEK 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 647 CSSIDLKK-EVELLQHLPLSPLVSGLQKTVVNILRvSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEH-YKKIMSQ 724
Cdd:PRK03918 512 LKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKK-ELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEEL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 725 SQDLQAQMNASRETQKSLRQEH-LAEKEKLAEKLeqEEKLKAKIQQLTEEKAALEESIGQ----EKSRSEEALEKAQARV 799
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKeLEREEKELKKL--EEELDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEY 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 800 RELENHLASQKEALEnsvaqekrKMREMLEAERRKAQDLENQLTQQKEISENntYEKL-KMRDTLEKEKRKIQDLENRLT 878
Cdd:PRK03918 669 LELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKE--LEKLeKALERVEELREKVKKYKALLK 738
|
..
gi 1720409130 879 KQ 880
Cdd:PRK03918 739 ER 740
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
77-124 |
1.12e-04 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 43.42 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720409130 77 HALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILRFGS 124
Cdd:cd22686 51 HAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELKIGE 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
380-1148 |
1.13e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 380 VTSLQKDMSARNEQVQQLQEEVNRLRIENRE--KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDME 457
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEElkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 458 KEVRKLREELKKNYMGQNIISKTLREKNKV------EEKLQED-----------SRRKLLQLQEMGNRENLIKINLERAV 520
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEelkllakeeeeLKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 521 GQLENFRNQVI---------KATFGKTKPFRDKPITDQQRQHLRACIPPHRARTCAPTLQSLPRRAGCLETSYclSSGQL 591
Cdd:pfam02463 324 KKAEKELKKEKeeieelekeLKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE--LELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 592 IEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQAcMRDSCSSIDLKKEVELLQHLPLSPLVSGL 671
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 672 QKTVVNILRVSLSWLEETEQLL----GDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL 747
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKEskarSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 748 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEA--LENSVAQEKRKMR 825
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVegILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 826 EMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 905
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 906 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILtddRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQT 985
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL---KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 986 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSG-DKEIACDHLIDDLLMAQKEILSQQEIIMKL 1064
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQkLEKLAEEELERLEEEITKEELLQELLLKEE 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1065 RTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSmLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLS 1144
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE-IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
....
gi 1720409130 1145 TEQK 1148
Cdd:pfam02463 957 EEEE 960
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
773-1001 |
1.27e-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: 46.76 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 773 EKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAqekrkmremleAERRKAQDLENQLTQQKEISENN 852
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----------EETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 853 TYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK------EQKENVLNNKLkdalvmvEDAQQMKTTESQRAETLALkL 926
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawleEQKEQKREART-------EKQAYWQVVEGALDAQLAL-L 734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 927 KETLAELETTKtkmiltDDRLKLQQQSMKalqdeRESQKHGFEEE-ISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 1001
Cdd:pfam12128 735 KAAIAARRSGA------KAELKALETWYK-----RDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFD 799
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
744-874 |
1.77e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 744 QEHLAEKEKLAEKLEQEEK--LKAK--IQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHL 806
Cdd:cd16269 145 QLYLEDREKLVEKYRQVPRkgVKAEevLQEFLQSKEAEAEAILQadqaltekekeieAERAKAEAAEQERKLLEEQQREL 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 807 ASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEiSENNTYEKLKMRDTLEKEKRKIQDLE 874
Cdd:cd16269 225 EQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKL-KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
726-998 |
1.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 726 QDLQAQMNASREtqkslrQEHLAEKEKLAEK-LEQEEKLKAKIQQLTEEKAALEESIGQeksrSEEALEKAQARVRELEN 804
Cdd:PRK11281 39 ADVQAQLDALNK------QKLLEAEDKLVQQdLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 805 HLASQ-KEALEN-SVAQEKRKMREMLEAERRKAQDLE-------NQLTQ----QKEISENNTyeklkmrdtlekekrKIQ 871
Cdd:PRK11281 109 DNDEEtRETLSTlSLRQLESRLAQTLDQLQNAQNDLAeynsqlvSLQTQperaQAALYANSQ---------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 872 DLENRLTKQK-EEIELKEQKENVLNNKLkdALVMVEDAQQMKTTE----------SQRAEtlaLKLKETLAELETTKTKM 940
Cdd:PRK11281 174 QIRNLLKGGKvGGKALRPSQRVLLQAEQ--ALLNAQNDLQRKSLEgntqlqdllqKQRDY---LTARIQRLEHQLQLLQE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 941 ILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQ 998
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQ 306
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
761-885 |
2.00e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 761 EKLKAKIQQLTEEKAALEESigqEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKMREMLEAERRKAQDL 838
Cdd:COG0542 414 DELERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARWEAekELIEEIQELKEELEQRYGKIPEL 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 839 ENQLTQ-QKEISENNTYEKL--------------------KMrdtLEKEKRKIQDLENRLTK----QKEEIE 885
Cdd:COG0542 491 EKELAElEEELAELAPLLREevteediaevvsrwtgipvgKL---LEGEREKLLNLEEELHErvigQDEAVE 559
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
387-978 |
2.01e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 387 MSARNEQVQQLQEEVnrlrienrekeyQLEALSSRCSVMKEELRKEEAQKDRReAQEKElklcrSQMQDMEKEVRKLREE 466
Cdd:pfam10174 153 LGARDESIKKLLEML------------QSKGLPKKSGEEDWERTRRIAEAEMQ-LGHLE-----VLLDQKEKENIHLREE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 467 LKKNYMGQNIISKTLREKNKVEEK------LQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQvikATFGKTKp 540
Cdd:pfam10174 215 LHRRNQLQPDPAKTKALQTVIEMKdtkissLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH---SKFMKNK- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 541 frdkpiTDQQRQHLracippHRARTCAPTLQSLprragcLETsycLSSGQLIEKI-IQVTEDNLSF-QQRKWTLQRET-- 616
Cdd:pfam10174 291 ------IDQLKQEL------SKKESELLALQTK------LET---LTNQNSDCKQhIEVLKESLTAkEQRAAILQTEVda 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 617 -HLHPKQEETMHSvEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHlplspLVSGLQKTVVNI---LRVSLSWLEETEQL 692
Cdd:pfam10174 350 lRLRLEEKESFLN-KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-----KINVLQKKIENLqeqLRDKDKQLAGLKER 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 693 LGDLDIELSDSDKGFSLCLIYLLEHYKKImsqsqdlqaqmNASRETQKSLRQEHLAEKEKLAEKL-EQEEKLKAKIQQLT 771
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERII-----------ERLKEQREREDRERLEELESLKKENkDLKEKVSALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 772 EEKAALEESIGQEKSRSEEALEKaQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKA------QDLENQLTQQ 845
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECSKLENQLK-KAHNAEEAVRTNPeindriRLLEQEVARY 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 846 KEISENNTYEKLKMRDTL---EKEK----RKIQDLENRLTKQ-KEEIELKEQKENVLNNKLKDALVMVEDAqqMKTTESQ 917
Cdd:pfam10174 571 KEESGKAQAEVERLLGILrevENEKndkdKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEEA--RRREDNL 648
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 918 RAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK-------ALQDERESQKhgfeEEISEYKEQ 978
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAekdghltNLRAERRKQL----EEILEMKQE 712
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
749-1003 |
2.33e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.19 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 749 EKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQ-EKSRSE--EALEKAQARVRELENhlasQKEAleNSVAQEKRKM 824
Cdd:pfam15905 91 EQDKRLQALEEElEKVEAKLNAAVREKTSLSASVASlEKQLLEltRVNELLKAKFSEDGT----QKKM--SSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 825 REMLEAERRKAQDLENQLTQQKEISENNtyeklkmrdtLEKEKRKIQDLENRL-TKQKEEIELKEQKENVLNNKLKdaLV 903
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKN----------LEHSKGKVAQLEEKLvSTEKEKIEEKSETEKLLEYITE--LS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 904 MVEDAQQMKTTESQRAETLalkLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKhgfEEEISEYKEQIKQHS 983
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEEL---LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---EELLREYEEKEQTLN 306
|
250 260
....*....|....*....|
gi 1720409130 984 QTIVSLEERLCQVTQYYQKI 1003
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
73-123 |
2.53e-04 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 41.77 E-value: 2.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 73 IDNHHALIEFN----EAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 123
Cdd:cd22677 41 ISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
784-1013 |
2.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 784 EKSRSEEALEKAQARVRELENHlasqKEALENsvAQEKRKMREMLEAERRKAQDLENQLTQQkeisenntyEKLKMRDTL 863
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA----HEALED--AREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 864 EKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAETLALKLKETLAELETTKTKMIL 942
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 943 TDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNN 1013
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
821-1213 |
2.64e-04 |
|
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: 45.49 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 821 KRKMREMLEAERRKAQDLENQLTQQKEISENNTY------------------EKLKMRDTLEKEKRKIQDLENRLTKQKE 882
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFylrqsvidlqtklqemqmERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 883 EIE-LKEQKENVLNnklkDALVMVEDAQQMKTTEsqraETLALKLKETLAELETTKTKMILTDDrlKLQQQSMKALQDER 961
Cdd:pfam15921 153 ELEaAKCLKEDMLE----DSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEHD--SMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 962 ESQKHGFEEEISEYK----------EQIKQHSQTIVSLeerlcQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL 1031
Cdd:pfam15921 223 SKILRELDTEISYLKgrifpvedqlEALKSESQNKIEL-----LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1032 DSgdkeiacdhlidDLLMAQKEILSQQEIIMKLRTDLgeaHSRMSDLRGELSEKQKM------ELERQVALVRQQSGELS 1105
Cdd:pfam15921 298 QS------------QLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAKRMyedkieELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1106 MLKAKVAQTTGLMEkkDRELKVLREALRASQEKPrphLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDL--- 1182
Cdd:pfam15921 363 TERDQFSQESGNLD--DQLQKLLADLHKREKELS---LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALlka 437
|
410 420 430
....*....|....*....|....*....|....
gi 1720409130 1183 -GVKCKGS--RHEETIQRQRKALSELRTRVRELE 1213
Cdd:pfam15921 438 mKSECQGQmeRQMAAIQGKNESLEKVSSLTAQLE 471
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
714-1026 |
2.65e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 714 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALE 793
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 794 KAQARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK 867
Cdd:pfam07888 126 AHEARIRELEEDIKTltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 868 RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDalvmVEDAQQMKTTESQRAETLALKLKETL------------AELET 935
Cdd:pfam07888 206 TQVLQLQDTITTLTQKLTTAHRKEAENEALLEE----LRSLQERLNASERKVEGLGEELSSMAaqrdrtqaelhqARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 936 TKTKMILTDDRLKLQQQSMKALQdERESQKHGFEEEiseyKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDT 1015
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQ-ERETLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNR 356
|
330
....*....|.
gi 1720409130 1016 GPKEEASQDLT 1026
Cdd:pfam07888 357 VQLSESRRELQ 367
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
77-124 |
3.59e-04 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 41.19 E-value: 3.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720409130 77 HALIEFNEAEGTFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 124
Cdd:cd22678 46 HARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
711-978 |
3.60e-04 |
|
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: 44.95 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 711 LIYLLEHYKKIMSQSQDlQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR--- 787
Cdd:COG5185 287 LIKQFENTKEKIAEYTK-SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEien 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 788 --SEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLEN-QLTQQKEISENNTYEKLKMRDT 862
Cdd:COG5185 366 ivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtlKAADRQIeELQRQIEQATSSNEEVSKLLNE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 863 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKlkdalvmvEDAQQmkttESQRAETLALKLKETLAELETTKTKMI- 941
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEINRSVRSKK--------EDLNE----ELTQIESRVSTLKATLEKLRAKLERQLe 513
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720409130 942 LTDDRLKLQQQSMKALQDERE-SQKHGFEEEISEYKEQ 978
Cdd:COG5185 514 GVRSKLDQVAESLKDFMRARGyAHILALENLIPASELI 551
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-883 |
3.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 252 QQDKDEIILLLGRE---VNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAAARQSnrcdpKLQGVDEGDDLRQK 328
Cdd:COG1196 277 EELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-----ELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 329 EIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAITsgmvtslqkdmsARNEQVQQLQEEVNRLRIEN 408
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAE-LAEAEEELEELAEELLEALRAAAEL------------AAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 409 REKEYQLEALSSRcsvmKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniisktLREKNKVE 488
Cdd:COG1196 419 LEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL-----------EAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 489 EKLQEDSRRKLLQLQEMGNREnlikinleravgqlenFRNQVIKATFGKTKPFRDKPITDQQRQHlracipPHRARTCAP 568
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYE----------------GFLEGVKAALLLAGLRGLAGAVAVLIGV------EAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 569 TlqslpRRAGCLETSYCLSSGQLIEKIIQVTEDNLSfqqrkwtlqRETHLHPKQEETMHSVEKLRVLLDKCQAcmrdscs 648
Cdd:COG1196 542 A-----ALAAALQNIVVEDDEVAAAAIEYLKAAKAG---------RATFLPLDKIRARAALAAALARGAIGAA------- 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 649 sIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVsLSWLEETEQLLGDLDIELSDSDKGfslcliyllehykkimsqsqdL 728
Cdd:COG1196 601 -VDLVASDLREADARYYVLGDTLLGRTLVAARL-EAALRRAVTLAGRLREVTLEGEGG---------------------S 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 729 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS 808
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 809 QKEALENSVAQEKRKMREM-----LEAERRKAQDLENQLT-----------QQKEISENntYEKLKM-RDTLEKEKRKIQ 871
Cdd:COG1196 738 LEELLEEEELLEEEALEELpeppdLEELERELERLEREIEalgpvnllaieEYEELEER--YDFLSEqREDLEEARETLE 815
|
650
....*....|..
gi 1720409130 872 DLENRLTKQKEE 883
Cdd:COG1196 816 EAIEEIDRETRE 827
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
723-962 |
3.99e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 723 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARV 799
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleaQIAELQSEIAEREEEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 800 RELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 879
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 880 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD 959
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
...
gi 1720409130 960 ERE 962
Cdd:COG4372 313 LED 315
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
736-972 |
4.00e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 736 RETQKSLRQEHLAEKEKLAEKLEQEEK-LKAKIQQLTEEKAALEESIGQEK---SRSEEALEKAQARVRELENHLASQKE 811
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKeLEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 812 ALE------NSVAQEKRKMREMLeaerrkaQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE 885
Cdd:pfam01576 83 RLEeeeersQQLQNEKKKMQQHI-------QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 886 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK---ETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 962
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250
....*....|
gi 1720409130 963 SQKHGFEEEI 972
Cdd:pfam01576 236 AQLAKKEEEL 245
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
745-927 |
4.30e-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: 45.21 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 745 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVreLENHLASQKEALE---NSVAQEK 821
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAI----SGSQSQLESTDQNA--LETNGQAQRDAILeesRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 822 RKMREMLEAERRKAQ-------------------DLENQL--------TQQKEISENNTYEKLKMRDTLEKEK------- 867
Cdd:NF012221 1623 TTLAQGLDALDSQATyagesgdqwrnpfagglldRVQEQLddakkisgKQLADAKQRHVDNQQKVKDAVAKSEagvaqge 1702
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 868 RKIQDLENRLTKQKEEIELKEQ----KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK 927
Cdd:NF012221 1703 QNQANAEQDIDDAKADAEKRKDdalaKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
783-941 |
4.37e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 783 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEIsenntyeklkmrdt 862
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQ-------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409130 863 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttesqrAETLALKLKETLAELETTKTKMI 941
Cdd:PRK12705 93 LDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTP--------EQARKLLLKLLDAELEEEKAQRV 163
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
751-1009 |
4.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 751 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaqEKRKMREMLEA 830
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 831 ERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQ 910
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 911 MKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLE 990
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|....*....
gi 1720409130 991 ERLCQVTQYYQKIEGEITT 1009
Cdd:COG4372 273 TEEEELEIAALELEALEEA 291
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
717-1012 |
4.65e-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: 44.46 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 717 HYKKIMSQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQ 796
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEE-------LDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 797 ARVRELE-------------NHLASQK--EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisennTYEKLKMR- 860
Cdd:pfam06160 153 KQLAEIEeefsqfeeltesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE-----GYREMEEEg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 861 ---DTLEKEKRkIQDLENRLTKQKEEI---ELKEQKENVLN-----NKLKDALVMVEDAQQ-----MKTTESQRAETLAl 924
Cdd:pfam06160 228 yalEHLNVDKE-IQQLEEQLEENLALLenlELDEAEEALEEieeriDQLYDLLEKEVDAKKyveknLPEIEDYLEHAEE- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 925 KLKETLAELETTKTKMILTDDRLKLQQQsmkaLQDERESQKHGFEeeisEYKEQIKQHSQTIVSLEERLCQVTQYYQKIE 1004
Cdd:pfam06160 306 QNKELKEELERVQQSYTLNENELERVRG----LEKQLEELEKRYD----EIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
....*...
gi 1720409130 1005 GEITTLKN 1012
Cdd:pfam06160 378 EEQEEFKE 385
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
261-528 |
4.89e-04 |
|
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: 44.72 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 261 LLGREVNRLSDFEMESKYKDALIMNLQAEVADlSQRLSETAAVAAARQSNRCDPKLQGV----DEGDDLR--QKEIESMK 334
Cdd:pfam15921 476 MLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAEITKLRSRVDLKLQELqhlkNEGDHLRnvQTECEALK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 335 SQinalqkgysqvlsqtLAERNTEIESLKNEGENLKR---DHAITSGmvtSLQKDMSARNEQVQQLQEEVNRLRIENREK 411
Cdd:pfam15921 555 LQ---------------MAEKDKVIEILRQQIENMTQlvgQHGRTAG---AMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 412 EYQLEALSSRCSVMK-----------EELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVrklrEELKKNYmgqniiskt 480
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY----EVLKRNF--------- 683
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720409130 481 lreKNKVEeklqedsrrkllqlqEMGNRENLIKINLERAVGQLENFRN 528
Cdd:pfam15921 684 ---RNKSE---------------EMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
714-1126 |
5.72e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 714 LLEHYKKIMSQSQDLQAQMNASRE-TQKSLRQEHLAEKEKLAEKL-----------EQEEKLKAKIQQLTEEKAALE--- 778
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKIENIvtkidkkkniyDEIKKLLNEIAEIEKDKTSLEevk 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 779 ---------------ESIGQEKSRSEEALEKAQARVRELENhLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLT 843
Cdd:TIGR01612 1214 ginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 844 QQK-------------EISENNtYEKLKMRD---TLEKEKRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDAL 902
Cdd:TIGR01612 1293 SKKhdenisdirekslKIIEDF-SEESDINDikkELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYT 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 903 VMVEDAQQMKTTESQRAETLALKLKETLAeLETTKTKMILTDDRLKLQQqsmkALQDERESQKHGFEEE--ISEYKEQIK 980
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKSKIESTLDDKDIDE----CIKKIKELKNHILSEEsnIDTYFKNAD 1446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 981 QHSQTIVSL---EERLCQVTQYYQKIEgeittlKNNDTgpkeeASQDLTAGPPLDSGDKEIACDHLIDDllmAQKEILSQ 1057
Cdd:TIGR01612 1447 ENNENVLLLfknIEMADNKSQHILKIK------KDNAT-----NDHDFNINELKEHIDKSKGCKDEADK---NAKAIEKN 1512
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409130 1058 QEIIMKLRTDLGEAHSRMSDLrgelsekqkmELERQVALVRQQS----GELSMLKAKVAQTTGLMEKKDRELK 1126
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNKYSAL----------AIKNKFAKTKKDSeiiiKEIKDAHKKFILEAEKSEQKIKEIK 1575
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
687-995 |
5.91e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 687 EETEQLLGDLDIELSDSDKgfslCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK 766
Cdd:pfam01576 71 QELEEILHELESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 767 IQQLTEEKAALEESIGQEKSRSEEALEKAQArVRELENHLASQKEALENSVAQEKrKMREMLEAERRK----AQDLENQL 842
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKlegeSTDLQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 843 T-QQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTtesqRAET 921
Cdd:pfam01576 225 AeLQAQIAE--------LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN----KAEK 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 922 LALKLKEtlaELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ----HSQTIVSLEERLCQ 995
Cdd:pfam01576 293 QRRDLGE---ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkHTQALEELTEQLEQ 367
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
64-103 |
6.14e-04 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 39.08 E-value: 6.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720409130 64 CRSDAESADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVN 103
Cdd:smart00240 10 CDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
727-993 |
7.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 727 DLQAQMNASRETQKSLRQEHLAEKEKLA---------EKLEQ-EEKLKAKIQQLTEEKAALEESIGQeKSRSEEALEKAQ 796
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqEKIERyQADLEELEERLEEQNEVVEEADEQ-QEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 797 ARVRELENHLASQKEALEnsvAQEKR--------------------------KMREMLEAERRKAQDLENQLTQ--QK-- 846
Cdd:PRK04863 390 EEVDELKSQLADYQQALD---VQQTRaiqyqqavqalerakqlcglpdltadNAEDWLEEFQAKEQEATEELLSleQKls 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 847 ---------------------EISENN----------TYEKLKMRD-TLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 894
Cdd:PRK04863 467 vaqaahsqfeqayqlvrkiagEVSRSEawdvarellrRLREQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 895 NNKLKDALV----------MVEDAQQMKTTESQRAETLALKLKET---LAELETTKTKMILTDDRL-KLQQQS------- 953
Cdd:PRK04863 547 GKNLDDEDEleqlqeeleaRLESLSESVSEARERRMALRQQLEQLqarIQRLAARAPAWLAAQDALaRLREQSgeefeds 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720409130 954 ------MKALQD-ERESQ--KHGFEEEISEYKEQIKQHSQTIVSLEERL 993
Cdd:PRK04863 627 qdvteyMQQLLErERELTveRDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
749-872 |
7.38e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 43.28 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 749 EKEKLAEKLEQEEK-----LKAKIQQLTEEKAALEESIGQEKSRseealekaqarvreLENHLASQKEALENSVAQEKRK 823
Cdd:pfam09755 93 EKETLAMNYEQEEEfltndLSRKLTQLRQEKVELEQTLEQEQEY--------------QVNKLMRKIEKLEAETLNKQTN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720409130 824 mremLEAERRKAQDLENQLTQQKEISENNTYEKLkmrDTLEKEKRKIQD 872
Cdd:pfam09755 159 ----LEQLRREKVELENTLEQEQEALVNRLWKRM---DKLEAEKRLLQE 200
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
713-921 |
8.48e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.78 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 713 YLLEHYKKIMSQSQDLQAQMNASretqKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAL 792
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKEL----SSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 793 EKA--------QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQL-TQQKEISENNTYEKLKMRDTL 863
Cdd:pfam06008 103 EKVatlgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIqTWFQSPQEENKALANALRDSL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 864 EKEKRKIQDLENRLtkqkEEIELKEQKENVLNNKLKDALVMVEdaQQMKTTESQRAET 921
Cdd:pfam06008 183 AEYEAKLSDLRELL----REAAAKTRDANRLNLANQANLREFQ--RKKEEVSEQKNQL 234
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
855-986 |
8.83e-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: 42.60 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 855 EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENvlnnKLKDALVMVEDAQQMK------TTESQRAETLALKLKE 928
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 929 TLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 986
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
744-880 |
1.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 744 QEHLAEKEKLAEKLE-----------QEEKLKAKIQQLTEEKAALEESIGQeksrseeaLEKAQARVRELENHLASQKEA 812
Cdd:COG4913 667 EREIAELEAELERLDassddlaaleeQLEELEAELEELEEELDELKGEIGR--------LEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 813 LENSVAQEkrkMREMLEaERRKAQDLENqltQQKEISENntyeklkMRDTLEKEKRKIQDLENRLTKQ 880
Cdd:COG4913 739 AEDLARLE---LRALLE-ERFAAALGDA---VERELREN-------LEERIDALRARLNRAEEELERA 792
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
719-891 |
1.15e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 719 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKlAEKLEQEEKLKAKIQQLTEEKAALEesigqeksrSEEALEKAQAR 798
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQAEEAAAKA---------AAAAKAKAEAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 799 VRELEnhlASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKrkiQDLENRLT 878
Cdd:PRK09510 153 AKRAA---AAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK---AAAEAKAA 226
|
170
....*....|...
gi 1720409130 879 KQKEEIELKEQKE 891
Cdd:PRK09510 227 AAKAAAEAKAAAE 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
740-892 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 740 KSLRQEHLAEKEKLAEKLEQEEKLKA------KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEAL 813
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAeaikkeALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 814 EnsvaqekrKMREMLEAERRKAQDLENQLTQQKEisennTYEKL--KMRDTLEK-------EKRKI--QDLENRLTKQK- 881
Cdd:PRK12704 106 E--------KREEELEKKEKELEQKQQELEKKEE-----ELEELieEQLQELERisgltaeEAKEIllEKVEEEARHEAa 172
|
170
....*....|....
gi 1720409130 882 ---EEIElKEQKEN 892
Cdd:PRK12704 173 vliKEIE-EEAKEE 185
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
668-957 |
1.28e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 668 VSGLQKTVvnILRVSLSWLEETEQLLGDLDIELSDSD--KGFSLCLIYLLEHYKKIMSQS--QDLQAQMNASRETQKSLR 743
Cdd:COG5022 861 FSLLKKET--IYLQSAQRVELAERQLQELKIDVKSISslKLVNLELESEIIELKKSLSSDliENLEFKTELIARLKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 744 QEHLAE--------KEKLAEKLEQEEKLKakiqQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLaSQKEALEN 815
Cdd:COG5022 939 NIDLEEgpsieyvkLPELNKLHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS-KQYGALQE 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 816 SVAQEKRKMREMLEAerrkaqdlenqltqqkeiseNNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEeiELKEQKENVLN 895
Cdd:COG5022 1014 STKQLKELPVEVAEL--------------------QSASKIISSESTELSILKPLQKLKGLLLLENN--QLQARYKALKL 1071
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 896 NKlKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDD---RLKLQQQSMKAL 957
Cdd:COG5022 1072 RR-ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAqmiKLNLLQEISKFL 1135
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-507 |
1.44e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 286 LQAEVADLSQRLSETAAVAAARQsnrcdpklqgvdegdDLRQ-----KEIESMKSQINALQKGYSQvLSQTLAERNTEIE 360
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDKLVQQ---------------DLEQtlallDKIDRQKEETEQLKQQLAQ-APAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 361 SLKNEG-ENLKRDHAITSgmVTSLQKDMSARNEQVQQLQEEVNrlrienrekEY--QLEALSSrcsvmkeelRKEEAQKD 437
Cdd:PRK11281 105 ALKDDNdEETRETLSTLS--LRQLESRLAQTLDQLQNAQNDLA---------EYnsQLVSLQT---------QPERAQAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 438 RREAQEkelklcRSQmqdmekevrKLREELKKNYMGQNIISKTLREKNKVEEKL---QEDSRRKLL----QLQEMGN 507
Cdd:PRK11281 165 LYANSQ------RLQ---------QIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKSLegntQLQDLLQ 226
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
759-965 |
1.48e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 759 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQA-RVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQD 837
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 838 LENQLTQQ--------KEISENNTYEKLkmRDTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKdalvmvEDA 908
Cdd:COG3206 241 RLAALRAQlgsgpdalPELLQSPVIQQL--RAQLAELEAELAELSARYTPNHPDViALRAQIAALRAQLQQ------EAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 909 QQMKTTESQRaETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQK 965
Cdd:COG3206 313 RILASLEAEL-EALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVAR 364
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
724-934 |
1.52e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 724 QSQDLQAQMnasRETQKSLRQEHLAEKEKLAEKLEQEEKLK---AKIQQLTEEKAALEESIGQ-EKSRSEEALEKA---- 795
Cdd:pfam01576 799 QLKKLQAQM---KDLQRELEEARASRDEILAQSKESEKKLKnleAELLQLQEDLAASERARRQaQQERDELADEIAsgas 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 796 -----QARVRELENHLASQKEALEnsvaqEKRKMREMLEAERRKAQDLENQLTQQKEiSENNTYEKLK-MRDTLEKE--- 866
Cdd:pfam01576 876 gksalQDEKRRLEARIAQLEEELE-----EEQSNTELLNDRLRKSTLQVEQLTTELA-AERSTSQKSEsARQQLERQnke 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 867 -KRKIQDLENRL-TKQKEEI--------ELKEQ-----KENVLNN--------KLKDALVMVEDAQQMKTTESQRAETLA 923
Cdd:pfam01576 950 lKAKLQEMEGTVkSKFKSSIaaleakiaQLEEQleqesRERQAANklvrrtekKLKEVLLQVEDERRHADQYKDQAEKGN 1029
|
250
....*....|.
gi 1720409130 924 LKLKETLAELE 934
Cdd:pfam01576 1030 SRMKQLKRQLE 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
790-1137 |
1.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 790 EALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENqlTQQKEISENNTYEKLKMrdtLEKEKRK 869
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE--INEISSELPELREELEK---LEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 870 IQDLENRLTKQKEEIELKEQKENVLNNKLKDalvmvedaqqmktTESQRAETLA--LKLKETLAELETTKTKMILTDDRL 947
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRE-------------LEERIEELKKeiEELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 948 KLQQQSMKALQdERESQKHGFEEEISEYKEQIKQHSqtivSLEERLCQVTQYYQKIEGEITTLKnndtgPKEEASQDLTA 1027
Cdd:PRK03918 300 EFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELE-----ERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1028 -GPPLDSGDKEIAC---DHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQK-----------MELER 1092
Cdd:PRK03918 370 kKEELERLKKRLTGltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEH 449
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1720409130 1093 QVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRASQE 1137
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
747-960 |
1.69e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 747 LAEKEKLAEKLEQEEKLKAKIQQLTEEkaaLEESIGQEKSRSEEALEKaqarVRELENHLASQKEALENSvaqeKRKMRE 826
Cdd:cd22656 99 LIDDLADATDDEELEEAKKTIKALLDD---LLKEAKKYQDKAAKVVDK----LTDFENQTEKDQTALETL----EKALKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 827 MLEAE-----RRKAQDLENQLTQQKEIsenntyEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENV--LNNKL 898
Cdd:cd22656 168 LLTDEggaiaRKEIKDLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALRLIAdLTAADTDLdnLLALI 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 899 KDALVMVedaQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 960
Cdd:cd22656 242 GPAIPAL---EKLQGAWQAIATDLD-SLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEK 299
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
715-920 |
1.70e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEK 794
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 795 -------AQARVRELENHLASQKEA-------LENSVAQEKRKMREmleaERRKAQDLENQLtqqkEISENNTYEKLKMR 860
Cdd:pfam17380 465 lrqqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIE----EERKRKLLEKEM----EERQKAIYEEERRR 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 861 DTlEKEKRKIQDLENRLTKQKEEIELKEQKenvlnNKLKDALVMVEDAQQMKTTESQRAE 920
Cdd:pfam17380 537 EA-EEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREMMRQIVESEKARAE 590
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
741-1011 |
1.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 741 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 811
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 812 ALENsvAQEkrkMREMLEAERRKAQ----DLENQLT--------QQKEISENN----TYEKLK------------MRDTL 863
Cdd:PRK04863 370 VVEE--ADE---QQEENEARAEAAEeevdELKSQLAdyqqaldvQQTRAIQYQqavqALERAKqlcglpdltadnAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 864 EKEKRKIQDLENRL--TKQKEEI--ELKEQKENVLN--NKLKDAlVMVEDAQQ-----MKTTESQRAETLALK-LKETLA 931
Cdd:PRK04863 445 EEFQAKEQEATEELlsLEQKLSVaqAAHSQFEQAYQlvRKIAGE-VSRSEAWDvarelLRRLREQRHLAEQLQqLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 932 ELEttktkmiltdDRLKLQQQSMKALQDerESQKHG--------FEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 1003
Cdd:PRK04863 524 ELE----------QRLRQQQRAERLLAE--FCKRLGknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
....*...
gi 1720409130 1004 EGEITTLK 1011
Cdd:PRK04863 592 QARIQRLA 599
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
73-131 |
2.41e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 39.14 E-value: 2.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 73 IDNHHALIEFNEAEGTFVLQDFnSRNGTFVNE--CHIQNVAVKLIPGDILRFGSAGMTYEL 131
Cdd:cd22701 46 ISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRSGSLIQIGGVLFYFLL 105
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
62-130 |
2.47e-03 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 38.73 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409130 62 CTCRSDaeSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYE 130
Cdd:cd22673 31 CDIRIQ--LPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFRFE 95
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
708-841 |
2.50e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.57 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 708 SLCLIYLL---EHYKKIMSQSQDLQAQMNASRETQKslrQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQE 784
Cdd:pfam06785 47 SLCLLLLLyywEDALKEKFEKSFLEEKEAKLTELDA---EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQL 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 785 KSRSEEALEKAQARVRELENHLAsQKEALENSVAQEKRKMREMLEAERRKAQDLENQ 841
Cdd:pfam06785 124 QIQLQQISQDFAEFRLESEEQLA-EKQLLINEYQQTIEEQRSVLEKRQDQIENLESK 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
723-1137 |
2.56e-03 |
|
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: 42.35 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 723 SQSQDLQAQMNASRETQKSLRQE-HLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA-------LEK 794
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAldaaereLAQ 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 795 AQARVRELENhLASQKEALENSVAQEKRKMREM------------LEAERRKA---------QDL--ENQLTQQKEIS-- 849
Cdd:TIGR02168 487 LQARLDSLER-LQENLEGFSEGVKALLKNQSGLsgilgvlselisVDEGYEAAieaalggrlQAVvvENLNAAKKAIAfl 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 850 -ENNT-------YEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVM--VEDAQQMK------- 912
Cdd:TIGR02168 566 kQNELgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddLDNALELAkklrpgy 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 913 ----------------TTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYK 976
Cdd:TIGR02168 646 rivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 977 EQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltAGPPLDSGDKEIA-----CDHLIDDLLMAQ 1051
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEeleaqIEQLKEELKALR 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1052 KEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREA 1131
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
....*.
gi 1720409130 1132 LRASQE 1137
Cdd:TIGR02168 882 RASLEE 887
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
715-814 |
2.64e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.36 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE--EKLKAKIQQLTEEKAALEESIG---QEKSRSE 789
Cdd:pfam13166 357 LDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHlvEEFKSEIDEYKDKYAGLEKAINsleKEIKNLE 436
|
90 100
....*....|....*....|....*
gi 1720409130 790 EALEKAQARVRELENHLASQKEALE 814
Cdd:pfam13166 437 AEIKKLREEIKELEAQLRDHKPGAD 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
259-472 |
3.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 259 ILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSEtaavaaarqsnrcdpklqgvdegddLRQKEIESMKSQIN 338
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE-------------------------LGFESVEELEERLK 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 339 ALQKGYSQVLS-----QTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARN-----EQVQQLQEEVNRLRIEN 408
Cdd:PRK03918 596 ELEPFYNEYLElkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSREL 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409130 409 REKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKL---CRSQMQDMEKEVRKLREELKKNYM 472
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekALERVEELREKVKKYKALLKERAL 742
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
805-1012 |
3.20e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 805 HLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 884
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKL--NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 885 -ELKEQKENVLNNK-----LKDALVMVEDAQQMKTT--------ESQRAETLALKLKETLAELETTKTKM--ILTDDRLK 948
Cdd:PRK05771 110 sELENEIKELEQEIerlepWGNFDLDLSLLLGFKYVsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVyvVVVVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 949 LQQQsmkalqdERESQKHGFEE-EISEykeqIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 1012
Cdd:PRK05771 190 SDEV-------EEELKKLGFERlELEE----EGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
357-886 |
3.40e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 41.98 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 357 TEIESLKNEGENLKR----DHAITSGMVTSLQKDMSA-RNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRK 431
Cdd:COG5244 130 EEIVELRRENEELDKinlsLRERISSEEPELNKDGSKlSYDELKEFVEESRVQVYDMVELVSDISETLNRNGSIQRSSVR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 432 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKknymgqniiskTLREKNKVEekLQEDSRRKllqlqemGNRENL 511
Cdd:COG5244 210 ECERSNIHDVLFLVNGILDGVIDELNGELERLRRQLV-----------SLMSSHGIE--VEENSRLK-------ATLEKF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 512 IKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQrQHLRACIPPhrartcaptlqslpRRAGCLETSYCLSSGQL 591
Cdd:COG5244 270 QSLELKVNTLQEELYQNKLLKKFYQIYEPFAQAALSSQL-QYLAEVIES--------------ENFGKLENIEIHIILKV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 592 ---IEKIIQVTEDNLSFQQRKWTLQRETHLHP-----KQEETMHSVEKLRVLLDKCQAcMRDSCSSIDLKK------EVE 657
Cdd:COG5244 335 lssISYALHIYTIKNTPDHLETTLQCFVNIAPismwlSEFLQRKFSSKQETAFSICQF-LEDNKDVTLILKilhpilETT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 658 LLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKG-FSLCLIYLLEHYKKIMSQSQDLQAQMNASR 736
Cdd:COG5244 414 VPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQDNRLFlYPSCDITLSSILTILFSDKLEVFFQGIESL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHLAEKEKLAEKLEQEEKLKakiQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENhlASQKEALENS 816
Cdd:COG5244 494 LENITIFPEQPSQQTSDSENIKENSLLS---DRLNEENIRLKEVLVQKENMLTEETKIKIIIGRDLER--KTLEENIKTL 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 817 VAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMrdTLEKEKRKIQDLENRLTKQKEEIEL 886
Cdd:COG5244 569 KVELNNKNNKLKEENFNLVNRLKNMELKLYQIKDNNTLNKIYL--DLVSEIMELRETIRRQIKEQKRVSI 636
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
719-949 |
3.48e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.56 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 719 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 798
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 799 VRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLT 878
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409130 879 KQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKL 949
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
283-504 |
3.57e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 283 IMNLQAEVADLSQRLSETAAVAAARQSNRC--DPKLQGVDEGDDLRQKEIESMKSQINALQKgysqvlsqtlaERNTEIE 360
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDSSntDTALTTLEEALSEKERIIERLKEQREREDR-----------ERLEELE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 361 SLKNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRRE 440
Cdd:pfam10174 472 SLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409130 441 AQEKELKLC---RSQMQDMEKEVRKLREELKK------NYMGqnIISKTLREKNKVEEKLQEDSRRKLLQLQE 504
Cdd:pfam10174 545 NAEEAVRTNpeiNDRIRLLEQEVARYKEESGKaqaeveRLLG--ILREVENEKNDKDKKIAELESLTLRQMKE 615
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
327-437 |
3.65e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 327 QKEIESMKSQINALQKgYSQVLSQTLAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEqVQQLQEEVNRLRI 406
Cdd:COG2433 412 EEEIRRLEEQVERLEA-EVEELEAELEEKDERIERLERELSEARS----------EERREIRKDRE-ISRLDREIERLER 479
|
90 100 110
....*....|....*....|....*....|.
gi 1720409130 407 ENREKEYQLEALSSRCSVMKeELRKEEAQKD 437
Cdd:COG2433 480 ELEEERERIEELKRKLERLK-ELWKLEHSGE 509
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
736-984 |
3.71e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 736 RETQKSLRQEHLAEKEKLAEKLE-QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRElenhlasQKEALE 814
Cdd:pfam15709 263 ASERGAFSSDSVVEDPWLSSKYDaEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKRE-------QEKASR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 815 NSVAQEKRKMReMLEAErRKAQDLENQLTQQKEISENNTyeklKMRDTLEKEKRKIQDlENRLTKQKEEIELKEQKENVL 894
Cdd:pfam15709 336 DRLRAERAEMR-RLEVE-RKRREQEEQRRLQQEQLERAE----KMREELELEQQRRFE-EIRLRKQRLEEERQRQEEEER 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 895 NNKLKDALV--------------MVEDAQQMKTTESQRAETLALKLKETLAEL-ETTKTKMILT-DDRLKLQQQSMKA-- 956
Cdd:pfam15709 409 KQRLQLQAAqerarqqqeefrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLaEEQKRLMEMAeEERLEYQRQKQEAee 488
|
250 260
....*....|....*....|....*....
gi 1720409130 957 -LQDERESQKHGFEEEISEYKEQIKQHSQ 984
Cdd:pfam15709 489 kARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
59-123 |
3.93e-03 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 38.49 E-value: 3.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 59 PGLCTCRSDAESADIDNHHALIEFNeAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 123
Cdd:cd22663 29 LGVTYQLVSTCPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-939 |
3.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 394 VQQLQEEVNRL-RIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnYM 472
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 473 GQNIISKTLREKNKVEEKLQEDSRRkllqlqemgnrenlikinLERAVGQLENFRNQVikatfgktkpfRDKPITDQQRQ 552
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPER------------------LEELEERLEELRELE-----------EELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 553 HLRACIPPHRARTCAPTLQSLprragcletsyclssGQLIEKIIQVtednlsfQQRKWTLQREthLHPKQEEtmhsVEKL 632
Cdd:COG4717 174 ELQEELEELLEQLSLATEEEL---------------QDLAEELEEL-------QQRLAELEEE--LEEAQEE----LEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 633 RVLLDKCQACMRDscssidlKKEVELLQHLPLSPLVSGLqktVVNILRVSLSWLEETEQLLGDLDIELsdsdkGFSLCLI 712
Cdd:COG4717 226 EEELEQLENELEA-------AALEERLKEARLLLLIAAA---LLALLGLGGSLLSLILTIAGVLFLVL-----GLLALLF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 713 YLLEHYKKIMSQSQD----LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqeksrS 788
Cdd:COG4717 291 LLLAREKASLGKEAEelqaLPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------Q 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 789 EEALEKAQARVreLENHLASQKEALEnSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRdtLEKEKR 868
Cdd:COG4717 365 LEELEQEIAAL--LAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEELEE 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409130 869 KIQDLENRLTKQKEEI-ELKEQKENVLNNklkDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTK 939
Cdd:COG4717 440 ELEELEEELEELREELaELEAELEQLEED---GELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
715-934 |
4.18e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKL------------AEKLEQEEKLKAKIQQLTEEKAALEESIG 782
Cdd:pfam13868 65 EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMdeiveriqeedqAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 783 QEKSRSEEALEKAQARVRELENHLAS---QKEALENSVAQEKRKMREMLEAERRKAQDLENQLtQQKEISENNTYEKLKM 859
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEreaEREEIEEEKEREIARLRAQQEKAQDEKAERDELR-AKLYQEEQERKERQKE 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409130 860 RDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvMVEDAQQMKTTESQRAETLALKLKETLAELE 934
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFER--MLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| DUF874 |
pfam05917 |
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ... |
863-966 |
4.35e-03 |
|
Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.
Pssm-ID: 283549 [Multi-domain] Cd Length: 398 Bit Score: 41.38 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 863 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALklketlaELETTKTKMIL 942
Cdd:pfam05917 129 LEQEKKEAENAEDRANKNGIELEQEKQKTNKSGIELANNQIKAEQEQQKTEQEKQKAEKEAI-------ELEQEKQKTIK 201
|
90 100
....*....|....*....|....
gi 1720409130 943 TDDRLKLQQQSMKALQDERESQKH 966
Cdd:pfam05917 202 TQRDLIKEQKDFIKETEQNCQENH 225
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
741-842 |
4.36e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 741 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 811
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlnlvQTALRQQEKIERYQEDLEELTERLEEQEE 368
|
90 100 110
....*....|....*....|....*....|....*
gi 1720409130 812 ALENsvAQEKrkmREMLEAERRKAQD----LENQL 842
Cdd:COG3096 369 VVEE--AAEQ---LAEAEARLEAAEEevdsLKSQL 398
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
737-979 |
4.40e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ------EKSRSEEALEKAQARVRELENHLaSQK 810
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeenSSWEKEEKRDSRLGRYKEEETEI-REK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 811 EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQK---EISENNTYEKLK----MRDTLEKEK----RKIQDLENRLTK 879
Cdd:pfam02029 139 EYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFakeEVKDEKIKKEKKvkyeSKVFLDQKRghpeVKSQNGEEEVTK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 880 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMK-------TTESQRAETLALKLKETLAELETTKTKMiltDDRLKLQQQ 952
Cdd:pfam02029 219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEelrrrrqEKESEEFEKLRQKQQEAELELEELKKKR---EERRKLLEE 295
|
250 260
....*....|....*....|....*..
gi 1720409130 953 SMKALQDERESQKHGFEEEISEYKEQI 979
Cdd:pfam02029 296 EEQRRKQEEAERKLREEEEKRRMKEEI 322
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-525 |
4.47e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 334 KSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEY 413
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQ-ISQNNKIISQLNEQISQLKKE-------LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 414 QLEALSSRCSVMKEELRKEEAQKDRREAQEKELKlcrSQMQDMEKEVRKLREELKKNymgqNIISKTLREKNKVEEKLQE 493
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKETIIKN----NSEIKDLTNQDSVKELIIK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720409130 494 --DSRRKLL--QLQEMGNRENLIKINLERAVGQLEN 525
Cdd:TIGR04523 458 nlDNTRESLetQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
76-129 |
4.69e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 37.75 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 76 HHAliEFNEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTY 129
Cdd:cd22684 43 RHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| V_HD-PTP_like |
cd09234 |
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ... |
251-516 |
4.76e-03 |
|
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.
Pssm-ID: 185747 [Multi-domain] Cd Length: 337 Bit Score: 40.74 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 251 SQQDKDEIilllgrevnrLSDFeMESKYKDALIMNLQAEVADLSQRLSETAAVAAARQSNRcDPKLQGVDEGDDLRQ--- 327
Cdd:cd09234 25 EIEDKDEE----------LDQF-LSSLQLDPLNVMDMDGQFELPQDLVERCAALSVRPDTI-KNLVEAMGELSDVYQdve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 328 ---KEIESMKSQINALQKGYSQVLSQTLAErNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSarneqvqqlqeevnrL 404
Cdd:cd09234 93 amlNEIESLLEEEELQEKEFQEAVGKRGSS-IAHVTELKRELKKYKEAHEKASQSNTELHKAMN---------------L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 405 RIENrekeyqLEALSSRCSVMKEEL-RKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLRE 483
Cdd:cd09234 157 HIAN------LKLLAGPLDELQKKLpSPSLLDRPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAIHEDDITSKLVTT 230
|
250 260 270
....*....|....*....|....*....|...
gi 1720409130 484 KNKVEEKLQEDSRRKLLQLQemgnreNLIKINL 516
Cdd:cd09234 231 TGGDMEDLFKEELKKHDQLV------NLIEQNL 257
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
253-503 |
4.92e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 253 QDKDEIILLLGR-EVNRLSDFEMESKYKDALimnlQAEVADLSQRLSETAA---VAAARQSNrcdpklqgVDEGDDLRQK 328
Cdd:PLN02939 138 QNAEKNILLLNQaRLQALEDLEKILTEKEAL----QGKINILEMRLSETDArikLAAQEKIH--------VEILEEQLEK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 329 EIESMKSQInALQKGYSQVLSQTLAERNTEIESLKNEGENLKR---DHAITSGMVTSLQKDMSARNEQVQQLQEEVnrlr 405
Cdd:PLN02939 206 LRNELLIRG-ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAeliEVAETEERVFKLEKERSLLDASLRELESKF---- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 406 IENREKEYQLEALSSRCsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK--KNYMGQNIISKTLRE 483
Cdd:PLN02939 281 IVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKeaNVSKFSSYKVELLQQ 358
|
250 260
....*....|....*....|.
gi 1720409130 484 KNK-VEEKLQEDSRRKLLQLQ 503
Cdd:PLN02939 359 KLKlLEERLQASDHEIHSYIQ 379
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
352-981 |
5.50e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 352 LAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsVMKEELRK 431
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKR----------KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR--LEEETAQK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 432 EEAQKDRREAQ------EKELKLCRSQMQDMEKEVRKLREELK-----------KNYMGQNIISKTLREKNKVEEKLQED 494
Cdd:pfam01576 260 NNALKKIRELEaqiselQEDLESERAARNKAEKQRRDLGEELEalkteledtldTTAAQQELRSKREQEVTELKKALEEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 495 SRRKLLQLQEMGNRENLIkinLERAVGQLENFRNqvIKATFGKTKPFRDKPITDQQRQhlracipphrartcaptLQSLP 574
Cdd:pfam01576 340 TRSHEAQLQEMRQKHTQA---LEELTEQLEQAKR--NKANLEKAKQALESENAELQAE-----------------LRTLQ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 575 RRAGCLETSYCLSSGQLIEKIIQVTEdnlSFQQRKWTLQRETHLHPKQEETMHSVEKLRvllDKCQACMRDsCSSID--L 652
Cdd:pfam01576 398 QAKQDSEHKRKKLEGQLQELQARLSE---SERQRAELAEKLSKLQSELESVSSLLNEAE---GKNIKLSKD-VSSLEsqL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 653 KKEVELLQH-----LPLSPLVSGLQKTvVNILRVSLSWLEET----EQLLGDLDIELSDSDK---GFSLCLIYLLEHYKK 720
Cdd:pfam01576 471 QDTQELLQEetrqkLNLSTRLRQLEDE-RNSLQEQLEEEEEAkrnvERQLSTLQAQLSDMKKkleEDAGTLEALEEGKKR 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 721 IMSQSQDLQAQMNASRE-------TQKSLRQE------HLAEKEKLAEKLEQeeKLKAKIQQLTEEKAAleesigqeKSR 787
Cdd:pfam01576 550 LQRELEALTQQLEEKAAaydklekTKNRLQQElddllvDLDHQRQLVSNLEK--KQKKFDQMLAEEKAI--------SAR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 788 SEEALEKAQARVRELENHLASQKEALEnsvaqEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE- 866
Cdd:pfam01576 620 YAEERDRAEAEAREKETRALSLARALE-----EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQv 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 867 ---KRKIQDLENRLT-----KQKEEI-----------------ELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAET 921
Cdd:pfam01576 695 eemKTQLEELEDELQatedaKLRLEVnmqalkaqferdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK 774
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 922 LALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 981
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKK 834
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
714-890 |
5.75e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 714 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEH------LAEKEKLA------EKLEQEEKLKAKIQQLTEEKAALEESI 781
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELdllrfqLEELEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 782 GQEKSRSEEALEKAQARVRELENH---LASQKEALENS------VAQEKRKMREMLEAERRKAQDLENQLTQQKEISE-- 850
Cdd:COG0497 236 SGGEGGALDLLGQALRALERLAEYdpsLAELAERLESAlieleeAASELRRYLDSLEFDPERLEEVEERLALLRRLARky 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720409130 851 NNTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 890
Cdd:COG0497 316 GVTVEELlAYAEELRAELAELENSDERLEELEAELAEAEAE 356
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
684-825 |
6.31e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 684 SWLEETEQLLGDLDIELSDSDKGFSlcliyLLEHYKKIMsqsqdlqAQMNASRETQKslrqehlaekeklaekleqeEKL 763
Cdd:pfam05911 716 SQLQESEQLIAELRSELASLKESNS-----LAETQLKCM-------AESYEDLETRL--------------------TEL 763
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 764 KAKIQQLTEEKAALEESIGQEKSRSEEALekaqARVRELENHL--ASQKEALENSVAQEKRKMR 825
Cdd:pfam05911 764 EAELNELRQKFEALEVELEEEKNCHEELE----AKCLELQEQLerNEKKESSNCDADQEDKKLQ 823
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
734-1132 |
6.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 734 ASRETQ-KSLRQEHlaekEKLAEKLEQEEKLKAKIQQLTEekaALEESIGQEKSRS-----EEALEKAQARVRELENHLA 807
Cdd:PRK04863 782 AAREKRiEQLRAER----EELAERYATLSFDVQKLQRLHQ---AFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALA 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 808 SQKEALensvaqekRKMREMLEAERRKAQDLeNQLTQQKEISENNTYEKLKM-----RDTLEKEKRKIQDLENRLTKQKE 882
Cdd:PRK04863 855 DHESQE--------QQQRSQLEQAKEGLSAL-NRLLPRLNLLADETLADRVEeireqLDEAEEAKRFVQQHGNALAQLEP 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 883 EIE-LKEQKENvlNNKLKDAlvmVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDrlklqqqsmKALQDE- 960
Cdd:PRK04863 926 IVSvLQSDPEQ--FEQLKQD---YQQAQQTQRDAKQQAFALT-EVVQRRAHFSYEDAAEMLAKN---------SDLNEKl 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 961 RESQKHGfEEEISEYKEQIKQHsqtivslEERLCQVTQYYQKIEGEITTLKNNdtgpKEEASQDLTA-GPPLDSGDKEia 1039
Cdd:PRK04863 991 RQRLEQA-EQERTRAREQLRQA-------QAQLAQYNQVLASLKSSYDAKRQM----LQELKQELQDlGVPADSGAEE-- 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1040 cdhliddllmaqkeilsqqeiimKLRTDLGEAHSRMSDLRGelsekQKMELERQVALvrqQSGELSMLKAKVaqttglmE 1119
Cdd:PRK04863 1057 -----------------------RARARRDELHARLSANRS-----RRNQLEKQLTF---CEAEMDNLTKKL-------R 1098
|
410
....*....|...
gi 1720409130 1120 KKDRELKVLREAL 1132
Cdd:PRK04863 1099 KLERDYHEMREQV 1111
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
724-904 |
7.12e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 724 QSQDLQAQMNASRETQKSLRQ------------EHLA---EKEKLAEKLEQEEKLKAKIQQLTeekaaleesigQEKSRS 788
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLKQqifalsevvqrrPHFSyedAVGLLGENSDLNEKLRARLEQAE-----------EARREA 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 789 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLE--------AE---RRKAQDLENQLTQQKeiSENNTYEKl 857
Cdd:COG3096 1004 REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeAEeraRIRRDELHEELSQNR--SRRSQLEK- 1080
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720409130 858 kmrdTLEKEKRKIQDLENRLTkqKEEIELKEQKENVLNNKLKDALVM 904
Cdd:COG3096 1081 ----QLTRCEAEMDSLQKRLR--KAERDYKQEREQVVQAKAGWCAVL 1121
|
|
| NFACT_N |
pfam05833 |
NFACT N-terminal and middle domains; This family contains the N-terminal and middle domains of ... |
714-896 |
7.16e-03 |
|
NFACT N-terminal and middle domains; This family contains the N-terminal and middle domains of NFACT (NEMF, FbpA, Caliban, and Tae2) proteins from eukaryotes, archaea and bacteria. Many members of this family act in ribosome quality control (RQC), including RqcH, which are involved in the addition of a poly-Ala tail to defective translated proteins to tag them for degradation. This process is analogous to the ssrA/tmRNA bacterial system. However, some other NFACT family members, such as bacterial proteins FbpA in Listeria or PavA in Streptococcus, are exported (despite lack of a classical signal peptide) and behave as fibronectin-binding adhesins associated with virulence.
Pssm-ID: 428644 [Multi-domain] Cd Length: 451 Bit Score: 40.69 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 714 LLEHYKKIMSQSQDLQAQMNASRETQKS------LRQEHLAEK--EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEK 785
Cdd:pfam05833 229 LYEAFQDLLNQLESGNFEPTLYYDDEPKdfsvlpLSHLGLEKEtfDSLSELLDEYYAEKAERDRVKQKRSDLEKVVQNEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 786 SRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMleaerrkaqDLENQLTQQKEI----------SEN-- 851
Cdd:pfam05833 309 EKLEKKLKKLEKELEEAENADEYRLygELLTANLYQIKKGMKEV---------ELPNYYDEGEPVtipldpakspSENaq 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720409130 852 ---NTYEKLKmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNN 896
Cdd:pfam05833 380 kyfKKYQKLK---------RAVEAVKEQIEETKEEIEYLESVETQLEN 418
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1197 |
7.29e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 856 KLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttESQRAETLALKLKETLAELET 935
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----EIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 936 tktkmiltddrlKLQQqsmkalqderesqkhgFEEEISEYKEQIKQHSQTIVSLEERLCQ----VTQYYQKIEGEITTLK 1011
Cdd:TIGR02169 745 ------------DLSS----------------LEQEIENVKSELKELEARIEELEEDLHKleeaLNDLEARLSHSRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1012 NNDTGPKEEASQDLTAgpPLDSGDKEIACDHLIDDLLmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELE 1091
Cdd:TIGR02169 797 QAELSKLEEEVSRIEA--RLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-ELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 1092 RQVALVRQQSGELSMLKAKVAQttglMEKKDRELKVLREALRASQEKPRPHLSTEQKprTLSQKCDISLQIEPAHPDSFS 1171
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKA--KLEALEEELSEIEDPKGEDEE 945
|
330 340
....*....|....*....|....*.
gi 1720409130 1172 SFQEEQSFSDLGVKCKgsRHEETIQR 1197
Cdd:TIGR02169 946 IPEEELSLEDVQAELQ--RVEEEIRA 969
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
326-474 |
7.68e-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: 40.78 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 326 RQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDHAITSGMV----------TSLQKDMSA 389
Cdd:pfam05667 333 REEELEELQEQLEDLESSIQELekeikkLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaeeniAKLQALVDA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 390 RNEQVQQLQEEVNRLRIENREKeyqLEALSSRCSvmkeelrkeeAQKDRREAQEKELKLCRSQMQDMEKEVRKlREELKK 469
Cdd:pfam05667 413 SAQRLVELAGQWEKHRVPLIEE---YRALKEAKS----------NKEDESQRKLEEIKELREKIKEVAEEAKQ-KEELYK 478
|
....*
gi 1720409130 470 NYMGQ 474
Cdd:pfam05667 479 QLVAE 483
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
737-962 |
7.79e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.41 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 737 ETQKSLRQEHL--AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALE 814
Cdd:COG3064 22 EAEKRAAAEAEqkAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 815 NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 894
Cdd:COG3064 102 KEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 895 NNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 962
Cdd:COG3064 182 LVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAE 249
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
715-836 |
8.34e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.42 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 715 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKiQQLTEEKAALEESIGQEKSRS-EEALE 793
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKAR-AKAAKAQEKVNEALSGIDSDDaTSALE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720409130 794 KAQARVRELENHLASQKE-ALENSVAQEKRKMREMLEAERRKAQ 836
Cdd:COG1842 169 RMEEKIEEMEARAEAAAElAAGDSLDDELAELEADSEVEDELAA 212
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
381-569 |
8.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 381 TSLQKDMSARNEQVQQLQEEVNRLRIENREKEyqLEALSSRCSVMKEELRkeeAQKDRREAQEKELKLCRSQMQDMEKEV 460
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPADSGA--EERARARRDELHARLS---ANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 461 RKLREELKKNY----MGQNIISKTLR--EKNKVEEKLQedsRRKLLQLQEMGNRENLIKIN--LERAVGQLENFRnQVIK 532
Cdd:PRK04863 1098 RKLERDYHEMReqvvNAKAGWCAVLRlvKDNGVERRLH---RRELAYLSADELRSMSDKALgaLRLAVADNEHLR-DVLR 1173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720409130 533 ATFGKTKPFRDKPITDQQRQHLRACIPPHRARTCAPT 569
Cdd:PRK04863 1174 LSEDPKRPERKVQFYIAVYQHLRERIRQDIIRTDDPV 1210
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
744-986 |
8.83e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.63 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 744 QEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEEsigqeksRSEEALEK---AQARVRELENHLasqkEALENSVAQ 819
Cdd:pfam00261 21 MKKLEEAEKRAEKAEAEvAALNRRIQLLEEELERTEE-------RLAEALEKleeAEKAADESERGR----KVLENRALK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 820 EKRKMRemleaerrkaqDLENQLTQQKEISENNTyeklkmrDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLK 899
Cdd:pfam00261 90 DEEKME-----------ILEAQLKEAKEIAEEAD-------RKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 900 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTkmiltddRLKLQQQSMKALQDERESqkhgFEEEISEYKEQI 979
Cdd:pfam00261 152 VVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAET-------RAEFAERSVQKLEKEVDR----LEDELEAEKEKY 220
|
....*..
gi 1720409130 980 KQHSQTI 986
Cdd:pfam00261 221 KAISEEL 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-469 |
9.07e-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: 40.13 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 382 SLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQkdrREAQEKELKLCRSQMQDMEKEVR 461
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELE 100
|
....*...
gi 1720409130 462 KLREELKK 469
Cdd:COG4942 101 AQKEELAE 108
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
878-1012 |
9.15e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 878 TKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKmILTDDRLKLQQQSMKAL 957
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE-KDQTALETLEKALKD-LLTDEGGAIARKEIKDL 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409130 958 QDERESQKhgfEEEISEYKEQIKQHSQTIVSLEERLC---QVTQYYQKIEGEITTLKN 1012
Cdd:cd22656 185 QKELEKLN---EEYAAKLKAKIDELKALIADDEAKLAaalRLIADLTAADTDLDNLLA 239
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
69-124 |
9.30e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 38.05 E-value: 9.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409130 69 ESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 124
Cdd:cd22695 61 DSRVLSRNHACLSCDPTTGKVYIRDLKSSNGTFVNGQKIRQNDVELKVGDEVDLGT 116
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
728-846 |
9.95e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 728 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR-SEEALEKAQARVRELENHL 806
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPaDSGAEERARARRDELHARL 1069
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720409130 807 A---SQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQK 846
Cdd:PRK04863 1070 SanrSRRNQLEKQLTFCEAEMDNLtkkLRKLERDYHEMREQVVNAK 1115
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
719-991 |
9.95e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 719 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEK-------EKLAEKLEQEEKLKAKIQQLTEE----KAA-----LEESIG 782
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRELRKSLLANRfsfgpalDELEKQLENLEEEFSQFVELTESgdyvEAReildqLEEELA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 783 QeksrSEEALEKAQARVRELENHLASQKEALENSVAQ--------EKRKMREMLEAERRKAQDLENQLTQQ--KEISENN 852
Cdd:PRK04778 209 A----LEQIMEEIPELLKELQTELPDQLQELKAGYRElveegyhlDHLDIEKEIQDLKEQIDENLALLEELdlDEAEEKN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409130 853 TY--EKL-KMRDTLEKEkrkiQDLENRLTKQKEEIE--LKEQKENvlNNKLKDALVMVEDAQQMKTTESQRAETLalklk 927
Cdd:PRK04778 285 EEiqERIdQLYDILERE----VKARKYVEKNSDTLPdfLEHAKEQ--NKELKEEIDRVKQSYTLNESELESVRQL----- 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409130 928 etLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQTIVSLEE 991
Cdd:PRK04778 354 --EKQLESLEKQYDEITERIAEQEIAYSELQEELEEI----LKQLEEIEKEQEKLSEMLQGLRK 411
|
|
| |
