|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-135 |
4.15e-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: 4.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 2 KAYLKSADGFFVLN-KSTTIGKHaDSDLVLQdhlvrgqhhpqwpgpstsiinqehapppglctcrsdaeSADIDNHHALI 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQ--------------------------------------SPGVEEQHAVI 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 81 EFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGSAGMTYELVIEN 135
Cdd:cd22700 42 EYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGDVLRFGFGGLPYELVVDN 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-1073 |
9.20e-18 |
|
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: 89.73 E-value: 9.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 323 DDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAItsgmvtsLQKDMSARNEQVQQLQEEVN 402
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 403 RLRIENREKEYQLEALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 478
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 479 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQLIEKII-Q 557
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 558 VTEDNLSFQQRKWTLQRE-THLHPKQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPlsplvSGLQKTVV 636
Cdd:TIGR02168 452 LQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL-----SGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 637 NILRVSLSWLEETEQLLGD--------------LDIE-LSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKS 701
Cdd:TIGR02168 527 ELISVDEGYEAAIEAALGGrlqavvvenlnaakKAIAfLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 702 LRQE-------------HLAEKEKLAEKLEQEEKLKAKIQQLTEE------------KAALEESIGQEKSRseeALEKAQ 756
Cdd:TIGR02168 607 LVKFdpklrkalsyllgGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitgGSAKTNSSILERRR---EIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 757 ARVRELENHLASQKEALeNSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyEKLKMRDTLEKEKRKIQDLENR 836
Cdd:TIGR02168 684 EKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRK-------DLARLEAEVEQLEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 837 LTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttESQRAETLALKLKETLAELEttktkMILTDDRLKLQQQSMKA 916
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELR-----AELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 917 LQDEResQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDK 996
Cdd:TIGR02168 827 ESLER--RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 997 EIAcdhliDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQ 1073
Cdd:TIGR02168 905 ELE-----SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
684-932 |
2.47e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 684 QSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEksrsEEALEKAQARVRELE 763
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 764 NHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENntyeklkmRDTLEKEKRKIQDLENRLTKQKEE 843
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 844 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKmILTDDRLKLQQQSMKALQDERES 923
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA-LAELLEELAEAAARLLLLLEAEA 501
|
....*....
gi 1039768044 924 QKHGFEEEI 932
Cdd:COG1196 502 DYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-972 |
1.82e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 273 EMESKYKDALIMNLQAEVADLSQRLSETAAvaAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYsQVLSQTL 352
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 353 AERNTEIESLKNEGENLKRDHAITSGMVTS-------LQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSR---C 422
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEEleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 423 SVMKEELRKEEAQKDRREAQ-EKELKLCRSQMQDMEKEVRKLREELKKNYMGQ-----NIISKTLREKNKVEEKLQEDSR 496
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 497 RKLLQLQEMGNRENLIKINLERAVGQLE--NFRNQVIKATFGKTKPFRD--KPITDQQL-IEKIIQVTEDNLSFQQrKWT 571
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAqlQARLDSLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVDE-GYE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 572 LQRETHLhpkqEETMHSVeklrvLLDKCQACMRDscssIDLKKEVELLQHLPLsPLVSGLQKTVVNILRVSLSWLEETEQ 651
Cdd:TIGR02168 537 AAIEAAL----GGRLQAV-----VVENLNAAKKA----IAFLKQNELGRVTFL-PLDSIKGTEIQGNDREILKNIEGFLG 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 652 LLGDLDielsDSDKGFSLCLIYLLEHY----------------------------------------------------- 678
Cdd:TIGR02168 603 VAKDLV----KFDPKLRKALSYLLGGVlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrre 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 679 --------KKIMSQSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE--------EKLKAKIQQLTEEKAALEESIG 742
Cdd:TIGR02168 679 ieeleekiEELEEKIAELEKALAELRKELEELEEE-LEQLRKELEELSRQisalrkdlARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 743 ---QEKSRSEEALEKAQARVRELENHLASQKEALENsvaqekrkMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKM 819
Cdd:TIGR02168 758 eleAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ--------LKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 820 RDTLEKEKRKIQDLENRLTKQKEEIELKEQ---KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETT 896
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 897 KTKMiltDDRLKLQQQSMKALQDEREsqkhGFEEEISEYKEQI-KQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 972
Cdd:TIGR02168 910 RSEL---RRELEELREKLAQLELRLE----GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-941 |
1.91e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 251 SQQDKDEIILLLGREVNRLSDFEMESKYKDALIMN----LQAEVADLSQRLSETAAVAAAR--QSNRCDPKLQGVDEGDD 324
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELESKLDELAEELAELeeKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 325 LRQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSarNEQVQQLQ 398
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 399 EEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 478
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 479 K---TLREKNKVEEKLQ------------------EDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGK 537
Cdd:TIGR02168 520 GilgVLSELISVDEGYEaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 538 TKPFRDKPITDQQLIEKIIQ-------VTED---------NLSFQQRKWTLQREThLHP------KQEETMHSVEKLRVL 595
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKALSyllggvlVVDDldnalelakKLRPGYRIVTLDGDL-VRPggvitgGSAKTNSSILERRRE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 596 LDKCQACMRDSCSSIDLKKevellqhlplsplvsglqkTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLL 675
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE-------------------KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 676 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALeesigqeksrsEEALEKA 755
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-----------REALDEL 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 756 QARVRELENHLASQKEALENSVAQekrkmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLEN 835
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERR--------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 836 RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltDDRLKLQQQSMK 915
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAE 957
|
730 740
....*....|....*....|....*.
gi 1039768044 916 ALQDERESQKHGFEEEISEYKEQIKQ 941
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-901 |
2.25e-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: 78.57 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 262 LGREVNRLSDFEMeskykdaliMNLQAEVADLS--QRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINA 339
Cdd:TIGR02169 277 LNKKIKDLGEEEQ---------LRVKEKIGELEaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 340 LQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLE--- 416
Cdd:TIGR02169 348 ERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAdln 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 417 -----------ALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTL 481
Cdd:TIGR02169 427 aaiagieakinELEEEKEDKALEIKKQEWKleqlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 482 REKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENF-----------------RNQVIKATF---GKTKPF 541
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFlplNKMRDE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 542 RDKP--ITDQQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRV------LLDKCQACM--RDSCSSID 611
Cdd:TIGR02169 587 RRDLsiLSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMvtlegeLFEKSGAMTggSRAPRGGI 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 612 LKKEVELLQHLPLSPLVSGLQKTvvniLRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyllehykkIMSQSQDLQAQ 691
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRE----LSSLQSELRRIENRLDELSQELSDASRKIGE-----------IEKEIEQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 692 MNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ-EKSRSEEALEKAQARVRELENHLASQK 770
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 771 EALENSVAQEKRK--MREMLEAERRKAQDLENQLTQQK-----EISENNTyEKLKMRDTLEKEKRKIQDLENRLTKQKEE 843
Cdd:TIGR02169 812 ARLREIEQKLNRLtlEKEYLEKEIQELQEQRIDLKEQIksiekEIENLNG-KKEELEEELEELEAALRDLESRLGDLKKE 890
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039768044 844 IELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAEtlalkLKETLAELETTKTKMI 901
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKrKRLSELKAKLEA-----LEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-837 |
1.95e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 287 QAEVA----DLSQRLSETAAVAAARQsnrcdpklqgvdegDDLRQKEIESMKSQINALQKGySQVLSQTLAERNTEIESL 362
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK--------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 363 KNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQ 442
Cdd:COG1196 273 RLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 443 EKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQ 522
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 523 LENFRNQVIKATFGKTKPFRDKPITDQQLIEKIIQVTEDNLSFQQRKWTLQ---------------RETHLHPKQEETMH 587
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEaalaelleelaeaaaRLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 588 SVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTV-------------------------VNILRVS 642
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVeddevaaaaieylkaakagratflpLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 643 LSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK 722
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 723 LKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaQEKRKMREMLEAERRKAQDLENQL 802
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL----EEELEEEALEEQLEAEREELLEEL 741
|
570 580 590
....*....|....*....|....*....|....*
gi 1039768044 803 TQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRL 837
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
675-1387 |
2.24e-13 |
|
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: 75.48 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 675 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL-AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEE 750
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLeELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 751 ALEKAQAR-------VRELENHLASQKEALENSVAQEKRKMREMLEAERRKaQDLENQLTQQKEISENNTYEKLKMRDTL 823
Cdd:TIGR02168 282 EIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 824 EKEKRKIQDLENRLTKQKEEIE-------LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKEtlAELETT 896
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 897 KTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQHSQTIVSLEERLCQVTQYYqkiEGEITTLKNN 973
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENLEGFS---EGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 974 DTGPKEEAS-QDLTAGPPLDSGDKEIACDHLIDDLLMAQKEilSQQEIIMKLR-TDLGEAH-SRMSDLRGELSEKQKMEL 1050
Cdd:TIGR02168 516 SGLSGILGVlSELISVDEGYEAAIEAALGGRLQAVVVENLN--AAKKAIAFLKqNELGRVTfLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1051 ERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALrasqekprphlstEQKPRTLSQKCDISLQIEPAHPDSF 1130
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL-------------ELAKKLRPGYRIVTLDGDLVRPGGV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1131 SSFQ-EEQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEKANScNHKDHVNESFLELRTLRMEKNVQKILLDAKp 1209
Cdd:TIGR02168 661 ITGGsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARL- 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1210 dLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAGEALELSEKLytDMIKTLGSLMNiKDMSSHTSLKHLSPKEREKVNH 1289
Cdd:TIGR02168 739 -EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIE-QLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1290 LRQKDLDLVFdKITQLKTRLQRKEELLKGYEQELEQLRH--SKVSVQM--YQTQVAKLEDDVHKEAEEKALLKEALERTE 1365
Cdd:TIGR02168 815 LNEEAANLRE-RLESLERRIAATERRLEDLEEQIEELSEdiESLAAEIeeLEELIEELESELEALLNERASLEEALALLR 893
|
730 740
....*....|....*....|..
gi 1039768044 1366 QQLSQERRFNRVFKQQKDRGED 1387
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRR 915
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
671-925 |
2.70e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 671 LIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL---AEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESI-- 741
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELeleeAQAEEYELLAELARLEQDIar 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 742 -GQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTyEKLKMR 820
Cdd:COG1196 307 lEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 821 DTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKM 900
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*
gi 1039768044 901 ILTDDRLKLQQQSMKALQDERESQK 925
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-1052 |
6.44e-13 |
|
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: 73.95 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 292 DLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLK 370
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 371 RDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsvMKEELRKEEAQKDRREAQEKELKLCR 450
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 451 SQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKveekLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQV 530
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDY---REKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 531 ------IKATFGKTKPFRDKPITDQQLIEKI---IQVTEDNLSFQQRKWTlQRETHLHPKQEETMHSVEKLRVLLDKCQA 601
Cdd:TIGR02169 444 edkaleIKKQEWKLEQLAADLSKYEQELYDLkeeYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 602 CMRDSCSSIDLKKEVELLQHLPLSplvSGLQKTVV----------------NILRVSLSWLEETEQLLGDLDIELSDSDK 665
Cdd:TIGR02169 523 VHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVeddavakeaiellkrrKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 666 GFSLCLIYLLEHYKKIMSQsqdlqaqmnASRETQkslrqehlaekekLAEKLEQEEKLKAKIQQLTEEKAALEES----- 740
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKY---------VFGDTL-------------VVEDIEAARRLMGKYRMVTLEGELFEKSgamtg 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 741 ------IGQEKSRSEEA-LEKAQARVRELENHLAS---QKEALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKE 807
Cdd:TIGR02169 658 gsraprGGILFSRSEPAeLQRLRERLEGLKRELSSlqsELRRIENRLDELSQELSDasrKIGEIEKEIEQLEQEEEKLKE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 808 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQR--------- 878
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSriearlrei 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 879 -AETLALKLKETLAELETTKTKMILTDdrLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSL-------E 950
Cdd:TIGR02169 818 eQKLNRLTLEKEYLEKEIQELQEQRID--LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkerdelE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 951 ERLCQVTQYYQKIEGEITTLKNND---TGPKEEASQDLTA-GPPLDSGDKEIACDHLIDDLLMA----QKEILSQQEIIM 1022
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLselKAKLEALEEELSEiEDPKGEDEEIPEEELSLEDVQAElqrvEEEIRALEPVNM 975
|
810 820 830
....*....|....*....|....*....|
gi 1039768044 1023 KLRTDLGEAHSRMSDLRgelSEKQKMELER 1052
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELK---EKRAKLEEER 1002
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
712-953 |
3.16e-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: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 712 KLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEAlENSVAQEKRKMREMLEAE 791
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEA----ELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 792 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQM 871
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----EEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 872 KTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 951
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
..
gi 1039768044 952 RL 953
Cdd:COG1196 464 LL 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
714-988 |
5.48e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 714 AEKLEQEEKLKAKIQQLTEEKAALE--------ESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMR 785
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 786 EMLEAERRKAQdLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 865
Cdd:COG1196 289 EEYELLAELAR-LEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 866 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQT 945
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1039768044 946 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAG 988
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-983 |
7.15e-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: 70.47 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 696 RETQKSLR--QEHLA-------EKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG----QEKSRSEEALEKAQARVREL 762
Cdd:TIGR02168 175 KETERKLErtRENLDrledilnELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 763 ENHLASQKEALENSVAQEKRKMREM----------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD 832
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 833 LENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 912
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039768044 913 SMKALQDERESQKHGFEE-EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 983
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-131 |
1.49e-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: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 12 FVLNKS-TTIGKHADSDLVLQDHLVrgqhhpqwpgpstsiinqehapppglctcrsdaeSAdidnHHALIEFNEaeGTFV 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTV----------------------------------SR----RHARIRRDG--GGWV 55
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1039768044 91 LQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYEL 131
Cdd:COG1716 56 LEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELRFRL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
695-971 |
2.67e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 695 SRETQKSLR-QEHLAEKEKLA--EKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKE 771
Cdd:TIGR02169 204 RREREKAERyQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 772 ALENSVAQEKRKMREmLEAERRKAQD----LENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK 847
Cdd:TIGR02169 284 LGEEEQLRVKEKIGE-LEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 848 EQKENVLNNKLKDalvMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHG 927
Cdd:TIGR02169 363 KEELEDLRAELEE---VDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 928 FEE-------EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 971
Cdd:TIGR02169 439 LEEekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-122 |
3.10e-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: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 18 TTIGKHADSDLVLQDhlvrgqhhpqwpgpstsiinqehapppglctcrsdaesADIDNHHALIEFNEaEGTFVLQDFNSR 97
Cdd:pfam00498 1 VTIGRSPDCDIVLDD--------------------------------------PSVSRRHAEIRYDG-GGRFYLEDLGST 41
|
90 100
....*....|....*....|....*
gi 1039768044 98 NGTFVNECHIQNVAVKLIPGDILRF 122
Cdd:pfam00498 42 NGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-130 |
3.49e-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: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 11 FFVLNKSTTIGKHADSDLVLQDHLVRGqhhpqwpgpstsiinqehapppglctcrsdaesadidnHHALIEFNEaeGTFV 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSR--------------------------------------RHARIEVDG--GGVY 53
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039768044 91 LQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYE 130
Cdd:cd00060 54 LEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFRFE 92
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
709-1108 |
9.00e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 709 EKEKLAEKLEQEEKLKAKIQQL---TEEKAALEESI--GQEKSRSEEALEKAQARvRELENhlaSQKEALENSVAQEKRK 783
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKkkAEEAKKADEAKKKAEEA-KKAEE---AKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 784 MREmleaERRKAQDLENQLTQQKEISEN--NTYEKLKMRDTLEK--EKRKIQDLENRLTKQKEEiELKEQKENVLNNKLK 859
Cdd:PTZ00121 1478 KAE----EAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 860 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 939
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 940 KQHSQTIVSLEERLCQVTQYyqKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQK-EILSQQ 1018
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaEELKKK 1710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1019 EIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGElsmlKAKVAQTTGLMEKKDRELK-----VLREALR 1093
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRkekeaVIEEELD 1786
|
410
....*....|....*
gi 1039768044 1094 ASQEKPRPHLSTEQK 1108
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
676-1373 |
2.85e-10 |
|
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: 65.38 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 676 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 755
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 756 QARVRELENHLASQKEALENSVAQEKRKMREMLEAER-RKAQDLENQLTQQKEISENNtyEKLKMRDTLEKEKRKIQDLE 834
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEeEKEAQLLLELARQLEDLLKE--EKKEELEILEEEEESIELKQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 835 NRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELET--------TKTKMILTDDR 906
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKarsglkvlLALIKDGVGGR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 907 LKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLT 986
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 987 AGPPLDSGDKEIACDH-------LIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQkMELERQVALVRQ 1059
Cdd:pfam02463 604 NLAQLDKATLEADEDDkrakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSE-LTKELLEIQELQ 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1060 QSGELSMLKAKVAQTTGLMEKKD----RELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQE 1135
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEqrekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1136 EQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEK-----ANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPD 1210
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEelralEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1211 LTTLARVEIRPpQNSPFNSGSTLVMEKSVKTDAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHL 1290
Cdd:pfam02463 843 KEEQKLEKLAE-EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1291 RQKDLDLVFDKITQLKTRLQRKEELLKGYEQE-LEQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLS 1369
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
....
gi 1039768044 1370 QERR 1373
Cdd:pfam02463 1002 EEKK 1005
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
353-922 |
3.00e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 353 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALssrcsvmkeELRKE 432
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV---------EARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 433 EAQKDRREAQEkELKLCRSQMQDMEKEVRKLREELKKnymgQNIISKTLREKNKVEEKLQEDSRRKLlqlqemGNRENLI 512
Cdd:PRK02224 318 ELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADD----LEERAEELREEAAELESELEEAREAV------EDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 513 KInLERAVGQLEnfrnqvikatfgktKPFRDKPITDQQLIEKIIQVTEDnlsfqqRKWTLQRETHLHPKQEETMHSVEKL 592
Cdd:PRK02224 387 EE-LEEEIEELR--------------ERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 593 RVLLD--KCQACMrdscssidlkkevellQHLPLSPLVSGlqktvvnilrvslswLEETEQLLGDLDIELSDsdkgfslc 670
Cdd:PRK02224 446 EALLEagKCPECG----------------QPVEGSPHVET---------------IEEDRERVEELEAELED-------- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 671 liyllehykkIMSQSQDLQAQMNASRETQKSLRQ-EHLAEKEKLAEKL--EQEEKLKAK---IQQLTEEKAALEESiGQE 744
Cdd:PRK02224 487 ----------LEEEVEEVEERLERAEDLVEAEDRiERLEERREDLEELiaERRETIEEKrerAEELRERAAELEAE-AEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 745 K----SRSEEALEKAQARVRELENHLASQKEALENSvaqekRKMREMLEAERRKAQDLENQLTQQKEISENNTYEklkmR 820
Cdd:PRK02224 556 KreaaAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREALAELNDER----R 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 821 DTLEKEKRKIQDLENRLTKQKEEiELKEQKENvlnnkLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKM 900
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARIE-EAREDKER-----AEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
570 580
....*....|....*....|..
gi 1039768044 901 iltdDRLKLQQQSMKALQDERE 922
Cdd:PRK02224 701 ----EALENRVEALEALYDEAE 718
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
642-1097 |
8.38e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 642 SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKsLRQEHLAEKEKLAEKLEQEE 721
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK-KLKELEKRLEELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 722 KLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQ 801
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCPVCGRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 802 LTQQKEISENNTYeKLKMRDtLEKEKRKIQDLENRLTKQKEEIELKEQKENVLnnklkdaLVMVEDAQQMKTTESQRAET 881
Cdd:PRK03918 445 LTEEHRKELLEEY-TAELKR-IEKELKEIEEKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 882 LALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD------ERESQKHGFEEEISEYKEQIKQHS-QTIVSLEERLC 954
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 955 QVTQYYQkiegEITTLKNndtGPKEeasqdltagppLDSGDKEIacDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSR 1034
Cdd:PRK03918 596 ELEPFYN----EYLELKD---AEKE-----------LEREEKEL--KKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1035 MSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQT-------TGLMEKKDRELKVLREALRASQE 1097
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTleklkeeLEEREKAKKELEKLEKALERVEE 725
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
70-131 |
8.81e-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: 8.81e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039768044 70 SADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGMTYEL 131
Cdd:cd22704 32 SRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-943 |
8.82e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 257 EIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAaarqsnrcdPKLQGVDEGDDLRQKEIESMKSQ 336
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------PELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 337 INALQKgysqvlsqtlaerntEIESLKNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLR-IENREKEYql 415
Cdd:PRK03918 240 IEELEK---------------ELESLEGSKRKLEEK-------IRELEERIEELKKEIEELEEKVKELKeLKEKAEEY-- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 416 EALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKknymgqniisKTLREKNKVEEKLQ--E 493
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----------ELEKRLEELEERHElyE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 494 DSRRKLLQLQEMgnRENLIKINLERAVGQLENFRNqvikatfgktkpfRDKPITDQqlIEKIIqvtednlsfqqrkwtlQ 573
Cdd:PRK03918 366 EAKAKKEELERL--KKRLTGLTPEKLEKELEELEK-------------AKEEIEEE--ISKIT----------------A 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 574 RETHLHPKQEETMHSVEKLRVLLDKCQACMRDscssIDLKKEVELLQHLPLSplvsglqktvvniLRVSLSWLEETEQLL 653
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCPVCGRE----LTEEHRKELLEEYTAE-------------LKRIEKELKEIEEKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 654 GDLDIELSDSDKgfslcliyLLEHYKKIMSQsQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTE 732
Cdd:PRK03918 476 RKLRKELRELEK--------VLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEIKSLKK 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 733 EKAALEESigqeKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLENQLTQQKEise 810
Cdd:PRK03918 547 ELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEK--- 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 811 nntyEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN-NKLKDALVMVEDAQQMKTTESQRAETLALKLKET 889
Cdd:PRK03918 620 ----ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 890 LAELETTKTKMILTDDRLKLQQQSMKALQDEResqkhgfeEEISEYKEQIKQHS 943
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKALERVEELR--------EKVKKYKALLKERA 741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1035 |
1.21e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 676 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ--EEKLKAK-IQQLTEEKAALEESI--GQEKSRSEE 750
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEeAKKKAEEAKKADEAKkkAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 751 ALEKAQ---ARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK-- 825
Cdd:PTZ00121 1488 AKKKAEeakKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKae 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 826 EKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVE------------DAQQMKTTESQRAETLALKLKETLAEL 893
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeakkaeeakiKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 894 ETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYK-EQIKQHSQTIVSLEERLCQVTQYYQKIEG-----EI 967
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaeEE 1727
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 968 TTLKNNDTGPKEEASQDLTAGPPLDSGDKEiACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRM 1035
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-1064 |
3.80e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 404 LRIENREKEYQ-----LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniIS 478
Cdd:PRK03918 155 LGLDDYENAYKnlgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 479 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKinleravgQLENFRNQVIKATfgktkpfrdkpitdQQLIEKIIQV 558
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIR--------ELEERIEELKKEI--------------EELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 559 TEdnlsfqqrkwtlqrethLHPKQEETMHSVEKLRVLLDKCQacmrdscssiDLKKEVEllqhlPLSPLVSGLQKtvvni 638
Cdd:PRK03918 286 KE-----------------LKEKAEEYIKLSEFYEEYLDELR----------EIEKRLS-----RLEEEINGIEE----- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 639 lrvSLSWLEETEQLLGDLDIELSDSDKGFSlcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKle 718
Cdd:PRK03918 329 ---RIKELEEKEERLEELKKKLKELEKRLE-----ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 719 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEaLEKAQARV----RELENH-----LASQKEALENsVAQEKRKMREMLE 789
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCpvcgRELTEEhrkelLEEYTAELKR-IEKELKEIEEKER 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 790 AERRKAQDLENQLTQQKEISEN--------NTYEKLKMRDT--LEKEKRKIQDLENRLTKQKEEIE-LKE--QKENVLNN 856
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLkelaeqlkELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKsLKKelEKLEELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 857 KLKDALVMVEDAQQMKTTESQRAETLALK----LKETLAELETTKTKMIltddRLKLQQQSMKALQDERESQkhgfEEEI 932
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFEsveeLEERLKELEPFYNEYL----ELKDAEKELEREEKELKKL----EEEL 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 933 SEYKEQIKQHSQTIVSLEERLCQVTQYY-----QKIEGEITTLKNNDTGPKEEASQdltagppLDSGDKEIACDhlIDDL 1007
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEE-------LEKRREEIKKT--LEKL 699
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 1008 LMAQKEILSQQEIIMKlrtdLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGEL 1064
Cdd:PRK03918 700 KEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLKERALSKVGEIASEI 752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
637-1071 |
3.92e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 637 NILRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEK 716
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 717 LEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaqarvrELENHLASQKEALENSVAQekrkmremLEAERRKAQ 796
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK------ELKSELKNQEKKLEEIQNQ--------ISQNNKIIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 797 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLEN----------RLTKQKEEIELKEQKENVLNNKLKDALVMVE 866
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKenqsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 867 DAQQMKTTESQRAETLALKLKETLAELETTKTKMILT----DDRLKLQQQSMKALQDERESQKHGFEE----------EI 932
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 933 SEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIACDHL---IDDLLM 1009
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE---LKKENLEKEIDEKnkeIEELKQ 575
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 1010 AQKEILSQQEiimKLRTDLGEAHSRMSDLRGELSEK--QKMELERQVALVRQQSGELSMLKAKV 1071
Cdd:TIGR04523 576 TQKSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKekKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
708-1060 |
9.29e-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: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 708 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEkAQARVRELENHLasqkealensVAQEKRKMREM 787
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYE----------LLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 788 LEAERRKAQDLENQLTQ-QKEISENNTyEKLKMRDTLEKEKRKIQDL-ENRLTKQKEEIELKEQKENVLNNKLKDALVMV 865
Cdd:TIGR02169 239 KEAIERQLASLEEELEKlTEEISELEK-RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 866 EDAQ-QMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQ 941
Cdd:TIGR02169 318 EDAEeRLAKLEAEIDKLLA-EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 942 HSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltagppldsgdkeiacdhLIDDLLMAQKEILSQQEII 1021
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-------------------LEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039768044 1022 MKLRTDLGEAHSRMSDLRGELS--EKQKMELERQVALVRQQ 1060
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDrvEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
683-844 |
1.19e-08 |
|
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: 60.08 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 683 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARV 759
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 760 RELENHLASQKEALENSVAQEK----------------------RKMREMLEAERRKAQDLENQLTQQKEISENNTYEKL 817
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
170 180
....*....|....*....|....*..
gi 1039768044 818 KMRDTLEKEKRKIQDLENRLTKQKEEI 844
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-983 |
1.42e-08 |
|
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: 59.65 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 328 KEIESMKSQINALQKGYsQVLSQTLAER-------NTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEE 400
Cdd:TIGR04523 40 KKLKTIKNELKNKEKEL-KNLDKNLNKDeekinnsNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 401 VNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKlcrSQMQDMEKEVRKLREELKKNymgQNIISKT 480
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK---KQKEELENELNLLEKEKLNI---QKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 481 LREKNKVEEKLQedsrrkLLQLQEMGNRENLIKIN-LERAVGQLENFRNQVIKATFGKTKPFRDkpiTDQQLIEKIIQVT 559
Cdd:TIGR04523 193 KNKLLKLELLLS------NLKKKIQKNKSLESQISeLKKQNNQLKDNIEKKQQEINEKTTEISN---TQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 560 EDNlsfqqrkwtlqreTHLHPKQEETMHSVEKLRVLLDKCQacmrdscssiDLKKEVELLQhlplsplvsglQKTVVNIL 639
Cdd:TIGR04523 264 KIK-------------KQLSEKQKELEQNNKKIKELEKQLN----------QLKSEISDLN-----------NQKEQDWN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 640 RVSLSWLEETEQLLGDLDIELSDSDKGFSlcliyllehykKIMSQSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQ 719
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSEKQRE-LEEKQNEIEKLKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 720 E-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQArvrelenhLASQKEALEnsvaQEKRKMREMLEAERRKAQDL 798
Cdd:TIGR04523 378 EnQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK--------LQQEKELLE----KEIERLKETIIKNNSEIKDL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 799 ENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNK----------LKDALVMVEDA 868
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeleekvkdLTKKISSLKEK 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 869 QQMKTTESQRAETLALKLKETLAELETTKTKMILTD---------DRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 939
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039768044 940 KQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 983
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
683-894 |
1.65e-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: 58.24 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 683 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVREL 762
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 763 ENHLASQKEALENSVA---QEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 839
Cdd:COG4942 96 RAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 840 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETL---ALKLKETLAELE 894
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-1192 |
1.94e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 700 KSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENH------LASQK 770
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEELkeeieeLEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 771 EALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKEISEN-NTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIE 845
Cdd:PRK03918 248 ESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKaEEYIKLsEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 846 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKM-ILTDDRLKLQQQSMKALQDERESQ 924
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 925 KHGFEEEISEYKEQIKQHSQTIVSLE--ERLCQV-----------------TQYYQKIEGEITTLKNNDTGPKEEASQdl 985
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKkaKGKCPVcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 986 tagppldsgdkeiacdhlIDDLLMAQKEILSQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELS 1065
Cdd:PRK03918 485 ------------------LEKVLKKESELIKLKELAEQLK----ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1066 MLKAKVAQTTGLMEKKDRELKVLREAlrasqEKPRPHLSTEQKPRTLSQKCDISLQI---EPAHPDSFSSFQEEQSFSDL 1142
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLkelEPFYNEYLELKDAEKELERE 617
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 1143 GVKCKGSRHE-----ETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELR 1192
Cdd:PRK03918 618 EKELKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS 672
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
348-1178 |
2.35e-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: 58.98 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 348 LSQTLAERNTEIESLKnegenlkrdhaitsGMVTSLQKDMSARNEQVQQ-----LQEEVNRLRIENREKEYQLEALSSRC 422
Cdd:pfam15921 222 ISKILRELDTEISYLK--------------GRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 423 SVMKEELRKEEAQKDRREAQEK-ELKLCRSQMQDMEKEVRKLREELKKnymgqniisktlrEKNKVEEKLQEDSRRKLLQ 501
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSELRE-------------AKRMYEDKIEELEKQLVLA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 502 LQEmgnrenlikinLERAVGQLENFRNQVikatfGKTKPFRDKPITDQQLIEKiiqvtEDNLSFQQRKWTLQRET----- 576
Cdd:pfam15921 355 NSE-----------LTEARTERDQFSQES-----GNLDDQLQKLLADLHKREK-----ELSLEKEQNKRLWDRDTgnsit 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 577 --HLHPKQEETMHSVEKLRVLL----DKCQACMRDSCSSIDLKKEvellQHLPLSPLVSGLQKT------VVNILRVSLS 644
Cdd:pfam15921 414 idHLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNE----SLEKVSSLTAQLESTkemlrkVVEELTAKKM 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 645 WLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQaQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLK 724
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 725 AKIQQLTE--------------EKAALEESIGQEKSRSEE---ALEKAQARVRELE---NHLASQKEALENSVAQEKRKM 784
Cdd:pfam15921 569 QQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEarvSDLELEKVKLVNAGSERLRAV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 785 REMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIelkEQKENVLnnklkdalvm 864
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL---EQTRNTL---------- 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 865 vedaqqmKTTESqrAETLALKLKETLAELETTKTKMIltdDRLKLQQQSMKALQDERESQKHGFEEEISEykeqikqhsq 944
Cdd:pfam15921 716 -------KSMEG--SDGHAMKVAMGMQKQITAKRGQI---DALQSKIQFLEEAMTNANKEKHFLKEEKNK---------- 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 945 tivsLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIA-CDHLIddllmaQKEilSQQEIIMK 1023
Cdd:pfam15921 774 ----LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA---LDKASLQFAeCQDII------QRQ--EQESVRLK 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1024 LRTDL------GEAHSRMSDLRGELseKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRAS-Q 1096
Cdd:pfam15921 839 LQHTLdvkelqGPGYTSNSSMKPRL--LQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSViN 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1097 EKPRPHLS-TEQKPRTLS--------QKCDISLQIEPAHPDSFSSFqeeqsfsdlgVKCKGSRHEETIQRQRKALselrt 1167
Cdd:pfam15921 917 EEPTVQLSkAEDKGRAPSlgalddrvRDCIIESSLRSDICHSSSNS----------LQTEGSKSSETCSREPVLL----- 981
|
890
....*....|.
gi 1039768044 1168 RVRELEKANSC 1178
Cdd:pfam15921 982 HAGELEDPSSC 992
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
691-1440 |
2.40e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 691 QMNASRETQKSLRQEHLAEKEKLAE--KLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS 768
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 769 QKEALENSVAQEKRKMREMLEAER-RKAQDLEnQLTQQKEISENNTYEKLKMRDTLEK--EKRKIQDLEnRLTKQKEEIE 845
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEvRKAEELR-KAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVK-KAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 846 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAEtlalklkETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQK 925
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-------EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 926 HGFEEEISEYKEQIKQHSQTIVSLEERlcqvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLid 1005
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1006 dllmaqKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMlKAKVAQTTGLMEKKDREL 1085
Cdd:PTZ00121 1384 ------KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1086 KVLREALRASQEKPRP-HLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRqrkalSE 1164
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1165 LRTRVRELEKANSCNHKDHVNESfLELRTLRMEKNVQKILLDAKPDLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAG 1244
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKA-EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1245 EAL-ELSEKLYTDMIKtlgslmniKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITqlKTRLQRKEELLKgyeQEL 1323
Cdd:PTZ00121 1611 EAKkAEEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDK---KKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1324 EQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEqQLSQERRFNRVFKQQKDRGEDPEQRNMSYSPFKDNEK 1403
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
730 740 750
....*....|....*....|....*....|....*..
gi 1039768044 1404 QRrlFVEMVKSKMQNSSVQAGAKKATLKTGQERETKK 1440
Cdd:PTZ00121 1757 KK--IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
683-1415 |
2.70e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.83 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 683 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkakiqqltEEKAALEESIGQEKSRSEEALEKAQARV--R 760
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK----------EEEKEKKLQEEELKLLAKEEEELKSELLklE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 761 ELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKiqdLENRLTKQ 840
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL---EEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 841 KEEIELKEQKENVLNNKLKDALVMvEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 920
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 921 RESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIAC 1000
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ-----KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1001 DHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSmlkakVAQTTGLMEK 1080
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE-----IDPILNLAQL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1081 KDRELKVLREALRAsqekprphlsteqKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQRK 1160
Cdd:pfam02463 609 DKATLEADEDDKRA-------------KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1161 ALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPDLTTLARVEIrPPQNSPFNSGSTLVMEKSVK 1240
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-NEELKLLKQKIDEEEEEEEK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1241 T--DAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLdlvfDKITQLKTRLQRKEELLKG 1318
Cdd:pfam02463 755 SrlKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK----EEAELLEEEQLLIEQEEKI 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1319 YEQELEQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLSQERRFNRVFKQQKDRGEDPEQRNMSYSPF 1398
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
730
....*....|....*..
gi 1039768044 1399 KDNEKQRRLFVEMVKSK 1415
Cdd:pfam02463 911 LLEEKENEIEERIKEEA 927
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
707-971 |
2.74e-08 |
|
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: 58.93 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 707 LAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEES-IGQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMR 785
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYeLLKEKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 786 EMLEAERRKAQDL--ENQLTQQKEISENnTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENVLN-----NK 857
Cdd:TIGR02169 272 QLLEELNKKIKDLgeEEQLRVKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDkLLAEIEELEReieeeRK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 858 LKDALV-MVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYK 936
Cdd:TIGR02169 351 RRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270
....*....|....*....|....*....|....*
gi 1039768044 937 EQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 971
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
646-938 |
3.90e-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: 57.38 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 646 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkiMSQSQDLQAQMNASRETQKSLRQE--HLAEKEKLAEKLEQE--- 720
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEEnkALREEAQAAEKALQRaeg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 721 ------------EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQ--------- 779
Cdd:pfam19220 161 elatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 780 -EKRKMREMLEAERRKAQDLENQLTQQkeisenntyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKL 858
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEA--------------RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 859 KDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRlklqqqsMKALQDERESQKHGFEEEISEYKEQ 938
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDR-------IAELTKRFEVERAALEQANRRLKEE 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
694-924 |
4.16e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 694 ASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLAS---QK 770
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAElekEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 771 EALENSVAQEKRKMREMLeaerRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 850
Cdd:COG4942 93 AELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 851 ENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQ 924
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
675-941 |
5.45e-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: 57.44 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 675 LEHYKKIMSQSQDLQAQMNasRETQKSLRQEHLA-EKEKLAEKLEQEEKlKAKIQQLTEEKAALE--------------- 738
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMD--RQAAIYAEQERMAmERERELERIRQEER-KRELERIRQEEIAMEisrmrelerlqmerq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 739 ---ESIGQE-------KSRSEEALEKAQARVRELENHLASQKEALENSVAQ-EKRKMREMleaERRKAQDLENQltQQKE 807
Cdd:pfam17380 389 qknERVRQEleaarkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREM---ERVRLEEQERQ--QQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 808 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENVLNNKLKDALV--MVEDAQQMKTTESQRAETlalk 885
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLekEMEERQKAIYEEERRREA---- 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768044 886 lketlaelETTKTKMILTDDRLKLQQQSMKAlqDERESQKHGFEEEiSEYKEQIKQ 941
Cdd:pfam17380 539 --------EEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMERE-REMMRQIVE 583
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1294 |
6.22e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 676 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ-EEKLKAKIQQLTEEKAALEES--IGQEKSRSEEAL 752
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 753 EKAQ---ARVRELENHLASQKEALE-NSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENNTYEKLKMRdtlEKEKR 828
Cdd:PTZ00121 1398 KKAEedkKKADELKKAAAAKKKADEaKKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 829 KIQDLENRLTKQKEEIELKEQKENVLN--NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDR 906
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 907 LKLQQQSMKALQDERESQKHGFEEEiseyKEQIKQHSQTIVSLEERlcqvtqyyqKIEGEITTLKNNDTGPKEEASQDLT 986
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEA---------RIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 987 AGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEiimKLRTDLGEAHSRMSDL-RGELSEKQKMELERQVALVRQQSGELS 1065
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1066 MLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSF-QEEQSFSDLGV 1144
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLkKEEEKKAEEIR 1774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1145 KCKGSRHEETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELRTLR-MEKNVQKILLDAKpdltTLARVEIRPPQ 1223
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKeMEDSAIKEVADSK----NMQLEEADAFE 1850
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768044 1224 NSPFNSGSTLVMEKSVKTDAGEALELSEK-----LYTDMIKTLgslmNIKDMSSHTSLKHLSPKEREKVNHLRQKD 1294
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDdeeeiEEADEIEKI----DKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
701-1442 |
6.62e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 701 SLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL-------ENHLASQKEA 772
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEEtENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldyLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 773 LE---NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQ 849
Cdd:pfam02463 242 LQellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 850 KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE 929
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 930 EEISEYKEQIkQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLM 1009
Cdd:pfam02463 402 EEEKEAQLLL-ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1010 AQKEILSQQEIIMKLRTDL-GEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVL 1088
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSqKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1089 REALRASQEKP---------RPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQR 1159
Cdd:pfam02463 561 EERQKLVRALTelplgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1160 -KALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPdLTTLARVEIRPPQNSPFNSGSTLVMEKS 1238
Cdd:pfam02463 641 aKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK-EEILRRQLEIKKKEQREKEELKKLKLEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1239 VKTDAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITQLKTRLQRKEELLKG 1318
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1319 YEQELEQLRHSKVSVQMYQTQVAKLEDDVH-KEAEEKALLKEALERTEQQLSQERRFNRVFKQQKDRGEDPEQRNMSYSP 1397
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKiKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1039768044 1398 FKDNEKQRRLFVEMVKSKMQNSSVQAGAKKATLKTGQERETKKEA 1442
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
679-876 |
9.48e-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: 55.93 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 679 KKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 755
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAAleRRIAALARRIRALEQElAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 756 QARVR-ELENHLASQKEALE--------NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE 826
Cdd:COG4942 114 YRLGRqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 827 K----RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTES 876
Cdd:COG4942 194 KaerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
73-130 |
9.83e-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: 9.83e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 73 IDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAGMTYE 130
Cdd:cd22665 40 VSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVKCQYV 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
697-1428 |
1.42e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 697 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQqltEEKAALEESIGQEKSRSEEALEKAQARvRELENHLASQKEALENS 776
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFAR-RQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 777 VAQEKRKMREMLEA-ERRKAQDLENQLTQQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 855
Cdd:PTZ00121 1285 KAEEKKKADEAKKAeEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 856 NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiltddrlklqqqsmKALQDERESQKHGFEEEISEY 935
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK-----------------KAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 936 KEQIKQHSQTIVSLEErlcqvtqyyqkiegeiTTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQKEIL 1015
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADE----------------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1016 SQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLME--KKDRELKVLREALR 1093
Cdd:PTZ00121 1484 KADEAKKKAE----EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1094 ASQEKPRPHLSTEQKPRTLS-QKCDISLQIEPAHPDSFSSFQEEQsfsdlgvkcKGSRHEETIQRQRKALSELRTRVREL 1172
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEE---------KKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1173 EKANSCNHKDHVNESFLELRTLRMEKNVQKIlldAKPDLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAGEALELSEk 1252
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1253 lytdmiktlgslmnikdmsshtsLKHLSPKEREKVNHLRQKDlDLVFDKITQLKtrlqRKEELLKGYEQELEQLRHSKVS 1332
Cdd:PTZ00121 1707 -----------------------LKKKEAEEKKKAEELKKAE-EENKIKAEEAK----KEAEEDKKKAEEAKKDEEEKKK 1758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1333 VQMYQTQVAKLEDDVHKEAEekALLKEALERTEQQLSQErrFNRVFKQQKDRGEDPEQRNMSYSPFKDNEKQrrLFVEMV 1412
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKE--AVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIEGGKEGNLVINDSKE--MEDSAI 1832
|
730
....*....|....*.
gi 1039768044 1413 KSKMQNSSVQAGAKKA 1428
Cdd:PTZ00121 1833 KEVADSKNMQLEEADA 1848
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
430-894 |
1.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 430 RKEEAQKDRREAQEKELKLcrsqmQDMEKEVRKLREELKknymgqniisktlREKNKVEEKLQEDSRRKLLQLQEMGNRE 509
Cdd:COG1196 173 RKEEAERKLEATEENLERL-----EDILGELERQLEPLE-------------RQAEKAERYRELKEELKELEAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 510 NLIKINLERAVGQLENFRNQVIKATfgktkpfrdkpiTDQQLIEKIIQVTEDnlsfqqrkwtlqrethlhpkqeetmhSV 589
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELE------------AELAELEAELEELRL--------------------------EL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 590 EKLRVLLDKCQAcmrdscssidlkKEVELLQhlplsplvsglqktvvnilrvslswleETEQLLGDLDIELsdsdkgfsl 669
Cdd:COG1196 277 EELELELEEAQA------------EEYELLA---------------------------ELARLEQDIARLE--------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 670 cliyllehykkimSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSE 749
Cdd:COG1196 309 -------------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE----ALLEAE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 750 EALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTyEKLKMRDTLEKEKRK 829
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEEEALEEAAEE 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 830 IQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 894
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-899 |
1.86e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 394 VQQLQEEVNRL-RIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnYM 472
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 473 GQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKinleravgQLENFRNQVIKATFGKTKPFRDKPITDQQLI 552
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE--------ELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 553 EKIIQVTEDnlsFQQRKWTLQREthLHPKQEEtmhsVEKLRVLLDKCQACMRDscssidlKKEVELLQHLPLSPLVSGLq 632
Cdd:COG4717 195 QDLAEELEE---LQQRLAELEEE--LEEAQEE----LEELEEELEQLENELEA-------AALEERLKEARLLLLIAAA- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 633 ktVVNILRVSLSWLEETEQLLGDLDIELsdsdkGFSLCLIYLLEHYKKIMSQSQDlQAQMNASRETQKSLRQEHLAEKEK 712
Cdd:COG4717 258 --LLALLGLGGSLLSLILTIAGVLFLVL-----GLLALLFLLLAREKASLGKEAE-ELQALPALEELEEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 713 LAEKLEQEEkLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVreLENHLASQKEALEnSVAQEKRKMREMLEAER 792
Cdd:COG4717 330 LPPDLSPEE-LLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELR-AALEQAEEYQELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 793 RKAQDLENQLTQQKEISENNTYEKLKMRdtLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNklkDALVMVEDAQQM 871
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELaELEAELEQLEED---GELAELLQELEE 480
|
490 500
....*....|....*....|....*...
gi 1039768044 872 KTTESQRAETLALKLKETLAELETTKTK 899
Cdd:COG4717 481 LKAELRELAEEWAALKLALELLEEAREE 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
676-1369 |
2.35e-07 |
|
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: 55.89 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 676 EHYKKIMS----QSQDLQAQMNASREtqkslrqehLAEKEKLAEKlEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA 751
Cdd:pfam15921 74 EHIERVLEeyshQVKDLQRRLNESNE---------LHEKQKFYLR-QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 752 LEKAQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKAQDLENQLTQQKEISENNTYEK--------------- 816
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHdsmstmhfrslgsai 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 817 LKMRDTLEKE----KRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLk 887
Cdd:pfam15921 223 SKILRELDTEisylKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 888 ETLAELETTKTKMILTddRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEI 967
Cdd:pfam15921 302 EIIQEQARNQNSMYMR--QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 968 TTLKNNDTGPKEEASQDLTAGPPL---DSGDkEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL-GEAHSRMSDLRGels 1043
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLwdrDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQG--- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1044 ekQKMELERQVALVRQQSGELSMLKAKVAQTTG---LMEKKDRELKVLREALrasQEKPRPHLSTEQKPRTLSQKCDISL 1120
Cdd:pfam15921 456 --KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASL---QEKERAIEATNAEITKLRSRVDLKL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1121 QiEPAHPDSfssfqEEQSFSDLGVKCKGSRHEETiqRQRKALSELRTRVRELEKANScNHKDHVNESFLELRTLRMEKNV 1200
Cdd:pfam15921 531 Q-ELQHLKN-----EGDHLRNVQTECEALKLQMA--EKDKVIEILRQQIENMTQLVG-QHGRTAGAMQVEKAQLEKEIND 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1201 QKILLDAKPDLTTLARVEIRPPQNSPfnsgSTLVMEKSVKTDAGealelSEKLYT--DMIKTLGSLMNiKDMSSHTSLKH 1278
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARV----SDLELEKVKLVNAG-----SERLRAvkDIKQERDQLLN-EVKTSRNELNS 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1279 LSPKEREKVNHLRQKDLDLvfdKITQLKTRLQrkeelLKGYEQELEQLRHS------------KVSVQM----------- 1335
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEM---ETTTNKLKMQ-----LKSAQSELEQTRNTlksmegsdghamKVAMGMqkqitakrgqi 743
|
730 740 750
....*....|....*....|....*....|....*.
gi 1039768044 1336 --YQTQVAKLEDDVHKEAEEKALLKEALERTEQQLS 1369
Cdd:pfam15921 744 daLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
675-1114 |
3.77e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 675 LEHYKKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAKIQQ---LTEEKAALEESIGQEKSRSE 749
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKLLQllpLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 750 EaLEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRK 829
Cdd:COG4717 150 E-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 830 IQDLENRLTKQKEEIELKEQKE----------------NVLNNKLKDA--------LVMVEDAQQMKTTESQRAETLALK 885
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 886 LKETLAELETTKTKMILTDDRLK-----------------LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSqtIVS 948
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPpdlspeellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEAGVED--EEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 949 LEERLCQVTQyYQKIEGEITTLKNNdtgpkeeasqdltagppLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL 1028
Cdd:COG4717 387 LRAALEQAEE-YQELKEELEELEEQ-----------------LEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1029 GEAHSRMSDLRGELSEkqkMELERQVALVRQqsgELSMLKAKVAQttglMEKKDRELKVLREALRASQEkprpHLSTEQK 1108
Cdd:COG4717 449 EELREELAELEAELEQ---LEEDGELAELLQ---ELEELKAELRE----LAEEWAALKLALELLEEARE----EYREERL 514
|
....*.
gi 1039768044 1109 PRTLSQ 1114
Cdd:COG4717 515 PPVLER 520
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
749-903 |
3.87e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 749 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAE----RRKAQDLENQLTQQKEISENNTyeklkmrDTLE 824
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRKL-------ELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 825 KEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV-----EDAQQM---KTTESQRAETLAL-KLKETLAELET 895
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEA 186
|
....*....
gi 1039768044 896 TKT-KMILT 903
Cdd:PRK12704 187 DKKaKEILA 195
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-124 |
4.29e-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: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 12 FVLNKST-TIGKHADSDLVLQDHLVRGqhhpqwpgpstsiinqehapppglctcrsdaesadidnHHALIEFNEaeGTFV 90
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSS--------------------------------------RHARIYLQG--SSWY 52
|
90 100 110
....*....|....*....|....*....|....
gi 1039768044 91 LQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 124
Cdd:cd22693 53 LEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
687-861 |
5.16e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 687 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA---LEKAQARVRELE 763
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 764 NH-----LASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyeklkmrdTLEKEKRKIQDLENRLT 838
Cdd:COG3206 289 NHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA--------------QLEARLAELPELEAELR 354
|
170 180
....*....|....*....|...
gi 1039768044 839 KQKEEIELKEQKENVLNNKLKDA 861
Cdd:COG3206 355 RLEREVEVARELYESLLQRLEEA 377
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
697-961 |
7.77e-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: 53.53 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 697 ETQKSLRqehlAEKEKLAEKLEQEEKL-KAKIQQLTEEKAALEEsigqEKsrseealEKAQARVRELENHLASQKEALEN 775
Cdd:pfam15070 4 ESLKQLQ----TERDQYAENLKEEGAVwQQKMQQLSEQVRTLRE----EK-------ERSVSQVQELETSLAELKNQAAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 776 SVAQEKRKMREMLEAERRKAQDLEnQLTQQKEISENNTYEKLKMRDTL-----EKEKRkIQDLENRLTKQKEEIELKEQk 850
Cdd:pfam15070 69 PPAEEEQPPAGPSEEEQRLQEEAE-QLQKELEALAGQLQAQVQDNEQLsrlnqEQEQR-LLELERAAERWGEQAEDRKQ- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 851 envlnnklkdalvMVEDAQQMKTTESqRAETLALKLKETLAELETTKTKmiLTDDRLKLqqqsMKALQDERESQKH---- 926
Cdd:pfam15070 146 -------------ILEDMQSDRATIS-RALSQNRELKEQLAELQNGFVK--LTNENMEL----TSALQSEQHVKKElakk 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039768044 927 --GFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 961
Cdd:pfam15070 206 lgQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQ 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
353-937 |
8.05e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 353 AERNTEIESLKNEGENLKR-DHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRK 431
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 432 EEAQKDRREAQEK----ELKLCRSQMQDMEKEVRKLREELKKNYMGQNI---ISKTLREKNKVEEKLQEDSRRKllQLQE 504
Cdd:PTZ00121 1378 KKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAKK--KAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 505 MGNRENLIKINLE-RAVGQLENFRNQVIKATFGKTKPFRDKPITDQ--QLIEKIIQVTEDNLSFQQRKWTLQRETHLHPK 581
Cdd:PTZ00121 1456 AKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 582 QEETMHSVEKLRV-LLDKCQACMR-DSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIE 659
Cdd:PTZ00121 1536 ADEAKKAEEKKKAdELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 660 LSDSDKGFSLcliYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKlkaKIQQLTEEKAALEE 739
Cdd:PTZ00121 1616 EEAKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 740 SIGQEKSRSEEALEKAQARVRELENHLASQ---KEALENSVAQEKRKMREmlEAERRKAQDL------ENQLTQQKEISE 810
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIKAEEAKKEA--EEDKKKAEEAkkdeeeKKKIAHLKKEEE 1767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 811 NNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVmVEDAQQMKTTESQRAETLALKLKETL 890
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV-INDSKEMEDSAIKEVADSKNMQLEEA 1846
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1039768044 891 AELETTKtkmiLTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKE 937
Cdd:PTZ00121 1847 DAFEKHK----FNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
359-469 |
1.31e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.94 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 359 IESLKNEGENLKRDHAITsgMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL---RKEEAQ 435
Cdd:COG2433 382 LEELIEKELPEEEPEAER--EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseaRSEERR 459
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039768044 436 KDRREAQ----EKELKLCRSQMQDMEKEVRKLREELKK 469
Cdd:COG2433 460 EIRKDREisrlDREIERLERELEEERERIEELKRKLER 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
359-844 |
1.75e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 359 IESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDR 438
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 439 REAqEKELKLCRSQMQDMEKEVRKLREELKKnymgqniISKTLREKNKVEEKLQEDSRrkllQLQEMGNRENLIKIN-LE 517
Cdd:COG4717 128 LPL-YQELEALEAELAELPERLEELEERLEE-------LRELEEELEELEAELAELQE----ELEELLEQLSLATEEeLQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 518 RAVGQLENFRNQVikatfgktkpfrdkpitdqQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLd 597
Cdd:COG4717 196 DLAEELEELQQRL-------------------AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 598 kcqacmrdscsSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEH 677
Cdd:COG4717 256 -----------AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 678 YKKIMSQSQDLQAQMNASRETQKSLrQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAlEKAQA 757
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 758 RVRELENHLASQ-KEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ-QKEISE-NNTYEKLKMRDTLEKEKRKIQDLE 834
Cdd:COG4717 403 ELEELEEQLEELlGELEELLEALDEEELEEELEELEEELEELEEELEElREELAElEAELEQLEEDGELAELLQELEELK 482
|
490
....*....|
gi 1039768044 835 NRLTKQKEEI 844
Cdd:COG4717 483 AELRELAEEW 492
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
49-219 |
2.02e-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: 52.07 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 49 SIINQEHAPPPGLCTCRSDAESADI----DNH-------------HALIEFneAEGTFVLQDfNSRNGTFVNECHI---Q 108
Cdd:COG3456 6 RIINSPDLESGSAASATFGRGGGTIgrsaDCDwvlpdpdrsvsrrHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 109 NVAVKLIPGDILRFGSagmtYEL---VIENPSPVSCPWVRGPAPWPSPQPHLS--SSPPDMPFHHGIQPATVQRSWSQGC 183
Cdd:COG3456 83 GRPVRLRDGDRLRIGD----YEIrveISGEDEGADDPLAAAPEPAVSSPSNLSdtEAAPDAALAFSFSLDPLEALDEAAT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039768044 184 PRPTMVPPAPHQRPMSASGKMFSFVMDPKSPVINQV 219
Cdd:COG3456 159 EAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQL 194
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
683-850 |
2.49e-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: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 683 SQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL 762
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 763 ENH------------------LASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 824
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 1039768044 825 KEKRKIQDLENRLTKQKEEIELKEQK 850
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-1097 |
2.57e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 330 IESMKSQINALQKgysqvlsQtlAERNTEIESLKNEGENLkrDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENR 409
Cdd:TIGR02168 195 LNELERQLKSLER-------Q--AEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 410 EKEYQLEALSSRCSVMKEELrkeeaqkdrrEAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniISKTLREKNKVEE 489
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEI----------EELQKELYALANEISRLEQQKQILRERLAN-------LERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 490 KLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVikatfgktKPFRDKPITDQQLIEkiiqvtednlsfqqrk 569
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLE---------------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 570 wTLQRETHLHPKQEETmhsveklrvlldkcqacmrdscssidLKKEVELLqhlplSPLVSGLQKTVvnilrvslswlEET 649
Cdd:TIGR02168 383 -TLRSKVAQLELQIAS--------------------------LNNEIERL-----EARLERLEDRR-----------ERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 650 EQLLGDLDIELSDSDKgfslcliyllehyKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQ 729
Cdd:TIGR02168 420 QQEIEELLKKLEEAEL-------------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 730 LTEEKAALEesigqeksRSEEALEKAQARVRELENHlASQKEALENSVAQ----EKRKMREMLEAERRKAQDL--ENQLT 803
Cdd:TIGR02168 487 LQARLDSLE--------RLQENLEGFSEGVKALLKN-QSGLSGILGVLSElisvDEGYEAAIEAALGGRLQAVvvENLNA 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 804 QQKEIS---ENNT-------YEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVM--VEDAQQM 871
Cdd:TIGR02168 558 AKKAIAflkQNELgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddLDNALEL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 872 K-----------------------TTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGF 928
Cdd:TIGR02168 638 AkklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 929 EEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltAGPPLDSGDKEIA-----CDHL 1003
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEeleaqIEQL 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1004 IDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDR 1083
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
810
....*....|....
gi 1039768044 1084 ELKVLREALRASQE 1097
Cdd:TIGR02168 874 ELEALLNERASLEE 887
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
392-1136 |
3.30e-06 |
|
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: 51.89 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 392 EQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL-RKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKn 470
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 471 ymgqniisktLREKNKVEEKLQEDSRR-KLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFgktkpfrdkpitDQ 549
Cdd:TIGR00618 252 ----------QEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ------------QA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 550 QLIEKIIQVTEDNLS--FQQRKWTLQRETHLHPKQ--EETMHSVEKLRVLLDKCQACMRDscssiDLKKEVELLQHLpls 625
Cdd:TIGR00618 310 QRIHTELQSKMRSRAklLMKRAAHVKQQSSIEEQRrlLQTLHSQEIHIRDAHEVATSIRE-----ISCQQHTLTQHI--- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 626 pLVSGLQKTVVNILRVSLSWLEETEQ-LLGDLDIELSDsdkgFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQ 704
Cdd:TIGR00618 382 -HTLQQQKTTLTQKLQSLCKELDILQrEQATIDTRTSA----FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 705 EHLAEKE---KLAEKLEQEEKLKAKIQQLTEEKAA----LEESIGQEKSRSEEALEKAQARVRELENH-LASQKEALENS 776
Cdd:TIGR00618 457 EKIHLQEsaqSLKEREQQLQTKEQIHLQETRKKAVvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 777 VA---QEKRKMREMLEAERRKAQDLENQLTqqkeiSENNTYEKLKMRDTLEKEK-RKIQDLENRLTKQKEEIELKEQKEN 852
Cdd:TIGR00618 537 YAqleTSEEDVYHQLTSERKQRASLKEQMQ-----EIQQSFSILTQCDNRSKEDiPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 853 VLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE-EE 931
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEkEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 932 ISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL-------DSGDKEIACDHLI 1004
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQartvlkaRTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1005 DDLLMAQKEILSQQEIIMKLRtDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRE 1084
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNR-LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1039768044 1085 LKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahPDSFSSFQEE 1136
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD---GDALIKFLHE 899
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
675-951 |
3.48e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 675 LEHYKKIMSQSQDLQAQMNA-SRETQKSLRQEHLAEKEKLAEKL--EQEEKLKAKIQQLTEEKAALEESIGQEKS--RSE 749
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINIlEMRLSETDARIKLAAQEKIHVEIleEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 750 EALEKAQARVreLENHLASQKEALENSVAQEKRkmREMLEAERRkaqDLENQL-TQQKEISENNTYEKlkmrDTLEKEKR 828
Cdd:PLN02939 235 NMLLKDDIQF--LKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 829 KIQDLENRLTKQKEEIELKEQKENVLNNKLKdalvmvedaqqmkttesqraetlalKLKETLAELETTKtkmiLTDDRLK 908
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVE 354
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1039768044 909 LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 951
Cdd:PLN02939 355 LLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
681-816 |
4.94e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.17 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 681 IMSQSQDLQAQMNASRETQKSlrQEHLaEKEKLAEKLEQEEKlKAKIQQLTEEKAALE---ESIGQEKSRSEEALEKAQA 757
Cdd:PTZ00491 659 ITTKSQEAAARHQAELLEQEA--RGRL-ERQKMHDKAKAEEQ-RTKLLELQAESAAVEssgQSRAEALAEAEARLIEAEA 734
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 758 RVRELEnhLASQKEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEIS--ENNTYEK 816
Cdd:PTZ00491 735 EVEQAE--LRAKALRIEAEAELEKLRKRQELELEYEQAQN-ELEIAKAKELAdiEATKFER 792
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
715-951 |
6.78e-06 |
|
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: 50.88 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 715 EKLEQ-EEKLKAKIQQLTEEKAALEEsIGQEKSRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMLEAE 791
Cdd:pfam05483 370 QRLEKnEDQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 792 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD---------LENRLTKQKEE---IELKEQKENVLNNKlK 859
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQEASdmtLELKKHQEDIINCK-K 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 860 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 939
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250
....*....|..
gi 1039768044 940 KQHSQTIVSLEE 951
Cdd:pfam05483 604 ENKNKNIEELHQ 615
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
246-505 |
9.37e-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: 50.12 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 246 MDHDLSQQDKDEiillLGREVNRLSDFEMESKYKDALiMNLQAEVADLSQRLsetaavaaARQSNRCDPKLQGVD---EG 322
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM--------AMERERELERIRQEErkrEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 323 DDLRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDHAITSGMVTSLQKDMSARNEQVQQL 397
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 398 QEE----VNRLRIENREKEYQLEAL--------SSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLRE 465
Cdd:pfam17380 441 EEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1039768044 466 ELKKNymgQNIISKTLREKNKVEE--KLQEDSRRKLLQLQEM 505
Cdd:pfam17380 521 EMEER---QKAIYEEERRREAEEErrKQQEMEERRRIQEQMR 559
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
674-860 |
1.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 674 LLEHYKKIMS---------QSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE------EKLKAKIQQLTEEKAALE 738
Cdd:COG4913 230 LVEHFDDLERahealedarEQIELLEPIRELAERYAAARER-LAELEYLRAALRLWfaqrrlELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 739 EsigqEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENN-- 812
Cdd:COG4913 309 A----ELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039768044 813 TYEKLK--MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKD 860
Cdd:COG4913 381 EFAALRaeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
69-123 |
1.21e-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: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 69 ESADIDNHHALIEFnEAEGTFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 123
Cdd:cd22683 36 SDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
686-826 |
1.53e-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: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 686 QDLQAQMNASRETQKSLRQEHLAEKEKLAE-KLEQEEKLKAKIQQLTEEKAALE----------ESIGQEKSRSEEALEK 754
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039768044 755 AQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNtyekLKMRDTLEKE 826
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL----LALRDALAEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-539 |
1.53e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 326 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR 405
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 406 --IENREKEY--QLEAL--SSRCSVMKEELRKE----------------EAQKDRREAQEKELKLCRSQMQDMEKEVRKL 463
Cdd:COG4942 97 aeLEAQKEELaeLLRALyrLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768044 464 REELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTK 539
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
689-952 |
1.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 689 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESIGQEKSRSEEALEKAQA--RVRELENH 765
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 766 LASQKEALE--NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK---EKRKIQDLENRLTKQ 840
Cdd:PTZ00121 1324 AEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 841 KEEI-ELK---EQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKET--LAELETTKTKMILTDDRLKLQQQSM 914
Cdd:PTZ00121 1404 KKKAdELKkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039768044 915 KALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEER 952
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
708-894 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 708 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREM 787
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 788 LEAERRK-----------AQDLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN 856
Cdd:COG3883 96 YRSGGSVsyldvllgsesFSDFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039768044 857 KLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 894
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
682-1174 |
1.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 682 MSQSQDLQAQMNAsRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESigqeKSRSEEALEKAQARVR 760
Cdd:PTZ00121 1262 MAHFARRQAAIKA-EEARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEA----KKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 761 ELEnhlaSQKEALENSVAQEKRKMREMLEAERR-KAQDLENQLTQQKEISENNTYEKLKMRDTL----EKEKRKIQDLEN 835
Cdd:PTZ00121 1337 KAE----EAKKAAEAAKAEAEAAADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaEEDKKKADELKK 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 836 RLTKQKEEIELKEQKENVlnNKLKDALVMVEDAQQM-----KTTESQRAETLALKLKETLAELETTKTkmilTDDRLKLQ 910
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 911 QQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 990
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 991 LDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAK 1070
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1071 VAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahpdsfssfqEEQSFSDLGVKCKGSR 1150
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAEELKKKEAE 1713
|
490 500
....*....|....*....|....
gi 1039768044 1151 HEETIQRQRKALSELRTRVRELEK 1174
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
709-1370 |
1.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 709 EKEKLAEKLEQEEKLKAKIQQLTEEKAALEES--IGQEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKM 784
Cdd:PRK03918 136 EIDAILESDESREKVVRQILGLDDYENAYKNLgeVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 785 REMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNnklkdalvm 864
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 865 vedaqqmkttESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQhsq 944
Cdd:PRK03918 287 ----------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKE--- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 945 tivsLEERLCQVTQYYQKIEgEITTLKNNdtgpKEEASQDLTAGPPldsgdkeiacDHLIDDLLMAQKEILSQQEIIMKL 1024
Cdd:PRK03918 350 ----LEKRLEELEERHELYE-EAKAKKEE----LERLKKRLTGLTP----------EKLEKELEELEKAKEEIEEEISKI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1025 RTDLGEAHSRMSDLRGELSEKQK-----------MELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLrEALR 1093
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1094 ASQEKPRPHLSTEQKPRTLSQKCDiSLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHE-ETIQRQRKALSELRTRVREL 1172
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElEKLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1173 EKANSCNHKDHVNESF-----LELRTLRMEKNVQKI--LLDAKPDLTtlarveirppqnspfnsgSTLVMEKSVKTDAGE 1245
Cdd:PRK03918 569 EEELAELLKELEELGFesveeLEERLKELEPFYNEYleLKDAEKELE------------------REEKELKKLEEELDK 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1246 ALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDldlvfDKITQLKTRLQRKEELLKGYEQELEQ 1325
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-----AELEELEKRREEIKKTLEKLKEELEE 705
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039768044 1326 LRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKE-ALERTEQQLSQ 1370
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVGEIASE 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-741 |
1.75e-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: 49.67 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 353 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKE 432
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 433 EAQKDRR-------EAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNI----ISKTLREKNKVEEKLQEDSRRKLLQ 501
Cdd:TIGR02168 746 EERIAQLskeltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 502 LQEMGNRENLIKINLERAVGQLENFRNQVIKATfgktkpfrdKPITDQQ-LIEKIIQVTEdnlSFQQRKWTLQRETHLHP 580
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLA---------AEIEELEeLIEELESELE---ALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 581 KQEETMhsVEKLRVLLDKCQacmrdscssiDLKKEVELLQHLpLSPLVSGLQKTVVNILRVslswleeTEQLLGDLDIEL 660
Cdd:TIGR02168 894 SELEEL--SEELRELESKRS----------ELRRELEELREK-LAQLELRLEGLEVRIDNL-------QERLSEEYSLTL 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 661 SDsdkgfslcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEES 740
Cdd:TIGR02168 954 EE-----------AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
.
gi 1039768044 741 I 741
Cdd:TIGR02168 1023 I 1023
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
64-123 |
2.27e-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: 2.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 64 CRSDAESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 123
Cdd:cd22724 30 CELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
646-807 |
2.42e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 646 LEETEQLLGDLDIELSDsdkgfslcLIYLLEHYKKIMSQSQDLQAQMNASRETQkSLRQEHLAEKEKLAEKLEQEEKLKA 725
Cdd:COG3206 221 LSELESQLAEARAELAE--------AEARLAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 726 KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRK--AQDLENQLT 803
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevARELYESLL 371
|
....
gi 1039768044 804 QQKE 807
Cdd:COG3206 372 QRLE 375
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
377-1096 |
2.55e-05 |
|
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: 49.27 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 377 SGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELklcrsqmQDM 456
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI-------LEL 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 457 EKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQED-SRRKLLQLQEMGNRENLIKINLER-------AVGQLENFRN 528
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDrKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdKDEQIRKIKS 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 529 QVIKATFGKTKPFRDKPITDQQL--IEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEEtmhsvEKLRVLLDKCQACMRDS 606
Cdd:TIGR00606 557 RHSDELTSLLGYFPNKKQLEDWLhsKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-----ESKEEQLSSYEDKLFDV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 607 CSSIDLKKEVELLqhlplsplvsglqKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQ 686
Cdd:TIGR00606 632 CGSQDEESDLERL-------------KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 687 DLQAQMNASRETQKSLrqehlaekEKLAEKLEQEEKLkakIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHL 766
Cdd:TIGR00606 699 DLQSKLRLAPDKLKST--------ESELKKKEKRRDE---MLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 767 ASQKEALENSVAQEKRK---MREMLEAERRKAQDLENQLTQQKEISENNTYEklkMRDTLEKEKRKIQDLENRLTKQKEE 843
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAkvcLTDVTIMERFQMELKDVERKIAQQAAKLQGSD---LDRTVQQVNQEKQEKQHELDTVVSK 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 844 IEL-----KEQKENVLN-----NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQS 913
Cdd:TIGR00606 845 IELnrkliQDQQEQIQHlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 914 MKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQK-IEGEITTLK---NNDTGPKEEASQDL-TAG 988
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNaqlEECEKHQEKINEDMrLMR 1004
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 989 PPLDSGDKeiacdhliddllmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQqsgELSMLK 1068
Cdd:TIGR00606 1005 QDIDTQKI--------------QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEE---NIDLIK 1067
|
730 740
....*....|....*....|....*...
gi 1039768044 1069 AKVAQTTGLMEKKDRELKVLREALRASQ 1096
Cdd:TIGR00606 1068 RNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
694-1197 |
2.73e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 694 ASRETQKSLRQEHLAEKEKLAEkLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELE------NHL 766
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 767 ASQKEALENsvaqEKRKMREMLEAERRKAQDLENQ---LTQQKEISENNTYEKLKMRDTLEKEkrkIQDLENRLTKQKEE 843
Cdd:PRK02224 313 EARREELED----RDEELRDRLEECRVAAQAHNEEaesLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 844 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmilTDDRLKLQQQsmkaLQDERES 923
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT-------ARERVEEAEA----LLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 924 QKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNndtgpkeeasqdltagppLDSGDKEIacDHL 1003
Cdd:PRK02224 455 PECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED------------------LVEAEDRI--ERL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1004 IDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQK--MELERQVALVRQQSGELSMLKA----------KV 1071
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaAEAEEEAEEAREEVAELNSKLAelkeriesleRI 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1072 AQTTGLMEKKDRELKVLREALRASQEKprphlsTEQKPRTLSQKCDISLQIEPAHPDsfSSFQEEQSfsdlgvkcKGSRH 1151
Cdd:PRK02224 595 RTLLAAIADAEDEIERLREKREALAEL------NDERRERLAEKRERKRELEAEFDE--ARIEEARE--------DKERA 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1039768044 1152 EETIQRQRKALSELRTRVRELEKANSCnhkdhVNESFLELRTLRME 1197
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGA-----VENELEELEELRER 699
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
634-764 |
3.03e-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: 47.70 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 634 TVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLqaqMNASRETQKSLRQEHLAEKEKL 713
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE---LDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 714 AEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA-------LEKAQARVRELEN 764
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKLLQS 285
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
632-893 |
3.05e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 632 QKTVVNILRVSLSWLEETEQLLGDLDielsdsdkgfslcliylleHYKKIMSQ----SQDLQAQMNASRETQKSLRqEHL 707
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAK-------------------QYQQVIDNfpklSAELRQQLNNERDEPRSVP-PNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 708 AEKEklaekLEQeEKLKAKIQQLTEEKAALEEsigQEKSR----SEEALEKAQARVRELENHLASQKEALENS---VAQE 780
Cdd:PRK10929 103 STDA-----LEQ-EILQVSSQLLEKSRQAQQE---QDRAReisdSLSQLPQQQTEARRQLNEIERRLQTLGTPntpLAQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 781 KRKMREMlEAERRKAQDLENQLTQqkeISENNTYEKLKMRDTLEKEKR-----KIQDLENRLTKQ-KEEIE--------L 846
Cdd:PRK10929 174 QLTALQA-ESAALKALVDELELAQ---LSANNRQELARLRSELAKKRSqqldaYLQALRNQLNSQrQREAEralestelL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 847 KEQKENV---------LNNKLKDALvmVEDAQQMKTTESQR--AETLALKLKETLAEL 893
Cdd:PRK10929 250 AEQSGDLpksivaqfkINRELSQAL--NQQAQRMDLIASQQrqAASQTLQVRQALNTL 305
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
701-924 |
3.35e-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: 47.45 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 701 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQ---------LTEEKAALEESiGQEKSRSEEALEKAQARVRELEN---HLAS 768
Cdd:pfam09787 4 SAKQELADYKQKAARILQSKEKLIASLKEgsgvegldsSTALTLELEEL-RQERDLLREEIQKLRGQIQQLRTelqELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 769 QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLekeKRKIQDLENRLTKQKEEIELKE 848
Cdd:pfam09787 83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 849 QkenvlnnklkdalvmvEDAQQMKTTESQRAETLALKLKETLAE-LETTKTKMILTDDRLklqQQSMKALQDERESQ 924
Cdd:pfam09787 160 Q----------------SSSSQSELENRLHQLTETLIQKQTMLEaLSTEKNSLVLQLERM---EQQIKELQGEGSNG 217
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
76-123 |
3.51e-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: 3.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1039768044 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 |
3.56e-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: 3.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039768044 76 HHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDILRFG 123
Cdd:cd22679 52 NHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDIVQFG 102
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
689-796 |
3.96e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 689 QAQMNASRETQKSLRQehLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlas 768
Cdd:COG2268 223 AEEAELEQEREIETAR--IAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQ----- 295
|
90 100
....*....|....*....|....*...
gi 1039768044 769 QKEAlENSVAQEKRKMREMLEAERRKAQ 796
Cdd:COG2268 296 EKEA-EREEAELEADVRKPAEAEKQAAE 322
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
67-131 |
4.15e-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: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 67 DAESADI--DNH-----HALIEF----NEAEGTFVLQ------DFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGMT 128
Cdd:cd22676 28 DRRVADIplDHPscskqHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLSTRE 107
|
...
gi 1039768044 129 YEL 131
Cdd:cd22676 108 YVL 110
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
707-834 |
5.43e-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: 46.90 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 707 LAEKEKLAEKLEQEE----KLKAKIQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHLASQ 769
Cdd:pfam02841 154 LEERDKLEAKYNQVPrkgvKAEEVLQEFLQSKEAVEEAILQtdqaltakekaieAERAKAEAAEAEQELLREKQKEEEQM 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 770 KEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLE 834
Cdd:pfam02841 234 MEAQERSYQEHVKQLIEKMEAEREQLLA-EQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
705-955 |
5.47e-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: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 705 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG-QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRk 783
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 784 mremLEAERRKAQDLENQLTQQkeISENNTyeklkmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDA-L 862
Cdd:COG4913 314 ----LEARLDALREELDELEAQ--IRGNGG--------------DRLEQLEREIERLERELEERERRRARLEALLAALgL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 863 VMVEDAQQMKTTESQRAETLAlKLKETLAELETTKtkmiltdDRLKLQQQsmkALQDERESQkhgfEEEISEYKEQIKQH 942
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE-ALEEELEALEEAL-------AEAEAALR---DLRRELREL----EAEIASLERRKSNI 438
|
250
....*....|...
gi 1039768044 943 SQTIVSLEERLCQ 955
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
411-978 |
5.67e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 411 KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEK 490
Cdd:PRK01156 136 GQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 491 LQEDSRRKLLQLQEMGNRENLIKINLERAVGQLE--NFRNQVIKATFGKTKPFRDKPITDQQLIEKIIQVTEDNLSFQQR 568
Cdd:PRK01156 216 TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 569 K----WTLQRETHLHPKQEETMHS-VEKLRVLLDKCQACMRDSCSSIDLKKEVELLQH--LPLSPLVSGLQKTVVNILRV 641
Cdd:PRK01156 296 YindyFKYKNDIENKKQILSNIDAeINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqiLELEGYEMDYNSYLKSIESL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 642 SLsWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQeHLAEKEKLAEKLEQEE 721
Cdd:PRK01156 376 KK-KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE-NLDELSRNMEMLNGQS 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 722 KLKAKIQQLTEEKAA-LEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLEN 800
Cdd:PRK01156 454 VCPVCGTTLGEEKSNhIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK----SINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 801 QLTQQKeISENntyeklkmrdTLEKEKRKIQDLENRLTKQKEEIeLKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 880
Cdd:PRK01156 530 DLEDIK-IKIN----------ELKDKHDKYEEIKNRYKSLKLED-LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLN 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 881 TLALKLKETLAELETTKT----KMILTDDRLKLQQQSMKALQDEReSQKHGFEEEISEYKEQIKQHSQTIVSLEE---RL 953
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENK-ILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRI 676
|
570 580
....*....|....*....|....*
gi 1039768044 954 CQVTQYYQKIEGEITTLKNNDTGPK 978
Cdd:PRK01156 677 NDIEDNLKKSRKALDDAKANRARLE 701
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
76-129 |
5.93e-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: 5.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 76 HHALI-----EFNEAEG----TFVLQDFnSRNGTFVNECHIQNVA-VKLIPGDILRFGSAGMTY 129
Cdd:cd22667 42 KHATLtvlhpEANLSDPdtrpELTLKDL-SKYGTFVNGEKLKGGSeVTLKDGDVITFGVLGSKF 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
710-938 |
6.53e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 710 KEKLAEKLEQEEKLKAKIQQLTEEKAALEesigqeksRSEEALEKAQARVRELENHLASQKEalensvaqekrkmremLE 789
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE--------AELDALQERREALQRLAEYSWDEID----------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 790 AERRKAQDLENQLTQqkeISENNtyeklkmrDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQ 869
Cdd:COG4913 665 SAEREIAELEAELER---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 870 -QMKTTESQRAETLALKLKETLAELETTKtkmILTDDRLKLQQQsMKALQDERESQKHGFEEEISEYKEQ 938
Cdd:COG4913 734 dRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-471 |
6.82e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 286 LQAEVADLSQRLSETAAVAAA---------RQSNRCDpKLQGVDEGD-DLR--QKEIESMKSQINALQKGYSQV--LSQT 351
Cdd:COG4913 615 LEAELAELEEELAEAEERLEAleaeldalqERREALQ-RLAEYSWDEiDVAsaEREIAELEAELERLDASSDDLaaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 352 LAERNTEIESLKNEGENLKRDHAitsgmvtSLQKDMSARNEQVQQLQEEVNrlRIENREKEYQLEALSSRCsvmkEELRK 431
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERF----AAALG 760
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039768044 432 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNY 471
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFNREW 800
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
694-880 |
6.92e-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: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 694 ASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLASQKEA 772
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 773 LENSVAQEKRKMR---------------------EMLEAERRKAQDLENQLTQQKEISENntyEKLKMRDTLEKEKRKIQ 831
Cdd:COG3883 88 LGERARALYRSGGsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039768044 832 DLEnrltKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 880
Cdd:COG3883 165 ELE----AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
711-912 |
8.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 711 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlaSQKEALENSVAQEKRKMREMLEA 790
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 791 ERRKAQDLENQLTQQKEISENNTYEKLKMR-DTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKDALVMVEDA 868
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERlEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039768044 869 QQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 912
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
45-133 |
8.90e-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: 43.58 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 45 GPSTSIINQEHAPPPGLCTCRSDAESADIDNHHALIEFNEAEGTFV--LQDFNSRNGTFVNECHI-QNVAVKLIPGDILR 121
Cdd:cd22681 38 SPSCYLIGREKGESTEIVVADIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDVIT 117
|
90
....*....|..
gi 1039768044 122 FgSAGMTYELVI 133
Cdd:cd22681 118 F-SKSNDYELVF 128
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
679-853 |
8.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 679 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG------QEKSRSE--- 749
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralYRSGGSVsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 750 ----------------EALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEisennt 813
Cdd:COG3883 106 dvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEAQQA------ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039768044 814 yEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENV 853
Cdd:COG3883 179 -EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
64-131 |
9.05e-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: 42.99 E-value: 9.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 64 CRSDAESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGMTYEL 131
Cdd:cd22725 30 CELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
676-868 |
9.09e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 676 EHYKKimsQSQDLQAQMNASRETQKSLRQEH----LAEKEKLAEkleQEEKLKAKIQQLTEEKAALEESIGQEKSRSEE- 750
Cdd:PRK10929 211 ELAKK---RSQQLDAYLQALRNQLNSQRQREaeraLESTELLAE---QSGDLPKSIVAQFKINRELSQALNQQAQRMDLi 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 751 ALEKAQA-----RVRELENHLASQK----------EALENSVAQ--EKRKM----REM--LEAERRKAQDLENQLTQQKE 807
Cdd:PRK10929 285 ASQQRQAasqtlQVRQALNTLREQSqwlgvsnalgEALRAQVARlpEMPKPqqldTEMaqLRVQRLRYEDLLNKQPQLRQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 808 ISENNTYeklkmrdTLEKEKRKIqdLENRLTKQKEEIE----------LKEQKENVLNNKLKDALVMVEDA 868
Cdd:PRK10929 365 IRQADGQ-------PLTAEQNRI--LDAQLRTQRELLNsllsggdtliLELTKLKVANSQLEDALKEVNEA 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
297-509 |
1.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 297 LSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRD 372
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 373 HAITSGMVTSLQKDMSARNE-----QVQQLQEEVNRLRIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELK 447
Cdd:COG3883 85 REELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039768044 448 LCRSQMQDMEKEVRKLREELkknymgQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRE 509
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
703-1197 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 703 RQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLA--------------- 767
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqerinrarka 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 768 -------------SQKEALENSVAQEKRKMREML----------EAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 824
Cdd:TIGR00618 293 aplaahikavtqiEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 825 KEKrkiqDLENRLTKQKEEIELKEQKENVLNNKLKdalvmVEDAQQmKTTESQRAETLALKLKETLAELETTKTKMILTD 904
Cdd:TIGR00618 373 QQH----TLTQHIHTLQQQKTTLTQKLQSLCKELD-----ILQREQ-ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 905 DRLKLQQQSMKALQDERESQKhgFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQD 984
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 985 LTAGPpldsgdkeiacdhLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGEL 1064
Cdd:TIGR00618 521 DNPGP-------------LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ-SFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1065 SMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLsQKCDISLQIEPAHPDSFSS--FQEEQSFSDL 1142
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL-QQCSQELALKLTALHALQLtlTQERVREHAL 665
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 1143 GVKCKGSRHEETIQRQRKAL-SELRTRVRELEKANSCNHKDH-VNESFLELRTLRME 1197
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLReLETHIEEYDREFNE 722
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
77-124 |
1.16e-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: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039768044 77 HALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILRFGS 124
Cdd:cd22686 51 HAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELKIGE 103
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
686-867 |
1.24e-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: 45.30 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 686 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRsEEALEKAQARV---REL 762
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 763 ENhLASQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQKEISEnntyeklKMRDTLEKEKRKIQDLENRLTK 839
Cdd:COG1579 92 EA-LQKEIESLKRRISDLEDEILELmerIEELEEELAELEAELAELEAELE-------EKKAELDEELAELEAELEELEA 163
|
170 180 190
....*....|....*....|....*....|....
gi 1039768044 840 QKEEI------ELKEQKENVLNNKLKDALVMVED 867
Cdd:COG1579 164 EREELaakippELLALYERIRKRKNGLAVVPVEG 197
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
324-961 |
1.37e-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: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 324 DLRQKEIESMKSQINALQ---KGY--SQVLSQTLAERNTEIESLKNEGENLKRDHAITSgmVTSLQKDMSARNEQVQQLQ 398
Cdd:pfam12128 244 TKLQQEFNTLESAELRLShlhFGYksDETLIASRQEERQETSAELNQLLRTLDDQWKEK--RDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 399 EEVNRlrIENREKEYQLEALSSRcsvmKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 478
Cdd:pfam12128 322 SELEA--LEDQHGAFLDADIETA----AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 479 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLEnfrnqvIKATFGKTKPFRDKPITDQQLIEKIiQV 558
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYR------LKSRLGELKLRLNQATATPELLLQL-EN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 559 TEDNLSFQQRKWTLQRETHLHPKQEETmhsveKLRVLLDKCQACMRD-SCSSIDLKKEVELLQHLpLSPLVSGLQ---KT 634
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELR-----QARKRRDQASEALRQaSRRLEERQSALDELELQ-LFPQAGTLLhflRK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 635 VVNILRVSLSWLEETEQLL-GDLDIELSDSDKGFSLCLIYLLEHYKKImsqsqdlqaqmnasretqkslrqehlaekeKL 713
Cdd:pfam12128 543 EAPDWEQSIGKVISPELLHrTDLDPEVWDGSVGGELNLYGVKLDLKRI------------------------------DV 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 714 AEKLEQEEKLKAKIQQLteekaaleesigqeksrsEEALEKAQARVRELENHLASQKEALENSVAqekrkmremleAERR 793
Cdd:pfam12128 593 PEWAASEEELRERLDKA------------------EEALQSAREKQAAAEEQLVQANGELEKASR-----------EETF 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 794 KAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK------EQKENVLNNKLkdalvmvED 867
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawleEQKEQKREART-------EK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 868 AQQMKTTESQRAETLALkLKETLAELETTKtkmiltDDRLKLQQQSMKalqdeRESQKHGFEEE-ISEYKEQIKQHSQTI 946
Cdd:pfam12128 717 QAYWQVVEGALDAQLAL-LKAAIAARRSGA------KAELKALETWYK-----RDLASLGVDPDvIAKLKREIRTLERKI 784
|
650
....*....|....*
gi 1039768044 947 VSLEERLCQVTQYYQ 961
Cdd:pfam12128 785 ERIAVRRQEVLRYFD 799
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
705-850 |
1.39e-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: 44.92 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 705 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR---SEEALEKAQARVRELENHLASQKEALENSVAQ-- 779
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARleaAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 780 EKRKMREM------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 850
Cdd:COG1579 84 NVRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
679-941 |
1.69e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 679 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 758
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 759 VrelenhlASQKEALENSVAQEKrkmremlEAERRKAQDLENQLTQQKEISENntyeklkmrdtlEKEKRKIQDLENRLT 838
Cdd:TIGR02794 123 E-------AKAKQAAEAKAKAEA-------EAERKAKEEAAKQAEEEAKAKAA------------AEAKKKAEEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 839 KQKEEIELKEQKENVLNNKLKdalvmvedAQQMKTTESQRAETLALKLKETLAELETTKTKMILT-DDRLKLQQQSMKAL 917
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAEEAKAK--------AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAElGDIFGLASGSNAEK 248
|
250 260
....*....|....*....|....
gi 1039768044 918 QDERESQKHGfeEEISEYKEQIKQ 941
Cdd:TIGR02794 249 QGGARGAAAG--SEVDKYAAIIQQ 270
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
696-846 |
1.89e-04 |
|
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: 45.71 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 696 RETQKSLRQEHLAEKEKLAEKLEQE-----EKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQK 770
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEE----EERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 771 EALENSVAQEKrkmREMLEAERRKAQDLENQLT-QQKEISENNTYEKLK-MRDTLEKEKRKIQDLENRLTKQKEEIEL 846
Cdd:pfam15709 433 QELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
696-938 |
2.17e-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: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 696 RETQKSLRQEHLAEKEKLAEKL-EQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaQARVRELENHLASQKEALE 774
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENkDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECS 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 775 NSVAQEKrKMREMLEAERRKA------QDLENQLTQQKEISENNTYEKLKMRDTL---EKEK----RKIQDLENRLTKQ- 840
Cdd:pfam10174 535 KLENQLK-KAHNAEEAVRTNPeindriRLLEQEVARYKEESGKAQAEVERLLGILrevENEKndkdKKIAELESLTLRQm 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 841 KEEIELKEQKENVLNNKLKDALVMVEDAqqMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK----- 915
Cdd:pfam10174 614 KEQNKKVANIKHGQQEMKKKGAQLLEEA--RRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAekdgh 691
|
250 260
....*....|....*....|....*
gi 1039768044 916 --ALQDERESQKhgfeEEISEYKEQ 938
Cdd:pfam10174 692 ltNLRAERRKQL----EEILEMKQE 712
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
686-958 |
2.28e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 686 QDLQAQMNASREtqkslrQEHLAEKEKLAEK-LEQEEKLKAKIQQLTEEKAALEESIGQeksrSEEALEKAQARVRELEN 764
Cdd:PRK11281 39 ADVQAQLDALNK------QKLLEAEDKLVQQdLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 765 HLASQ-KEALEN-SVAQEKRKMREMLEAERRKAQDLE-------NQLTQ----QKEISENNTyeklkmrdtlekekrKIQ 831
Cdd:PRK11281 109 DNDEEtRETLSTlSLRQLESRLAQTLDQLQNAQNDLAeynsqlvSLQTQperaQAALYANSQ---------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 832 DLENRLTKQK-EEIELKEQKENVLNNKLkdALVMVEDAQQMKTTE----------SQRAEtlaLKLKETLAELETTKTKM 900
Cdd:PRK11281 174 QIRNLLKGGKvGGKALRPSQRVLLQAEQ--ALLNAQNDLQRKSLEgntqlqdllqKQRDY---LTARIQRLEHQLQLLQE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 901 ILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQ 958
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQ 306
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
721-845 |
2.50e-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: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 721 EKLKAKIQQLTEEKAALEESigqEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKMREMLEAERRKAQDL 798
Cdd:COG0542 414 DELERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARWEAekELIEEIQELKEELEQRYGKIPEL 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039768044 799 ENQLTQ-QKEISENNTYEKL--------------------KMrdtLEKEKRKIQDLENRLTK----QKEEIE 845
Cdd:COG0542 491 EKELAElEEELAELAPLLREevteediaevvsrwtgipvgKL---LEGEREKLLNLEEELHErvigQDEAVE 559
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
73-123 |
2.61e-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: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768044 73 IDNHHALIEFN----EAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 123
Cdd:cd22677 41 ISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
744-973 |
3.07e-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: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 744 EKSRSEEALEKAQARVRELENHlasqKEALENsvAQEKRKMREMLEAERRKAQDLENQLTQQkeisenntyEKLKMRDTL 823
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA----HEALED--AREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 824 EKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAETLALKLKETLAELETTKTKMIL 902
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 903 TDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNN 973
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
679-941 |
3.50e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 679 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 758
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 759 VRELENHLASQKEalENSVAQEKRKMREMLEAERRKAQ------DLENQLTQQ-KEISenntyEKLKMRDTLEKEKRKIQ 831
Cdd:COG1340 91 REELDELRKELAE--LNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELVEKiKELE-----KELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 832 DLENRLTKQKEEI-ELKEQKENVLN--NKLKDALV-MVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRL 907
Cdd:COG1340 164 ELRAELKELRKEAeEIHKKIKELAEeaQELHEEMIeLYKEADELR----KEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1039768044 908 -KLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 941
Cdd:COG1340 240 rELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
77-124 |
3.70e-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: 3.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1039768044 77 HALIEFNEAEGTFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 124
Cdd:cd22678 46 HARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
768-990 |
4.35e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 768 SQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ-QKEIsenntyeklkmrDTLEKEkrkIQDLENRLTKQKEEIE- 845
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEAlQAEI------------DKLQAE---IAEAEAEIEERREELGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 846 -LKEQKENVLNNKLKDALVMVED-------AQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKAL 917
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESfsdfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039768044 918 QDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 990
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
705-887 |
4.45e-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: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 705 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVreLENHLASQKEALE---NSVAQEK 781
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAI----SGSQSQLESTDQNA--LETNGQAQRDAILeesRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 782 RKMREMLEAERRKAQ-------------------DLENQL--------TQQKEISENNTYEKLKMRDTLEKEK------- 827
Cdd:NF012221 1623 TTLAQGLDALDSQATyagesgdqwrnpfagglldRVQEQLddakkisgKQLADAKQRHVDNQQKVKDAVAKSEagvaqge 1702
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 828 RKIQDLENRLTKQKEEIELKEQ----KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK 887
Cdd:NF012221 1703 QNQANAEQDIDDAKADAEKRKDdalaKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
357-846 |
4.53e-04 |
|
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: 44.68 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 357 TEIESLKNEGENLKR----DHAITSGMVTSLQKDMSA-RNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRK 431
Cdd:COG5244 130 EEIVELRRENEELDKinlsLRERISSEEPELNKDGSKlSYDELKEFVEESRVQVYDMVELVSDISETLNRNGSIQRSSVR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 432 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK------KNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEM 505
Cdd:COG5244 210 ECERSNIHDVLFLVNGILDGVIDELNGELERLRRQLVslmsshGIEVEENSRLKATLEKFQSLELKVNTLQEELYQNKLL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 506 GNRENLIKINLERAVGQLENFRNQVIKAT-FGKTKPFRDKPITDQQL-IEKIIQVTEDNLSFQQRKWTLQRETHLHP--- 580
Cdd:COG5244 290 KKFYQIYEPFAQAALSSQLQYLAEVIESEnFGKLENIEIHIILKVLSsISYALHIYTIKNTPDHLETTLQCFVNIAPism 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 581 --KQEETMHSVEKLRVLLDKCQAcMRDSCSSIDLKK------EVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQL 652
Cdd:COG5244 370 wlSEFLQRKFSSKQETAFSICQF-LEDNKDVTLILKilhpilETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 653 LGDLDIELSDSDKG-FSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKakiQQLT 731
Cdd:COG5244 449 IGKEEISKQDNRLFlYPSCDITLSSILTILFSDKLEVFFQGIESLLENITIFPEQPSQQTSDSENIKENSLLS---DRLN 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 732 EEKAALEESIGQEKSRSEEALEKAQARVRELENhlASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISEN 811
Cdd:COG5244 526 EENIRLKEVLVQKENMLTEETKIKIIIGRDLER--KTLEENIKTLKVELNNKNNKLKEENFNLVNRLKNMELKLYQIKDN 603
|
490 500 510
....*....|....*....|....*....|....*
gi 1039768044 812 NTYEKLKMrdTLEKEKRKIQDLENRLTKQKEEIEL 846
Cdd:COG5244 604 NTLNKIYL--DLVSEIMELRETIRRQIKEQKRVSI 636
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
687-972 |
4.68e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 687 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESIGQE----------------KS 746
Cdd:PTZ00440 956 NLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILNKKIDDLikkqhddiielidkliKE 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 747 RSEEALEKAQARVRELEN--------HLASQKEALENSVAQEK-RKMREMLEAERRKAQDLENQLTQQKEISENNTY--- 814
Cdd:PTZ00440 1036 KGKEIEEKVDQYISLLEKmktklssfHFNIDIKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnad 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 815 -EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN----KLKDALVMVEDAQQMKTTESQRAETLALKLKET 889
Cdd:PTZ00440 1116 kEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESY 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 890 LAELETTKTKMILTD----DRLKLQQQSMKALQDERE----SQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 961
Cdd:PTZ00440 1196 KKDIDQVKKNMSKERndhlTTFEYNAYYDKATASYENieelTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENN 1275
|
330
....*....|.
gi 1039768044 962 KIEGEITTLKN 972
Cdd:PTZ00440 1276 KMENALHEIKN 1286
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
674-986 |
5.21e-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: 44.50 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 674 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALE 753
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 754 KAQARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK 827
Cdd:pfam07888 126 AHEARIRELEEDIKTltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 828 RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDalvmVEDAQQMKTTESQRAETLALKLKETL------------AELET 895
Cdd:pfam07888 206 TQVLQLQDTITTLTQKLTTAHRKEAENEALLEE----LRSLQERLNASERKVEGLGEELSSMAaqrdrtqaelhqARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 896 TKTKMILTDDRLKLQQQSMKALQdERESQKHGFEEEiseyKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDT 975
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQ-ERETLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNR 356
|
330
....*....|.
gi 1039768044 976 GPKEEASQDLT 986
Cdd:pfam07888 357 VQLSESRRELQ 367
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
704-834 |
5.59e-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: 43.72 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 704 QEHLAEKEKLAEKLEQEEK--LKAK--IQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHL 766
Cdd:cd16269 145 QLYLEDREKLVEKYRQVPRkgVKAEevLQEFLQSKEAEAEAILQadqaltekekeieAERAKAEAAEQERKLLEEQQREL 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 767 ASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEiSENNTYEKLKMRDTLEKEKRKIQDLE 834
Cdd:cd16269 225 EQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKL-KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
64-103 |
6.33e-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: 6.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1039768044 64 CRSDAESADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVN 103
Cdd:smart00240 10 CDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
743-901 |
7.00e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 743 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEIsenntyeklkmrdt 822
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQ-------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039768044 823 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttesqrAETLALKLKETLAELETTKTKMI 901
Cdd:PRK12705 93 LDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTP--------EQARKLLLKLLDAELEEEKAQRV 163
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
327-975 |
9.57e-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: 43.89 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 327 QKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSAR-NEQVQQLQEEVNRLR 405
Cdd:TIGR01612 798 QINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKiDSEHEQFAELTNKIK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 406 IENREK-----EYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEK---EVRKLREELKKNYmgqnii 477
Cdd:TIGR01612 878 AEISDDklndyEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKfhnKQNILKEILNKNI------ 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 478 sKTLREKNKVEEKLQEDSRRKLLQlqemgNRENLIKINLERAVGQLENFRNQVI------KATFGKTK------PFRDKP 545
Cdd:TIGR01612 952 -DTIKESNLIEKSYKDKFDNTLID-----KINELDKAFKDASLNDYEAKNNELIkyfndlKANLGKNKenmlyhQFDEKE 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 546 ITDQQLIEKIIQVTEDNLSFQqrkwtLQRETHLHPKQEETMHSVEKLRVLLDKcQACMRDSCSSIDLKKEVELLQHLPLS 625
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIE-----IAIHTSIYNIIDEIEKEIGKNIELLNK-EILEEAEINITNFNEIKEKLKHYNFD 1099
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 626 PLVSglqktvvnilRVSLSWLEETEQLLGDLDIELSDSDKGFSlcliYLLEHYKKIMSQSQDLQAQMNASRE-TQKSLRQ 704
Cdd:TIGR01612 1100 DFGK----------EENIKYADEINKIKDDIKNLDQKIDHHIK----ALEEIKKKSENYIDEIKAQINDLEDvADKAISN 1165
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 705 EHLAEKEKLAEKL-----------EQEEKLKAKIQQLTEEKAALE------------------ESIGQEKSRSEEALEKA 755
Cdd:TIGR01612 1166 DDPEEIEKKIENIvtkidkkkniyDEIKKLLNEIAEIEKDKTSLEevkginlsygknlgklflEKIDEEKKKSEHMIKAM 1245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 756 QARVRELENhLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQK-------------EISENNtYEKLKMRD- 821
Cdd:TIGR01612 1246 EAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKhdenisdirekslKIIEDF-SEESDINDi 1323
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 822 --TLEKEKRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAeLE 894
Cdd:TIGR01612 1324 kkELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LE 1402
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 895 TTKTKMILTDDRLKLQQqsmkALQDERESQKHGFEEE--ISEYKEQIKQHSQTIVSL---EERLCQVTQYYQKIEgeitt 969
Cdd:TIGR01612 1403 ECKSKIESTLDDKDIDE----CIKKIKELKNHILSEEsnIDTYFKNADENNENVLLLfknIEMADNKSQHILKIK----- 1473
|
....*.
gi 1039768044 970 lKNNDT 975
Cdd:TIGR01612 1474 -KDNAT 1478
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
687-953 |
1.30e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 687 DLQAQMNASRETQKSLRQEHLAEKEKLA---------EKLEQ-EEKLKAKIQQLTEEKAALEESIGQeKSRSEEALEKAQ 756
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqEKIERyQADLEELEERLEEQNEVVEEADEQ-QEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 757 ARVRELENHLASQKEALEnsvAQEKR--------------------------KMREMLEAERRKAQDLENQLTQ--QK-- 806
Cdd:PRK04863 390 EEVDELKSQLADYQQALD---VQQTRaiqyqqavqalerakqlcglpdltadNAEDWLEEFQAKEQEATEELLSleQKls 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 807 ---------------------EISENN----------TYEKLKMRD-TLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 854
Cdd:PRK04863 467 vaqaahsqfeqayqlvrkiagEVSRSEawdvarellrRLREQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 855 NNKLKDALV----------MVEDAQQMKTTESQRAETLALKLKET---LAELETTKTKMILTDDRL-KLQQQS------- 913
Cdd:PRK04863 547 GKNLDDEDEleqlqeeleaRLESLSESVSEARERRMALRQQLEQLqarIQRLAARAPAWLAAQDALaRLREQSgeefeds 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039768044 914 ------MKALQD-ERESQ--KHGFEEEISEYKEQIKQHSQTIVSLEERL 953
Cdd:PRK04863 627 qdvteyMQQLLErERELTveRDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
781-1173 |
1.41e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 781 KRKMREMLEAERRKAQDLENQLTQQKEISENNTY------------------EKLKMRDTLEKEKRKIQDLENRLTKQKE 842
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFylrqsvidlqtklqemqmERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 843 EIE-LKEQKENVLNnklkDALVMVEDAQQMKTTEsqraETLALKLKETLAELETTKTKMILTDDrlKLQQQSMKALQDER 921
Cdd:pfam15921 153 ELEaAKCLKEDMLE----DSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEHD--SMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 922 ESQKHGFEEEISEYK----------EQIKQHSQTIVSLeerlcQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL 991
Cdd:pfam15921 223 SKILRELDTEISYLKgrifpvedqlEALKSESQNKIEL-----LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 992 DSgdkeiacdhlidDLLMAQKEILSQQEIIMKLRTDLgeaHSRMSDLRGELSEKQKM------ELERQVALVRQQSGELS 1065
Cdd:pfam15921 298 QS------------QLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAKRMyedkieELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1066 MLKAKVAQTTGLMEkkDRELKVLREALRASQEKPrphLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDL--- 1142
Cdd:pfam15921 363 TERDQFSQESGNLD--DQLQKLLADLHKREKELS---LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALlka 437
|
410 420 430
....*....|....*....|....*....|....
gi 1039768044 1143 -GVKCKGS--RHEETIQRQRKALSELRTRVRELE 1173
Cdd:pfam15921 438 mKSECQGQmeRQMAAIQGKNESLEKVSSLTAQLE 471
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
696-932 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 696 RETQKSLRQEHLAEKEKLAEKLEQEEK-LKAKIQQLTEEKAALEESIGQEK---SRSEEALEKAQARVRELENHLASQKE 771
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKeLEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 772 ALE------NSVAQEKRKMREMLeaerrkaQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE 845
Cdd:pfam01576 83 RLEeeeersQQLQNEKKKMQQHI-------QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 846 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK---ETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 922
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250
....*....|
gi 1039768044 923 SQKHGFEEEI 932
Cdd:pfam01576 236 AQLAKKEEEL 245
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
380-1098 |
1.42e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 380 VTSLQKDMSARNEQVQQLQEEVNRLRIENRE--KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDME 457
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEElkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 458 KEVRKLREELKKNYMGQNIISKTLREKNKV------EEKLQE------DSRRKLLQLQEMGNRENLIKINLERAVGQLEN 525
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEeelkllAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 526 FRNQVIKATFGKTKPFRDKPITDQQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQACMRD 605
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 606 SCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKiMSQS 685
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ-LVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 686 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEK--------------SRSEEA 751
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKvaistavivevsatADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 752 LEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQ 831
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 832 DLENRLTKQKEEIELKEQKenvlnNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQ 911
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEK-----SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 912 QSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVS--------LEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 983
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrlkkeekEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 984 DLTAGP-PLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSG 1062
Cdd:pfam02463 798 AQEEELrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1039768044 1063 EL----SMLKAKVAQTTGLMEKKDRELKVLREALRASQEK 1098
Cdd:pfam02463 878 ELeeqkLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
704-840 |
1.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 704 QEHLAEKEKLAEKLE-----------QEEKLKAKIQQLTEEKAALEESIGQeksrseeaLEKAQARVRELENHLASQKEA 772
Cdd:COG4913 667 EREIAELEAELERLDassddlaaleeQLEELEAELEELEEELDELKGEIGR--------LEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 773 LENSVAQEkrkMREMLEaERRKAQDLENqltQQKEISENntyeklkMRDTLEKEKRKIQDLENRLTKQ 840
Cdd:COG4913 739 AEDLARLE---LRALLE-ERFAAALGDA---VERELREN-------LEERIDALRARLNRAEEELERA 792
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
709-832 |
1.69e-03 |
|
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: 42.12 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 709 EKEKLAEKLEQEEK-----LKAKIQQLTEEKAALEESIGQEKSRseealekaqarvreLENHLASQKEALENSVAQEKRK 783
Cdd:pfam09755 93 EKETLAMNYEQEEEfltndLSRKLTQLRQEKVELEQTLEQEQEY--------------QVNKLMRKIEKLEAETLNKQTN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1039768044 784 mremLEAERRKAQDLENQLTQQKEISENNTYEKLkmrDTLEKEKRKIQD 832
Cdd:pfam09755 159 ----LEQLRREKVELENTLEQEQEALVNRLWKRM---DKLEAEKRLLQE 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
815-946 |
1.72e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 815 EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENvlnnKLKDALVMVEDAQQMK------TTESQRAETLALKLKE 888
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 889 TLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 946
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
709-963 |
1.88e-03 |
|
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: 42.11 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 709 EKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQ-EKSRSE--EALEKAQARVRELENhlasQKEAleNSVAQEKRKM 784
Cdd:pfam15905 91 EQDKRLQALEEElEKVEAKLNAAVREKTSLSASVASlEKQLLEltRVNELLKAKFSEDGT----QKKM--SSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 785 REMLEAERRKAQDLENQLTQQKEISENNtyeklkmrdtLEKEKRKIQDLENRL-TKQKEEIELKEQKENVLNNKLKdaLV 863
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKN----------LEHSKGKVAQLEEKLvSTEKEKIEEKSETEKLLEYITE--LS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 864 MVEDAQQMKTTESQRAETLalkLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKhgfEEEISEYKEQIKQHS 943
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEEL---LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---EELLREYEEKEQTLN 306
|
250 260
....*....|....*....|
gi 1039768044 944 QTIVSLEERLCQVTQYYQKI 963
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
261-528 |
1.89e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 261 LLGREVNRLSDFEMESKYKDALIMNLQAEVADlSQRLSETAAVAAARQSNRCDPKLQGV----DEGDDLR--QKEIESMK 334
Cdd:pfam15921 476 MLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAEITKLRSRVDLKLQELqhlkNEGDHLRnvQTECEALK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 335 SQinalqkgysqvlsqtLAERNTEIESLKNEGENLKR---DHAITSGmvtSLQKDMSARNEQVQQLQEEVNRLRIENREK 411
Cdd:pfam15921 555 LQ---------------MAEKDKVIEILRQQIENMTQlvgQHGRTAG---AMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 412 EYQLEALSSRCSVMK-----------EELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVrklrEELKKNYmgqniiskt 480
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY----EVLKRNF--------- 683
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039768044 481 lreKNKVEeklqedsrrkllqlqEMGNRENLIKINLERAVGQLENFRN 528
Cdd:pfam15921 684 ---RNKSE---------------EMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-507 |
2.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 286 LQAEVADLSQRLSETAAVAAARQsnrcdpklqgvdegdDLRQ-----KEIESMKSQINALQKGYSQvLSQTLAERNTEIE 360
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDKLVQQ---------------DLEQtlallDKIDRQKEETEQLKQQLAQ-APAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 361 SLKNEG-ENLKRDHAITSgmVTSLQKDMSARNEQVQQLQEEVNrlrienrekEY--QLEALSSrcsvmkeelRKEEAQKD 437
Cdd:PRK11281 105 ALKDDNdEETRETLSTLS--LRQLESRLAQTLDQLQNAQNDLA---------EYnsQLVSLQT---------QPERAQAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 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]; |
719-925 |
2.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 719 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQA-RVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQD 797
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 798 LENQLTQQ--------KEISENNTYEKLkmRDTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKdalvmvEDA 868
Cdd:COG3206 241 RLAALRAQlgsgpdalPELLQSPVIQQL--RAQLAELEAELAELSARYTPNHPDViALRAQIAALRAQLQQ------EAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 869 QQMKTTESQRaETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQK 925
Cdd:COG3206 313 RILASLEAEL-EALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVAR 364
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
700-852 |
2.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 700 KSLRQEHLAEKEKLAEKLEQEEKLKA------KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEAL 773
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAeaikkeALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 774 EnsvaqekrKMREMLEAERRKAQDLENQLTQQKEisennTYEKL--KMRDTLEK-------EKRKI--QDLENRLTKQK- 841
Cdd:PRK12704 106 E--------KREEELEKKEKELEQKQQELEKKEE-----ELEELieEQLQELERisgltaeEAKEIllEKVEEEARHEAa 172
|
170
....*....|....
gi 1039768044 842 ---EEIElKEQKEN 852
Cdd:PRK12704 173 vliKEIE-EEAKEE 185
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
675-880 |
2.47e-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: 42.42 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 675 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEK 754
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 755 -------AQARVRELENHLASQKEA-------LENSVAQEKRKMREmleaERRKAQDLENQLtqqkEISENNTYEKLKMR 820
Cdd:pfam17380 465 lrqqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIE----EERKRKLLEKEM----EERQKAIYEEERRR 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 821 DTlEKEKRKIQDLENRLTKQKEEIELKEQKenvlnNKLKDALVMVEDAQQMKTTESQRAE 880
Cdd:pfam17380 537 EA-EEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREMMRQIVESEKARAE 590
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
73-131 |
2.49e-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: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039768044 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 |
2.55e-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: 2.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039768044 62 CTCRSDaeSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYE 130
Cdd:cd22673 31 CDIRIQ--LPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFRFE 95
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
673-881 |
2.66e-03 |
|
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: 41.24 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 673 YLLEHYKKIMSQSQDLQAQMNASretqKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAL 752
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKEL----SSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 753 EKA--------QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQL-TQQKEISENNTYEKLKMRDTL 823
Cdd:pfam06008 103 EKVatlgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIqTWFQSPQEENKALANALRDSL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039768044 824 EKEKRKIQDLENRLtkqkEEIELKEQKENVLNNKLKDALVMVEdaQQMKTTESQRAET 881
Cdd:pfam06008 183 AEYEAKLSDLRELL----REAAAKTRDANRLNLANQANLREFQ--RKKEEVSEQKNQL 234
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
647-955 |
2.95e-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: 42.08 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 647 EETEQLLGDLDIELSDSDKgfslCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK 726
Cdd:pfam01576 71 QELEEILHELESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 727 IQQLTEEKAALEESIGQEKSRSEEALEKAQArVRELENHLASQKEALENSVAQEKRKMREMLEAERR---KAQDLENQLT 803
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 804 -QQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTtesqRAETL 882
Cdd:pfam01576 226 eLQAQIAE--------LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN----KAEKQ 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 883 ALKLKEtlaELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ----HSQTIVSLEERLCQ 955
Cdd:pfam01576 294 RRDLGE---ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkHTQALEELTEQLEQ 367
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
628-917 |
3.13e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 628 VSGLQKTVvnILRVSLSWLEETEQLLGDLDIELSDSD--KGFSLCLIYLLEHYKKIMSQS--QDLQAQMNASRETQKSLR 703
Cdd:COG5022 861 FSLLKKET--IYLQSAQRVELAERQLQELKIDVKSISslKLVNLELESEIIELKKSLSSDliENLEFKTELIARLKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 704 QEHLAE--------KEKLAEKLEQEEKLKakiqQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLaSQKEALEN 775
Cdd:COG5022 939 NIDLEEgpsieyvkLPELNKLHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS-KQYGALQE 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 776 SVAQEKRKMREMLEAerrkaqdlenqltqqkeiseNNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEeiELKEQKENVLN 855
Cdd:COG5022 1014 STKQLKELPVEVAEL--------------------QSASKIISSESTELSILKPLQKLKGLLLLENN--QLQARYKALKL 1071
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 856 NKlKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDD---RLKLQQQSMKAL 917
Cdd:COG5022 1072 RR-ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAqmiKLNLLQEISKFL 1135
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
679-797 |
3.23e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 679 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKlAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 758
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK 161
|
90 100 110
....*....|....*....|....*....|....*....
gi 1039768044 759 VRELENHLASQKEALENSVAQEKRKMREmlEAERRKAQD 797
Cdd:PRK09510 162 KAAAEAKKKAEAEAAKKAAAEAKKKAEA--EAAAKAAAE 198
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
765-972 |
3.31e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 765 HLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 844
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKL--NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 845 -ELKEQKENVLNNK-----LKDALVMVEDAQQMKTT--------ESQRAETLALKLKETLAELETTKTKM--ILTDDRLK 908
Cdd:PRK05771 110 sELENEIKELEQEIerlepWGNFDLDLSLLLGFKYVsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVyvVVVVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039768044 909 LQQQsmkalqdERESQKHGFEE-EISEykeqIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 972
Cdd:PRK05771 190 SDEV-------EEELKKLGFERlELEE----EGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
701-971 |
3.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 701 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 771
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 772 ALENsvAQEkrkMREMLEAERRKAQ----DLENQLT--------QQKEISENN----TYEKLK------------MRDTL 823
Cdd:PRK04863 370 VVEE--ADE---QQEENEARAEAAEeevdELKSQLAdyqqaldvQQTRAIQYQqavqALERAKqlcglpdltadnAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 824 EKEKRKIQDLENRL--TKQKEEI--ELKEQKENVLN--NKLKDAlVMVEDAQQ-----MKTTESQRAETLALK-LKETLA 891
Cdd:PRK04863 445 EEFQAKEQEATEELlsLEQKLSVaqAAHSQFEQAYQlvRKIAGE-VSRSEAWDvarelLRRLREQRHLAEQLQqLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 892 ELEttktkmiltdDRLKLQQQSMKALQDerESQKHG--------FEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 963
Cdd:PRK04863 524 ELE----------QRLRQQQRAERLLAE--FCKRLGknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
....*...
gi 1039768044 964 EGEITTLK 971
Cdd:PRK04863 592 QARIQRLA 599
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
677-972 |
3.64e-03 |
|
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: 41.76 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 677 HYKKIMSQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQ 756
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEE-------LDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 757 ARVRELE-------------NHLASQK--EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisennTYEKLKMR- 820
Cdd:pfam06160 153 KQLAEIEeefsqfeeltesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE-----GYREMEEEg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 821 ---DTLEKEKRkIQDLENRLTKQKEEI---ELKEQKENVLN-----NKLKDALVMVEDAQQ-----MKTTESQRAETLAl 884
Cdd:pfam06160 228 yalEHLNVDKE-IQQLEEQLEENLALLenlELDEAEEALEEieeriDQLYDLLEKEVDAKKyveknLPEIEDYLEHAEE- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 885 KLKETLAELETTKTKMILTDDRLKLQQQsmkaLQDERESQKHGFEeeisEYKEQIKQHSQTIVSLEERLCQVTQYYQKIE 964
Cdd:pfam06160 306 QNKELKEELERVQQSYTLNENELERVRG----LEKQLEELEKRYD----EIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
....*...
gi 1039768044 965 GEITTLKN 972
Cdd:pfam06160 378 EEQEEFKE 385
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
59-123 |
3.94e-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: 3.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768044 59 PGLCTCRSDAESADIDNHHALIEFNeAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 123
Cdd:cd22663 29 LGVTYQLVSTCPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
683-922 |
4.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 683 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARV 759
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleaQIAELQSEIAEREEEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 760 RELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 839
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 840 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD 919
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
...
gi 1039768044 920 ERE 922
Cdd:COG4372 313 LED 315
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
671-938 |
4.41e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 671 LIYLLEHYKKIMSQSQDlQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR--- 747
Cdd:COG5185 287 LIKQFENTKEKIAEYTK-SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEien 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 748 --SEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLE-NQLTQQKEISENNTYEKLKMRDT 822
Cdd:COG5185 366 ivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtlKAADRQiEELQRQIEQATSSNEEVSKLLNE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 823 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKlkdalvmvEDAQQmkttESQRAETLALKLKETLAELETTKTKMI- 901
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEINRSVRSKK--------EDLNE----ELTQIESRVSTLKATLEKLRAKLERQLe 513
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039768044 902 LTDDRLKLQQQSMKALQDERE-SQKHGFEEEISEYKEQ 938
Cdd:COG5185 514 GVRSKLDQVAESLKDFMRARGyAHILALENLIPASELI 551
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
398-774 |
4.55e-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: 41.58 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 398 QEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAqKDRREAQEKELKLCRSQmqdmekevrkLREELKKNYMGQNII 477
Cdd:pfam13166 95 QEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEA-DFLDECWKKIKRKKNSA----------LSEALNGFKYEANFK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 478 SKTLREKNKVEEK----LQEDSRRKLLQLQEMGNRENLIKINLERAvgQLENFRNQVIKATfgktkpfrdKPITDQQLIE 553
Cdd:pfam13166 164 SRLLREIEKDNFNagvlLSDEDRKAALATVFSDNKPEIAPLTFNVI--DFDALEKAEILIQ---------KVIGKSSAIE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 554 KIIqvteDNLsfQQRKWtLQRETHLHP---------KQEETMHSVEKLRVLLDKC----QACMRDSCSSIDLKKEvELLQ 620
Cdd:pfam13166 233 ELI----KNP--DLADW-VEQGLELHKahldtcpfcGQPLPAERKAALEAHFDDEftefQNRLQKLIEKVESAIS-SLLA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 621 HLPLSPLVSGL-------QKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKgfslcliylLEHYKKIMSQSQDLQAQMN 693
Cdd:pfam13166 305 QLPAVSDLASLlsafeldVEDIESEAEVLNSQLDGLRRALEAKRKDPFKSIE---------LDSVDAKIESINDLVASIN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 694 ASRETQKSLRQEHLAEKEKLAEKLEQE--EKLKAKIQQLTEEKAALEESIG---QEKSRSEEALEKAQARVRELENHLAS 768
Cdd:pfam13166 376 ELIAKHNEITDNFEEEKNKAKKKLRLHlvEEFKSEIDEYKDKYAGLEKAINsleKEIKNLEAEIKKLREEIKELEAQLRD 455
|
....*.
gi 1039768044 769 QKEALE 774
Cdd:pfam13166 456 HKPGAD 461
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
327-437 |
4.67e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 327 QKEIESMKSQINALQKgYSQVLSQTLAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEqVQQLQEEVNRLRI 406
Cdd:COG2433 412 EEEIRRLEEQVERLEA-EVEELEAELEEKDERIERLERELSEARS----------EERREIRKDRE-ISRLDREIERLER 479
|
90 100 110
....*....|....*....|....*....|.
gi 1039768044 407 ENREKEYQLEALSSRCSVMKeELRKEEAQKD 437
Cdd:COG2433 480 ELEEERERIEELKRKLERLK-ELWKLEHSGE 509
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
76-129 |
4.84e-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: 4.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039768044 76 HHAliEFNEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTY 129
Cdd:cd22684 43 RHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
711-969 |
5.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 711 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaqEKRKMREMLEA 790
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 791 ERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQ 870
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 871 MKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLE 950
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|....*....
gi 1039768044 951 ERLCQVTQYYQKIEGEITT 969
Cdd:COG4372 273 TEEEELEIAALELEALEEA 291
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
677-1181 |
5.53e-03 |
|
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: 41.25 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 677 HYKKIMSQSqDLQAQMNASRETQKSLRQEHLAEKEKL---AEKLEQEEKLKAKIQQLTEEKAALEE-SIGQEKS--RSEE 750
Cdd:pfam05483 60 HYQEGLKDS-DFENSEGLSRLYSKLYKEAEKIKKWKVsieAELKQKENKLQENRKIIEAQRKAIQElQFENEKVslKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 751 ALEKAQARVRE--LENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ----KEISENNTYEKLKMRDTLE 824
Cdd:pfam05483 139 EIQENKDLIKEnnATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafEELRVQAENARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 825 KEKRKIQDLENrltKQKEEIELKEQKENVL-------NNKLKDALVMVEDAQQMKTTESQRAETLALKLKETL------- 890
Cdd:pfam05483 219 EDHEKIQHLEE---EYKKEINDKEKQVSLLliqitekENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIekkdhlt 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 891 AELETTKTKMILT-------DDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 963
Cdd:pfam05483 296 KELEDIKMSLQRSmstqkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 964 EG-----------------EITTLKNNDTGPKEEASQDLTAGPPLDSGDKEI--------ACDHLIDDLLMAQKEILSQQ 1018
Cdd:pfam05483 376 EDqlkiitmelqkksseleEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFekiaeelkGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1019 EIIMKLRTDLGEAHSR-MSDLRGELSEKQ-----------KMELERQvALVRQQSGELSMLKAKVAQTTGLMEKKDRELK 1086
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKeVEDLKTELEKEKlknieltahcdKLLLENK-ELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 1087 VLrEALRASQEKPRPHLST---EQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEetIQRQRKALS 1163
Cdd:pfam05483 535 QI-ENLEEKEMNLRDELESvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--IENKNKNIE 611
|
570
....*....|....*...
gi 1039768044 1164 ELRTRVRELEKANSCNHK 1181
Cdd:pfam05483 612 ELHQENKALKKKGSAENK 629
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
668-801 |
5.55e-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: 39.80 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 668 SLCLIYLL---EHYKKIMSQSQDLQAQMNASRETQKslrQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQE 744
Cdd:pfam06785 47 SLCLLLLLyywEDALKEKFEKSFLEEKEAKLTELDA---EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQL 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039768044 745 KSRSEEALEKAQARVRELENHLAsQKEALENSVAQEKRKMREMLEAERRKAQDLENQ 801
Cdd:pfam06785 124 QIQLQQISQDFAEFRLESEEQLA-EKQLLINEYQQTIEEQRSVLEKRQDQIENLESK 179
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
701-802 |
5.58e-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: 41.48 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 701 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 771
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlnlvQTALRQQEKIERYQEDLEELTERLEEQEE 368
|
90 100 110
....*....|....*....|....*....|....*
gi 1039768044 772 ALENsvAQEKrkmREMLEAERRKAQD----LENQL 802
Cdd:COG3096 369 VVEE--AAEQ---LAEAEARLEAAEEevdsLKSQL 398
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
707-920 |
7.47e-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: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 707 LAEKEKLAEKLEQEEKLKAKIQQLTEEkaaLEESIGQEKSRSEEALEKaqarVRELENHLASQKEALENSvaqeKRKMRE 786
Cdd:cd22656 99 LIDDLADATDDEELEEAKKTIKALLDD---LLKEAKKYQDKAAKVVDK----LTDFENQTEKDQTALETL----EKALKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 787 MLEAE-----RRKAQDLENQLTQQKEIsenntyEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENV--LNNKL 858
Cdd:cd22656 168 LLTDEggaiaRKEIKDLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALRLIAdLTAADTDLdnLLALI 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039768044 859 KDALVMVedaQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 920
Cdd:cd22656 242 GPAIPAL---EKLQGAWQAIATDLD-SLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEK 299
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
674-850 |
7.49e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 674 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEH------LAEKEKLA------EKLEQEEKLKAKIQQLTEEKAALEESI 741
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELdllrfqLEELEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 742 GQEKSRSEEALEKAQARVRELENH---LASQKEALENS------VAQEKRKMREMLEAERRKAQDLENQLTQQKEISE-- 810
Cdd:COG0497 236 SGGEGGALDLLGQALRALERLAEYdpsLAELAERLESAlieleeAASELRRYLDSLEFDPERLEEVEERLALLRRLARky 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039768044 811 NNTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 850
Cdd:COG0497 316 GVTVEELlAYAEELRAELAELENSDERLEELEAELAEAEAE 356
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
684-894 |
7.99e-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: 40.93 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 684 QSQDLQAQMnasRETQKSLRQEHLAEKEKLAEKLEQEEKLK---AKIQQLTEEKAALEESIGQ-EKSRSEEALEKA---- 755
Cdd:pfam01576 799 QLKKLQAQM---KDLQRELEEARASRDEILAQSKESEKKLKnleAELLQLQEDLAASERARRQaQQERDELADEIAsgas 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 756 -----QARVRELENHLASQKEALENS-------------VAQEKRKMREMLEAERRKAQDLENQlTQQKEISENNTYEKL 817
Cdd:pfam01576 876 gksalQDEKRRLEARIAQLEEELEEEqsntellndrlrkSTLQVEQLTTELAAERSTSQKSESA-RQQLERQNKELKAKL 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 818 KMRDTLEKEKRK--IQDLENRLTKQKEEIElKEQKENVLNN--------KLKDALVMVEDAQQMKTTESQRAETLALKLK 887
Cdd:pfam01576 955 QEMEGTVKSKFKssIAALEAKIAQLEEQLE-QESRERQAANklvrrtekKLKEVLLQVEDERRHADQYKDQAEKGNSRMK 1033
|
....*..
gi 1039768044 888 ETLAELE 894
Cdd:pfam01576 1034 QLKRQLE 1040
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
253-503 |
8.17e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 253 QDKDEIILLLGR-EVNRLSDFEMESKYKDALimnlQAEVADLSQRLSETAA---VAAARQSNrcdpklqgVDEGDDLRQK 328
Cdd:PLN02939 138 QNAEKNILLLNQaRLQALEDLEKILTEKEAL----QGKINILEMRLSETDArikLAAQEKIH--------VEILEEQLEK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 329 EIESMKSQInALQKGYSQVLSQTLAERNTEIESLKNEGENLKR---DHAITSGMVTSLQKDMSARNEQVQQLQEEVnrlr 405
Cdd:PLN02939 206 LRNELLIRG-ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAeliEVAETEERVFKLEKERSLLDASLRELESKF---- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 406 IENREKEYQLEALSSRCsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK--KNYMGQNIISKTLRE 483
Cdd:PLN02939 281 IVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKeaNVSKFSSYKVELLQQ 358
|
250 260
....*....|....*....|.
gi 1039768044 484 KNK-VEEKLQEDSRRKLLQLQ 503
Cdd:PLN02939 359 KLKlLEERLQASDHEIHSYIQ 379
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
283-597 |
9.32e-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: 40.58 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 283 IMNLQAEVADLSQRLSETAAVAAARQSNRC--DPKLQGVDEGDDLRQKEIESMKSQINALQKgysqvlsqtlaERNTEIE 360
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDSSntDTALTTLEEALSEKERIIERLKEQREREDR-----------ERLEELE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 361 SLKNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRRE 440
Cdd:pfam10174 472 SLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 441 AQEKELKLC---RSQMQDMEKEVRKLREElkknymgqniisktlreknkvEEKLQEDSRRKLLQLQEMGNRENLikinLE 517
Cdd:pfam10174 545 NAEEAVRTNpeiNDRIRLLEQEVARYKEE---------------------SGKAQAEVERLLGILREVENEKND----KD 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 518 RAVGQLENFRNQVIKATFGKTKPFRDKPitdQQLIEKIIQVTEDNLsfqqRKWTLQRETHLHPKQEETMHSVEKLRVLLD 597
Cdd:pfam10174 600 KKIAELESLTLRQMKEQNKKVANIKHGQ---QEMKKKGAQLLEEAR----RREDNLADNSQQLQLEELMGALEKTRQELD 672
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
684-864 |
9.65e-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: 40.71 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 684 QSQDLQAQMNASRETQKSLRQ------------EHLA---EKEKLAEKLEQEEKLKAKIQQLTeekaaleesigQEKSRS 748
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLKQqifalsevvqrrPHFSyedAVGLLGENSDLNEKLRARLEQAE-----------EARREA 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768044 749 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLE--------AE---RRKAQDLENQLTQQKeiSENNTYEKl 817
Cdd:COG3096 1004 REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeAEeraRIRRDELHEELSQNR--SRRSQLEK- 1080
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039768044 818 kmrdTLEKEKRKIQDLENRLTkqKEEIELKEQKENVLNNKLKDALVM 864
Cdd:COG3096 1081 ----QLTRCEAEMDSLQKRLR--KAERDYKQEREQVVQAKAGWCAVL 1121
|
|
| |
