|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
112-320 |
4.99e-79 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 253.38 E-value: 4.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 112 IRKGIPHHFRAIVWQLLCSATDMPVKN---QYSELLKMSSPCEKL----IRRDIARTYPEHEFFKGQDSLGQEVLFNVMK 184
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTSAdkdLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 185 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVRLMQEYRLReLFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRS 263
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1583180519 264 QSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQTELM 320
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
152-320 |
9.79e-57 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 192.08 E-value: 9.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 152 KLIRRDIARTYPEHEFFKGQDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVRLMQEYRLRE 230
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 231 LFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIV-FRVGL 309
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 1583180519 310 ALLQVNQTELM 320
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
108-330 |
6.98e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 163.05 E-value: 6.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 108 LKELIRKGIPHHFRAIVWQLLCSATDM--PVKNQYSELLKM-------SSPCEKLIRRDIARTYPEHEFFKGQDSLGQEV 178
Cdd:COG5210 205 LRELIRKGIPNELRGDVWEFLLGIGFDldKNPGLYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAEN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 179 LFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVRLMQEYRLRELFKPSMAELGLCIYQFEYMLQEQLPDL 257
Cdd:COG5210 285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583180519 258 NTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQTELMQLDMEGMSQY 330
Cdd:COG5210 365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDL 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-719 |
7.66e-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: 72.40 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 376 EEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQeaeenyvIKRELAVVRQQCSSTAEDLQKAQSTIRQLQ 455
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 456 EQQENprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVARLQEELKALKVREGEAVASARE 535
Cdd:TIGR02168 747 ERIAQ---LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---------IEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 536 LKLQLQELSDTWQAHLSRGGRWKESprklvLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAER 615
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERR-----LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 616 AALQEKLQYLAAQNKGLQTQLSESRRKqaeaeckskeevmavrLREADSMAAVAEMRQRIAELEIQREEGRI--QGQLNH 693
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRE----------------LEELREKLAQLELRLEGLEVRIDNLQERLseEYSLTL 953
|
330 340
....*....|....*....|....*.
gi 1583180519 694 SDSSQYIRELKDQIEELKTEVRLLKG 719
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-718 |
7.70e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSTAE 442
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 443 DLQKAQSTIRQLQEQQENprltedfVAHLETELEQSRLRETETLGALREMQdkvldMEKRNSSLPDENNVARLQEELKAL 522
Cdd:COG1196 345 ELEEAEEELEEAEAELAE-------AEEALLEAEAELAEAEEELEELAEEL-----LEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 523 KVREGEAVASARELKLQLQELSDTwqahlsrggrwkesprklvLGELQDELMTVRLREAQALADGREWRQRVVELETQDN 602
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEE-------------------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 603 IHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQR 682
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350
....*....|....*....|....*....|....*.
gi 1583180519 683 EegriqgqlNHSDSSQYIRELKDQIEELKTEVRLLK 718
Cdd:COG1196 554 E--------DDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-765 |
9.92e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 373 KEMEEQIE-IKRLRTEnrlLKQRIETLEKEsaaladrliqgqvtrAQEAEENYVIKRELAVVRQQcsSTAEDLQKAQSTI 451
Cdd:COG1196 182 EATEENLErLEDILGE---LERQLEPLERQ---------------AEKAERYRELKEELKELEAE--LLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 452 RQLQEQQEnprltedfvaHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENN-----VARLQEELKALKVRE 526
Cdd:COG1196 242 EELEAELE----------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaeLARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 527 GEAVASARELKLQLQELSDTWQAHLSRGGRWKESprklvLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRN 606
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 607 LLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGR 686
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1583180519 687 IQGQLNHSDSSQYIRELKDQIEELKTEVRLLKGPPTFEDPLAFDGLSLTRHLDEDSLPSSDEELLGVGVGVGAALQDPL 765
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
359-713 |
1.44e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIE--------------TLEKESAALADRLIQGQVTRAQEAEENY 424
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleeelaELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 425 VIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNS 504
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 505 SLPDE---------NNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRgGRWKESPRKLVLGELQDELMT 575
Cdd:COG1196 435 EEEEEeeealeeaaEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 576 VRLREAQALA-DGREWRQRVVELETQDNIH--RNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 652
Cdd:COG1196 514 LLLAGLRGLAgAVAVLIGVEAAYEAALEAAlaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1583180519 653 EvmAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKTE 713
Cdd:COG1196 594 R--GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
364-713 |
8.23e-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: 59.31 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 364 EKEYAAMKSKEMEEQIEikRLRTENRLLKQRIETLEKESA-ALADRLIQgqvTRAQEAEEnYVIKRELAVVRQQCSSTAE 442
Cdd:TIGR02169 171 KKEKALEELEEVEENIE--RLDLIIDEKRQQLERLRREREkAERYQALL---KEKREYEG-YELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 443 DLQKAQSTIRQLQEQQENPRLTedfVAHLETELEQSRLR-ETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKA 521
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKR---LEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASL--ERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 522 LKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESprklvLGELQDELMTVRLREAQALADGREWRQRVVELETQD 601
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-----YAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 602 NIHRNLLNRVEAERAALQEKLQYLaaqnkglqtqlsESRRKQAEAECKSKEE-VMAVRLREADSMAAVAEMRQRIAELEI 680
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRL------------SEELADLNAAIAGIEAkINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350
....*....|....*....|....*....|...
gi 1583180519 681 QREEGRIQgqlnHSDSSQYIRELKDQIEELKTE 713
Cdd:TIGR02169 463 DLSKYEQE----LYDLKEEYDRVEKELSKLQRE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-641 |
1.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 392 KQRIETLEKESAALADRL--IQGQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVA 469
Cdd:COG4913 609 RAKLAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 470 HLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVARLQEELKALKVREGEAVASARElkLQLQELSDTWQA 549
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 550 HLSRggrwkESPRKLV--LGELQDELMTVRLREAQALADG-----REWRQRVVELETQ-DNIH--RNLLNRVEAER-AAL 618
Cdd:COG4913 758 ALGD-----AVERELRenLEERIDALRARLNRAEEELERAmrafnREWPAETADLDADlESLPeyLALLDRLEEDGlPEY 832
|
250 260
....*....|....*....|....*...
gi 1583180519 619 QEKL-QYLAAQNK----GLQTQLSESRR 641
Cdd:COG4913 833 EERFkELLNENSIefvaDLLSKLRRAIR 860
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
362-710 |
7.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 362 RLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSTA 441
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 442 EDLQKAQ---STIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEK------------RNSSL 506
Cdd:COG1196 498 EAEADYEgflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAaaieylkaakagRATFL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 507 PDENNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKEsprKLVLGELQDELMTVRLREAQALAD 586
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA---RLEAALRRAVTLAGRLREVTLEGE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 587 GREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMA 666
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1583180519 667 AVAEMRQ-RIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEEL 710
Cdd:COG1196 735 EELLEELlEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
363-713 |
1.29e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLE-------KESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQ 435
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 436 QCSSTAEDLQKAQSTIRQLQEQQEnpRLTEDfVAHLETELE--QSRLRETETL---GALREMQDKVLDMEKRNSSLPDEN 510
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD--ELRER-EAELEATLRtaRERVEEAEALleaGKCPECGQPVEGSPHVETIEEDRE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 511 NVARLQEELKALKVREG------EAVASARELKLQLQELSDTWQAHLSRggrwkESPRKLVLGELQDELMTVRLREAQAL 584
Cdd:PRK02224 476 RVEELEAELEDLEEEVEeveerlERAEDLVEAEDRIERLEERREDLEEL-----IAERRETIEEKRERAEELRERAAELE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 585 ADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAqnkgLQTQLSESRRKQAEAEcKSKEEVMAVRLREADS 664
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIE-RLREKREALAELNDER 625
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1583180519 665 MAAVAEMRQRIAELEIQREEGRIQG-QLNHSDSSQYIRELKDQIEELKTE 713
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDEARIEEaREDKERAEEYLEQVEEKLDELREE 675
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
358-709 |
1.51e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQC 437
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 438 SSTAEDLQKAQSTI---RQLQEQQENPRLTEDF--VAHLETeLEQSRLRETETLGALREMQDKVLDMEKRNSSLPD---- 508
Cdd:PRK02224 429 AELEATLRTARERVeeaEALLEAGKCPECGQPVegSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDlvea 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 509 ENNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLvLGELQDELMTVRLREaQALADGR 588
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-EEEAEEAREEVAELN-SKLAELK 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 589 EWRQRVVELETQDNIHRNLlnrvEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEE-VMAVRLREADSMAA 667
Cdd:PRK02224 586 ERIESLERIRTLLAAIADA----EDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEY 661
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1583180519 668 VAEMRQRIAELEIQREE--GRIQGQLNHSDSSQYIRELKDQIEE 709
Cdd:PRK02224 662 LEQVEEKLDELREERDDlqAEIGAVENELEELEELRERREALEN 705
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-652 |
8.19e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 437 CSSTAEDLQKAQSTIRQLQEQQENprltedfvahLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQ 516
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--EQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 517 EELKALKVREGEAVASARELKLQLQELSDTWQAhLSRGGRWK-----ESPRKLV-LGELQDELMTVRLREAQAL-ADGRE 589
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYR-LGRQPPLAlllspEDFLDAVrRLQYLKYLAPARREQAEELrADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583180519 590 WRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 652
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-717 |
1.19e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAAL--------ADRLIQGQVTRAQEAEENYvikRE 429
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeleaLEAELAELPERLEELEERL---EE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 430 LAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEdfVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDE 509
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 510 NNVARLQEELKALKV--------------------------------------------REGEAVASARELKLQLQELSD 545
Cdd:COG4717 236 LEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 546 ----TWQAHLSRGGRWKESPRKLVLGELQdelmtvRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAE------- 614
Cdd:COG4717 316 leeeELEELLAALGLPPDLSPEELLELLD------RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelra 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 615 RAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADsmAAVAEMRQRIAELeiQREEGRIQGQLNHS 694
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE--EELEELEEELEEL--REELAELEAELEQL 465
|
410 420
....*....|....*....|...
gi 1583180519 695 DSSQYIRELKDQIEELKTEVRLL 717
Cdd:COG4717 466 EEDGELAELLQELEELKAELREL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-623 |
1.35e-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: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 348 LKAYQVKYNPKK--MKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYV 425
Cdd:TIGR02168 262 LQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 426 IKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENprltedfvahLETELEQSRLRETETLGALREMQDKVLDMEKRNSS 505
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEE----------LEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 506 LpdENNVARLQEELKAL--KVREGEAVASARELKLQLQELSDTwQAHLSRGGRWKEsprklvlgELQDELMTVRLREAQA 583
Cdd:TIGR02168 412 L--EDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEEL-QEELERLEEALE--------ELREELEEAEQALDAA 480
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1583180519 584 LADGREWRQRVVELETQDNihrNLLNRVEAERAALQEKLQ 623
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQE---NLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-684 |
1.39e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 361 KRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSST 440
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 441 AEDLQKAQST--IRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKV--------LDMEKRNSSLPDEN 510
Cdd:COG1196 511 KAALLLAGLRglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratfLPLDKIRARAALAA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 511 NVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTV-------------- 576
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGsaggsltggsrrel 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 577 RLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMA 656
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
330 340
....*....|....*....|....*...
gi 1583180519 657 VRLREADSMAAVAEMRQRIAELEIQREE 684
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-647 |
2.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 391 LKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQenprltedfvAH 470
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----------AE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 471 LETELEQSRLRETETLGALREM--QDKVLDMEKRNSSLPDENNVARLQEELKALKVRegeavasARELKLQLQELSdtwq 548
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ-------AEELRADLAELA---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 549 ahlsrggrwkesprklvlgELQDELMTVRLREAQALADGREWRQRvveLETQDNIHRNLLNRVEAERAALQEKLQYLAAQ 628
Cdd:COG4942 164 -------------------ALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|....*....
gi 1583180519 629 NKGLQTQLSESRRKQAEAE 647
Cdd:COG4942 222 AEELEALIARLEAEAAAAA 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
361-714 |
2.56e-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: 51.12 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 361 KRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSST 440
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 441 AEDLQKAQSTIRQ-----------LQEQQENPRLTEDFVAHLETELEQSRLRETETLGALRemqdkvldmekrnsslpDE 509
Cdd:TIGR00618 472 EQQLQTKEQIHLQetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR-----------------GE 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 510 NNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKL--VLGELQDEL-MTVRLREAQALAD 586
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnITVRLQDLTeKLSEAEDMLACEQ 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 587 GREWRQRVVELETQDnihrnllnrVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKS-KEEVMAVRLREADsm 665
Cdd:TIGR00618 615 HALLRKLQPEQDLQD---------VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlPKELLASRQLALQ-- 683
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1583180519 666 aavaEMRQRIAELEIQREEgriqgqLNHSDSSqyIRELKDQIEELKTEV 714
Cdd:TIGR00618 684 ----KMQSEKEQLTYWKEM------LAQCQTL--LRELETHIEEYDREF 720
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-684 |
5.97e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 435 QQCSSTAEDLQKAQSTIRQLQEQQENprlTEDFVAHLETELEQSRLRETETLGALREMQDKvldmekrnsslpdennVAR 514
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---LKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 515 LQEELKALKVREGEAVASARELKLQLQELSDTWQahlsRGGRwkESPRKLVLGELQDELMTVRLREAQALADGRewRQRV 594
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALY----RLGR--QPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 595 VELETQdnihRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQR 674
Cdd:COG4942 153 EELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|
gi 1583180519 675 IAELEIQREE 684
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-711 |
7.76e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 354 KYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQ----VTRAQEAEENYVIKRE 429
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARkaeeARKAEDAKKAEAARKA 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 430 LAVVRQQCSSTAEDLQKAQSTIRQLQEQ--QENPRLTEDFVAHLETELEQSRLRETETLGA--LREMQDKVLDMEKRNSS 505
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERkaEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAeeERNNEEIRKFEEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 506 LPDENNVARLQEELKALKVREGEAVASAREL-KLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQAL 584
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 585 ADGREWRQRvvelETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEV--MAVRLREA 662
Cdd:PTZ00121 1345 AEAAKAEAE----AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKA 1420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1583180519 663 DSMAAVAEMRQRIAELEIQREEGRIQGQL-NHSDSSQYIRELKDQIEELK 711
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAkKKAEEAKKAEEAKKKAEEAK 1470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
511-719 |
9.39e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 511 NVARLQEELKALKVREGEAVASARELKL--QLQELSDTWQAHLSRGGRWKE--SPRKLVLGELQDELMTVRLREAQALAD 586
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 587 GREwrQRVVELETQDNIHRNLLNRVEAERAALQ-EKLQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSM 665
Cdd:COG4913 306 RLE--AELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE----ALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1583180519 666 AAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKTEVRLLKG 719
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
349-713 |
1.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 349 KAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAAL--ADRLIQG--QVTRAQEAEEny 424
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKaeEKKKADEAKK-- 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 425 viKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDF-----VAHLETELEQSRlRETETLGALREMQDKVLDM 499
Cdd:PTZ00121 1439 --KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeakkADEAKKKAEEAK-KKADEAKKAAEAKKKADEA 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 500 ----EKRNSSLPDENNVARLQEEL-KALKVREGEAVASARELKlQLQELSDTWQAHLSRGGRWKESPRKLVLGELQ---- 570
Cdd:PTZ00121 1516 kkaeEAKKADEAKKAEEAKKADEAkKAEEKKKADELKKAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEeari 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 571 DELMTVRLRE----AQALADGREWRQRVVELETQDNIHRNL--LNRVEAERAALQEKLQYLAAQNKGLQTQLS----ESR 640
Cdd:PTZ00121 1595 EEVMKLYEEEkkmkAEEAKKAEEAKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeEDK 1674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 641 RK-----QAEAECKSKEEVMAvrlREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIR---ELKDQIEELKT 712
Cdd:PTZ00121 1675 KKaeeakKAEEDEKKAAEALK---KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeaeEDKKKAEEAKK 1751
|
.
gi 1583180519 713 E 713
Cdd:PTZ00121 1752 D 1752
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
351-709 |
1.66e-05 |
|
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: 48.58 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 351 YQVKYNPKKMKrlEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKREL 430
Cdd:pfam17380 256 YTVRYNGQTMT--ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 431 AVVRQQcSSTAEDLQKAQSTIRQLQEQQENPRLTEDfvahlETELEQSRLRETETLGALREMQDKvldmekrnsslpden 510
Cdd:pfam17380 334 AIYAEQ-ERMAMERERELERIRQEERKRELERIRQE-----EIAMEISRMRELERLQMERQQKNE--------------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 511 nvaRLQEELKAlkvregeavasARELKLQLQElsdtwqahlsRGGRWKESPRKLvlGELQDELMTVRLREAQALADGREW 590
Cdd:pfam17380 393 ---RVRQELEA-----------ARKVKILEEE----------RQRKIQQQKVEM--EQIRAEQEEARQREVRRLEEERAR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 591 ---RQRVVELETQDNIHRnlLNRVEAERAalQEKLQYLAAQNKglQTQLSESRRKQAEAECKSKEEVMAVRLR------- 660
Cdd:pfam17380 447 emeRVRLEEQERQQQVER--LRQQEEERK--RKKLELEKEKRD--RKRAEEQRRKILEKELEERKQAMIEEERkrkllek 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583180519 661 --EADSMAAVAEMRQRIAELEIQR-----EEGRIQGQLNHS-------DSSQYIRELKDQIEE 709
Cdd:pfam17380 521 emEERQKAIYEEERRREAEEERRKqqemeERRRIQEQMRKAteersrlEAMEREREMMRQIVE 583
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-718 |
1.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 381 IKRLR--TENRLLKQRIETLEKESAALADRL--IQGQVTRAQEAEENYVIKRELAvvrqqcsstAEDLQKAQSTIRQLQE 456
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERLngLESELAELDEEIERYEEQREQA---------RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 457 QQENprltedfVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVARLQEELKALkvrEGEAVASARE- 535
Cdd:PRK02224 249 RREE-------LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREe 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 536 LKLQLQELSDTWQAHLSRGGRWKESPRklvlgelqdelmtvRLREAQALADGR--EWRQRVVELETQDNIHRNLLNRVEA 613
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAE--------------SLREDADDLEERaeELREEAAELESELEEAREAVEDRRE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 614 ERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQ--GQ- 690
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCPecGQp 460
|
330 340
....*....|....*....|....*...
gi 1583180519 691 LNHSDSSQYIRELKDQIEELKTEVRLLK 718
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-623 |
2.57e-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: 48.13 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 359 KMKRLEKEyaamkSKEMEEQIEikRLRTENRLLKQRIETLEKESAALAdRLIQGQVTRAQEAEEnyvikrELAVVRQQCS 438
Cdd:TIGR02168 254 ELEELTAE-----LQELEEKLE--ELRLEVSELEEEIEELQKELYALA-NEISRLEQQKQILRE------RLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 439 STAEDLQKAQStirQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEE 518
Cdd:TIGR02168 320 ELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL--RSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 519 LKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQALADGREWRQRVVELE 598
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260
....*....|....*....|....*
gi 1583180519 599 TQDNIHRNLLNRVEAERAALQEKLQ 623
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
364-723 |
3.38e-05 |
|
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: 47.66 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 364 EKEYAAMKsKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSST-AE 442
Cdd:pfam02463 169 RKKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQElLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 443 DLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpDENNVARLQEELKAL 522
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD-DEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 523 KVREGEAVASARELKLQLQELSDTWQAHLSRggRWKESPRKLVLGELQDELMTVRLREAQAL--ADGREWRQRVVELETQ 600
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEE--EEELEKLQEKLEQLEEELLAKKKLESERLssAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 601 DNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEI 680
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1583180519 681 QREEGRIQGQLNHSDSSQ-YIRELKDQIEELKTEVRLLKGPPTF 723
Cdd:pfam02463 485 QLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAH 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-718 |
3.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 362 RLEKEYAAMKSKEMEEQIEIKRLRTENRLLK--------QRIETLEKESAALADRLiqgqvTRAQEAEENYviKRELAVV 433
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLEREL-----EERERRRARL--EALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 434 RQQCSSTAEDLQKAQSTIRQLQEQqenprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnVA 513
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEA------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR--LL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 514 RLQEEL-KALKVREGEA--VAsarELkLQLQELSDTWQ------------------AHLSRGGRWKES------------ 560
Cdd:COG4913 444 ALRDALaEALGLDEAELpfVG---EL-IEVRPEEERWRgaiervlggfaltllvppEHYAAALRWVNRlhlrgrlvyerv 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 561 -----------------PRKLVL------GELQDEL--------------------------MTVRLREAQALADGREWR 591
Cdd:COG4913 520 rtglpdperprldpdslAGKLDFkphpfrAWLEAELgrrfdyvcvdspeelrrhpraitragQVKGNGTRHEKDDRRRIR 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 592 QRVVeLeTQDNIHRnlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRK------------------QAEAECKSKEE 653
Cdd:COG4913 600 SRYV-L-GFDNRAK--LAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvaSAEREIAELEA 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1583180519 654 VMAvRLREADSmaAVAEMRQRIAELEIQREEGRIQ-GQLNHSdssqyIRELKDQIEELKTEVRLLK 718
Cdd:COG4913 676 ELE-RLDASSD--DLAALEEQLEELEAELEELEEElDELKGE-----IGRLEKELEQAEEELDELQ 733
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
452-683 |
6.65e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 452 RQLQEQQENPRLTEDFvahLETELEQSR--LRETETlgALREMQDK--VLDMEKRNSSLpdENNVARLQEELKALKVREG 527
Cdd:COG3206 164 QNLELRREEARKALEF---LEEQLPELRkeLEEAEA--ALEEFRQKngLVDLSEEAKLL--LQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 528 EAVASARELKLQLQELSDTWQAHLsrggrwkESPrklVLGELQDELMTVRLREAQALADGREWRQRVVELETQ------- 600
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELL-------QSP---VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQiaalraq 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 601 -DNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaeckskeevMAVRLREADSMAAV-AEMRQRIAEL 678
Cdd:COG3206 307 lQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELyESLLQRLEEA 377
|
....*
gi 1583180519 679 EIQRE 683
Cdd:COG3206 378 RLAEA 382
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
364-711 |
7.88e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.22 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 364 EKEYAAMKSKEMEEQI-----EIKRLRTENRLLKQRI---ETLEKESAALADRLIQGQVTRAQEAEENY----------- 424
Cdd:pfam05622 8 EKDELAQRCHELDQQVsllqeEKNSLQQENKKLQERLdqlESGDDSGTPGGKKYLLLQKQLEQLQEENFrletarddyri 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 425 ---VIKRELAVVRQQcsstAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRlRETETLGALREmQDKVLdmEK 501
Cdd:pfam05622 88 kceELEKEVLELQHR----NEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYK-KKLEDLGDLRR-QVKLL--EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 502 RNSSLPDENnvARLQEELKalkvREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKL-----VLGELQDELMTV 576
Cdd:pfam05622 160 RNAEYMQRT--LQLEEELK----KANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLeekleALQKEKERLIIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 577 R--LREAQ-----ALADGREWRQRVVELETQDNIHRNLlnRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECK 649
Cdd:pfam05622 234 RdtLRETNeelrcAQLQQAELSQADALLSPSSDPGDNL--AAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1583180519 650 SKEEVMAVR--LREADSMAavaemRQRIAELEIQREE--GRIQGQLNHS-DSSQYIRELKDQIEELK 711
Cdd:pfam05622 312 LLEDANRRKneLETQNRLA-----NQRILELQQQVEElqKALQEQGSKAeDSSLLKQKLEEHLEKLH 373
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-646 |
9.50e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALadrliqgqvtraqeaeenyviKRELAVVRQQC 437
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT---------------------ERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 438 SSTAEDLQKAQSTIRQLQEQQEnpRLTEDFVAHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQE 517
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIE--ELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSEL--RRELEELRE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 518 ELKALKVREGeavasarELKLQLQELSDTwqahlsrggrwkesprklVLGELQDELMTVRLREAQALADGREWRQRVVEL 597
Cdd:TIGR02168 923 KLAQLELRLE-------GLEVRIDNLQER------------------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1583180519 598 ETQ-DNIHR-NLLnrVEAERAALQEKLQYLAAQnkglQTQLSESRRKQAEA 646
Cdd:TIGR02168 978 ENKiKELGPvNLA--AIEEYEELKERYDFLTAQ----KEDLTEAKETLEEA 1022
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
358-691 |
1.62e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENR---------LLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKR 428
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAkkeeelqaaLARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 429 ELAvvRQQCSSTAEDLQ-------------KAQSTIRQLQEQQ--ENPRLTEDFVAHLETELEQSRLRETETLGALREMQ 493
Cdd:pfam01576 288 NKA--EKQRRDLGEELEalkteledtldttAAQQELRSKREQEvtELKKALEEETRSHEAQLQEMRQKHTQALEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 494 DKV----LDMEKRNSSLPDENNvaRLQEELKALKVREGEAVASARELKLQLQELsdtwQAHLSRGGRWKESpRKLVLGEL 569
Cdd:pfam01576 366 EQAkrnkANLEKAKQALESENA--ELQAELRTLQQAKQDSEHKRKKLEGQLQEL----QARLSESERQRAE-LAEKLSKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 570 QDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLN--------------RVEAERAALQEKL-------QYLAAQ 628
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqklnlstrlrQLEDERNSLQEQLeeeeeakRNVERQ 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1583180519 629 NKGLQTQLSESRRKQAE--AECKSKEEVMAVRLREADsmAAVAEMRQRIAELE-IQREEGRIQGQL 691
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEdaGTLEALEEGKKRLQRELE--ALTQQLEEKAAAYDkLEKTKNRLQQEL 582
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
344-718 |
1.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 344 DKLVLKAYQVKyNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRllKQRIETLEK--ESAALADRLIQGQVTRAQEAE 421
Cdd:PTZ00121 1332 DAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKkaEEKKKADEAKKKAEEDKKKAD 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 422 EnyVIKRELAVVR-QQCSSTAEDLQKAQstirQLQEQQENPRLTEDfvahLETELEQSRlrETETLGALREMQDKVLDME 500
Cdd:PTZ00121 1409 E--LKKAAAAKKKaDEAKKKAEEKKKAD----EAKKKAEEAKKADE----AKKKAEEAK--KAEEAKKKAEEAKKADEAK 1476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 501 KRNSSLPDENNVARLQEELKalkvREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTV-RLR 579
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELK 1552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 580 EAQALADGREWRQrvVELETQDNIHRNL-LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEevmavr 658
Cdd:PTZ00121 1553 KAEELKKAEEKKK--AEEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE------ 1624
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1583180519 659 LREADSMAAVAEMRQRIAELEIQREEgriqgQLNHSDSSQYIR--ELKDQIEELKTEVRLLK 718
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAE-----ELKKAEEENKIKaaEEAKKAEEDKKKAEEAK 1681
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-543 |
1.73e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 380 EIKRLRTENRLLKQRIETLEKESAALADRLIQgqvtraqeaeenyvIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQE 459
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEA--------------AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 460 NPRLTEDFVAhLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREGEAVAsarELKLQ 539
Cdd:COG1579 84 NVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAELDEELA---ELEAE 157
|
....
gi 1583180519 540 LQEL 543
Cdd:COG1579 158 LEEL 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-543 |
1.98e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQ-----GQVTRAQEAEENYVIKR---- 428
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 429 ---------ELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDM 499
Cdd:COG4942 114 yrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1583180519 500 EKRNSSLpdennVARLQEELKALKVREGEAVASARELKLQLQEL 543
Cdd:COG4942 194 KAERQKL-----LARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
353-714 |
2.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 353 VKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLiqGQVTRAQEAEENYVI----KR 428
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKELKEKAEEYIKlsefYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 429 ELAVVRQQCSSTAEDL-QKAQSTIRQLQEQQE-NPRLTEDFVAHLETELEQSRLRET-ETLGALREMQDKVLDMEKRNSS 505
Cdd:PRK03918 304 EYLDELREIEKRLSRLeEEINGIEERIKELEEkEERLEELKKKLKELEKRLEELEERhELYEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 506 LPDENNVARLQ----------EELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMT 575
Cdd:PRK03918 384 LTPEKLEKELEelekakeeieEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 576 VRLREAQALADGREWRQRVVELETQDNIHRNLL-------------------NRVEAERAA-----LQEKLQYLAAQNKG 631
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESELIklkelaeqlkeleeklkkyNLEELEKKAeeyekLKEKLIKLKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 632 LQTQLS-----ESRRKQAEAECKSKEEVMAVRLREADSMA--AVAEMRQRIAELEIQREEgriqgQLNHSDSSQYIRELK 704
Cdd:PRK03918 544 LKKELEkleelKKKLAELEKKLDELEEELAELLKELEELGfeSVEELEERLKELEPFYNE-----YLELKDAEKELEREE 618
|
410
....*....|
gi 1583180519 705 DQIEELKTEV 714
Cdd:PRK03918 619 KELKKLEEEL 628
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
373-545 |
2.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 373 KEMEEQIEIKRLRTENRLLKQRIETLEKESAALadrliQGQVTRAQEAEENyvIKRELAVVRQQC-SSTAEDLQKAQSTI 451
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARL-----EAELERLEARLDA--LREELDELEAQIrGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 452 RQLQEQQENprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMekrnsslpdennVARLQEELKALKVREGEAVA 531
Cdd:COG4913 348 ERLERELEE---RERRRARLEALLAALGLPLPASAEEFAALRAEAAAL------------LEALEEELEALEEALAEAEA 412
|
170
....*....|....
gi 1583180519 532 SARELKLQLQELSD 545
Cdd:COG4913 413 ALRDLRRELRELEA 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-534 |
2.81e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELavvrqqcS 438
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-------D 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 439 STAEDLQKAQSTIRQLQEQQENprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEE 518
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAG---IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL--KEEYDRVEKE 484
|
170
....*....|....*.
gi 1583180519 519 LKALKVREGEAVASAR 534
Cdd:TIGR02169 485 LSKLQRELAEAEAQAR 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-544 |
2.98e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 354 KYNPKKMKRLEKEYAAMKSK--EMEEQI--------EIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEEN 423
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKliKLKGEIkslkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 424 YvikRELAVVRQQCSStaedLQKAQSTIRQLQEQQENprltedfvahLETELEQSRLRETETLGALREMQDKVLDMEK-- 501
Cdd:PRK03918 594 L---KELEPFYNEYLE----LKDAEKELEREEKELKK----------LEEELDKAFEELAETEKRLEELRKELEELEKky 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1583180519 502 --------RNSSLPDENNVARLQEELKALKVREGEAVASARELKLQLQELS 544
Cdd:PRK03918 657 seeeyeelREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
457-679 |
3.30e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.54 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 457 QQENPRLTE------DFVAHLETELEQSRlretetlgALREMQDKVLDMEKRNSslpdennvarlqEELKalkvregEAV 530
Cdd:PLN03188 1050 EQERLRWTEaeskwiSLAEELRTELDASR--------ALAEKQKHELDTEKRCA------------EELK-------EAM 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 531 ASARELKLQ-LQELSDTWQAHLSRGGRWKEsprklvlgeLQDELMTVRLREAQALADGREWRqrvveletqdnihrnLLN 609
Cdd:PLN03188 1103 QMAMEGHARmLEQYADLEEKHIQLLARHRR---------IQEGIDDVKKAAARAGVRGAESK---------------FIN 1158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1583180519 610 RVEAERAAL----QEKLQYLAAQNKGLQTQLsesrRKQAEAECKSKEevMAVRLREADSMAAVAEMRQRIAELE 679
Cdd:PLN03188 1159 ALAAEISALkverEKERRYLRDENKSLQAQL----RDTAEAVQAAGE--LLVRLKEAEEALTVAQKRAMDAEQE 1226
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
376-711 |
3.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 376 EEQIEIKRLRTENRLLKQRIETLEKESAALADRlIQGQVTRAQEAEENYV-----------------------------I 426
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEERDdllaeaglddadaeavearreeledrdeeL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 427 KRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRlteDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSL 506
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELR---EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 507 PD-----ENNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHL--SRGGRWKESPRKLVLGELQDELMTVRLR 579
Cdd:PRK02224 404 PVdlgnaEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpECGQPVEGSPHVETIEEDRERVEELEAE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 580 EAQALADGREWRQRVVELETQDNIHRNlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmavRL 659
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK----RE 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1583180519 660 READSMAAVAEMRQRIAELEIQREE--GRIQGQLNHSDSSQYIRELKDQIEELK 711
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAElkERIESLERIRTLLAAIADAEDEIERLR 612
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
363-718 |
4.43e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKrELAVVRQQCSSTAE 442
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK-ELEFEIQSQEQDSE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 443 DLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETET------LGALREMQDKVLDMEKRNSSLPDE------- 509
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVedlkrkLEREEKYREEAATLELEKEKLEQElqswvkl 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 510 ---------------NNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLS-----RGGRWKESP------RK 563
Cdd:pfam05557 268 aqdtglnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKkiedlNKKLKRHKAlvrrlqRR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 564 LVLGELQDELMTVRLR----EAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSES 639
Cdd:pfam05557 348 VLLLTKERDGYRAILEsydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 640 RRKQAEAE-CKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDS----------SQYIRELKDQIE 708
Cdd:pfam05557 428 RQQESLADpSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpaAEAYQQRKNQLE 507
|
410
....*....|
gi 1583180519 709 ELKTEVRLLK 718
Cdd:pfam05557 508 KLQAEIERLK 517
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
363-710 |
7.00e-04 |
|
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: 43.40 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRL--------IQGQVTRAQE--------AEENYVI 426
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLnlvqtalrQQEKIERYQEdleelterLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 427 KRELAVVRQQCSSTAE--------------DLQKA---QSTiRQLQEQQ------------ENPRLTEDfvaHLETELEQ 477
Cdd:COG3096 370 VEEAAEQLAEAEARLEaaeeevdslksqlaDYQQAldvQQT-RAIQYQQavqalekaralcGLPDLTPE---NAEDYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 478 SRLRETETLGALREMQDKVldmekrnsSLPDEnNVARLQEELKALK-----VREGEAVASARELKLQLQELsdtwQAHLS 552
Cdd:COG3096 446 FRAKEQQATEEVLELEQKL--------SVADA-ARRQFEKAYELVCkiageVERSQAWQTARELLRRYRSQ----QALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 553 RggrwkESPRKLVLGELQDELMtvRLREAQALADGREWRQRvVELETQDNIHRnLLNRVEAERAALQEKLQYLAAQNKGL 632
Cdd:COG3096 513 R-----LQQLRAQLAELEQRLR--QQQNAERLLEEFCQRIG-QQLDAAEELEE-LLAELEAQLEELEEQAAEAVEQRSEL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 633 QTQLSESRRKQAEAECKS----KEEVMAVRLREA-----DSMAAVAEMRQRIAELEIQREEGRiqgqlnhSDSSQYIREL 703
Cdd:COG3096 584 RQQLEQLRARIKELAARApawlAAQDALERLREQsgealADSQEVTAAMQQLLEREREATVER-------DELAARKQAL 656
|
....*..
gi 1583180519 704 KDQIEEL 710
Cdd:COG3096 657 ESQIERL 663
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
357-543 |
8.66e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 357 PKKMKRLEKEYAamKSKEMEEQIEIKRLRTENRLLKQRI----ETLEKESAA------LADRLIQgQVTRAQeaEENYVI 426
Cdd:PRK04778 255 EKEIQDLKEQID--ENLALLEELDLDEAEEKNEEIQERIdqlyDILEREVKArkyvekNSDTLPD-FLEHAK--EQNKEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 427 KRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENprltedfVAHLETELEQSRLRETETLGALREMQDKVLDMEKrnssl 506
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELESVRQLEKQLESLEKQ-------YDEITERIAEQEIAYSELQEELEEILKQLEEIEK----- 397
|
170 180 190
....*....|....*....|....*....|....*....
gi 1583180519 507 pdenNVARLQEELKALkvREGEAVA--SARELKLQLQEL 543
Cdd:PRK04778 398 ----EQEKLSEMLQGL--RKDELEAreKLERYRNKLHEI 430
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
380-506 |
9.29e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.93 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 380 EIKRLRTENRLLKQRIETLEKESAALADRLiQGQVTRAQEAEENYviKREL---AVVRQQCSSTAEDLQKAQSTIRQLQE 456
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDL-EKQAEIAREAQQNY--ERELvlhAEDIKALQALREELNELKAEIAELKA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1583180519 457 QqenprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSL 506
Cdd:pfam07926 79 E------AESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLL 122
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-681 |
1.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 357 PKKMKRLEKEYAAMKSKEMEeqieIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYV-IKRELAVVRQ 435
Cdd:COG4717 145 PERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAeLEEELEEAQE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 436 QCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAH---------------------------------------LETELE 476
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllallflllaREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 477 QSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVARLQEELKAL-KVREGEAVASARELKLQLQELSDTWQAHLSRGG 555
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIeELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 556 ---------------RWKESPRKLVLGELQDELMTVRLREAQALADGREWRQRVVELETQdnihrnlLNRVEAERAALQE 620
Cdd:COG4717 381 vedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE-------LEELEEELEELRE 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1583180519 621 KLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQ 681
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
399-709 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 399 EKESAALADRLIQgQVTRAQEAEENYVIKRE----LAVVRQQCsstaEDLQKAQSTIRQLQEQQEnprLTEDFVAHLETE 474
Cdd:COG4913 220 EPDTFEAADALVE-HFDDLERAHEALEDAREqielLEPIRELA----ERYAAARERLAELEYLRA---ALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 475 LEQSRLRETETlgalremqdkvldmekrnsslpdenNVARLQEELKALKVREGEAVASARELKlqlqelsdtwQAHLSRG 554
Cdd:COG4913 292 LLEAELEELRA-------------------------ELARLEAELERLEARLDALREELDELE----------AQIRGNG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 555 GRWKEsprklvlgelqdelmtvrlreaqaladgrEWRQRVVELETQdnihrnlLNRVEAERAALQEKLQYLAAQNKGLQT 634
Cdd:COG4913 337 GDRLE-----------------------------QLEREIERLERE-------LEERERRRARLEALLAALGLPLPASAE 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1583180519 635 QLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAEL--EIQREEGRiqgqlnHSDSSQYIRELKDQIEE 709
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaEIASLERR------KSNIPARLLALRDALAE 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
404-628 |
1.63e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 404 ALADRLIQGQVTRAQEAEENYV--IKRELAVVRQQcsstaedLQKAQSTIRQLQEQ------QENPRLTEDFVAHLETEL 475
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALefLEEQLPELRKE-------LEEAEAALEEFRQKnglvdlSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 476 EQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVARLQEELKALKVREGEAVA-------SARELKLQLQELSDTWQ 548
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 549 AHLSRGGRWKESPRKLV---LGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAerAALQEKLQYL 625
Cdd:COG3206 309 QEAQRILASLEAELEALqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVG 386
|
...
gi 1583180519 626 AAQ 628
Cdd:COG3206 387 NVR 389
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
358-647 |
2.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQC 437
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 438 SSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVARLQE 517
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 518 ELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQALADGreWRQRVVEL 597
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL--IGALEDAL 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1583180519 598 ETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAE 647
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
363-684 |
2.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQ-VTRAQEAEENYVIkrELAVVRQQCSSTA 441
Cdd:PRK04863 291 LRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQtALRQQEKIERYQA--DLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 442 EDLQKAQStirQLQEQQENPRLTEDFVAHLETELE--QSRLRETETLgALREMQDK-VLDMEKRNSSLPD--ENNVARLQ 516
Cdd:PRK04863 369 EVVEEADE---QQEENEARAEAAEEEVDELKSQLAdyQQALDVQQTR-AIQYQQAVqALERAKQLCGLPDltADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 517 EELKAlkvREGEAVASARELKlqlQELSDTwQAHLSRGGRWKESPRKLVlGELQDELMTVRLREaqALADGREWRQRVVE 596
Cdd:PRK04863 445 EEFQA---KEQEATEELLSLE---QKLSVA-QAAHSQFEQAYQLVRKIA-GEVSRSEAWDVARE--LLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 597 LETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQ-LSESRRKQAEAECKS-KEEVMAVRLREADSMAAVAEMRQR 674
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEdELEQLQEELEARLESlSESVSEARERRMALRQQLEQLQAR 594
|
330
....*....|
gi 1583180519 675 IAELEIQREE 684
Cdd:PRK04863 595 IQRLAARAPA 604
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-718 |
2.43e-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: 41.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 384 LRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENyvikrelAVVRQQCSSTAEDLQKAQSTIRqlQEQQENPRL 463
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES-------GNLDDQLQKLLADLHKREKELS--LEKEQNKRL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 464 TEDFVAHletELEQSRLRetetlgalREMQDKvlDMEkrnsslpdennVARLQEELKALKVR---EGEAVASARELKLQL 540
Cdd:pfam15921 404 WDRDTGN---SITIDHLR--------RELDDR--NME-----------VQRLEALLKAMKSEcqgQMERQMAAIQGKNES 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 541 QELSDTWQAHLSRGgrwKESPRKlVLGELQDELMTVRL--REAQALADGREWRQRVVElETQDNIHRnLLNRVEAEraaL 618
Cdd:pfam15921 460 LEKVSSLTAQLEST---KEMLRK-VVEELTAKKMTLESseRTVSDLTASLQEKERAIE-ATNAEITK-LRSRVDLK---L 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 619 QEkLQYLAAQNKGLQtqlsesrrkQAEAECKskeevmAVRLREADSMAAVAEMRQRIAEL-EIQREEGRIQGQLnHSDSS 697
Cdd:pfam15921 531 QE-LQHLKNEGDHLR---------NVQTECE------ALKLQMAEKDKVIEILRQQIENMtQLVGQHGRTAGAM-QVEKA 593
|
330 340
....*....|....*....|.
gi 1583180519 698 QYIRELKDQIEELKtEVRLLK 718
Cdd:pfam15921 594 QLEKEINDRRLELQ-EFKILK 613
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
442-630 |
2.78e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 442 EDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRetetlgaLREMQDKVLDMEKRNSSLPDENNVARLQEELKA 521
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 522 LKVRegeavasARELKLQLQELSDtWQAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQALADGREWRQRVVELETQD 601
Cdd:COG4717 144 LPER-------LEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 1583180519 602 NIHRNLLNRVEAERAALQEKLQYLAAQNK 630
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
371-678 |
2.81e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.28 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 371 KSKEMEE--QIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQ 448
Cdd:pfam07111 138 SQRELEEiqRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 449 STIRQLQEQQENPRLTEdfVAHLETELEQSRLreTETLGALREmqdkvldmekrnsslpdenNVARLQEELKALKVRege 528
Cdd:pfam07111 218 TLVESLRKYVGEQVPPE--VHSQTWELERQEL--LDTMQHLQE-------------------DRADLQATVELLQVR--- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 529 aVASARELkLQLQElsdtwqahlsrggrwKESPRKLvlgELQDELMTVRLREAQALAdgREWRQRV----VELETQDNIH 604
Cdd:pfam07111 272 -VQSLTHM-LALQE---------------EELTRKI---QPSDSLEPEFPKKCRSLL--NRWREKVfalmVQLKAQDLEH 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 605 RNLLNRVEAERAALQEK--------------LQYLAAQ-------NKGLQTQLS---ESRRKQ----AEAECKSKEEVMA 656
Cdd:pfam07111 330 RDSVKQLRGQVAELQEQvtsqsqeqailqraLQDKAAEvevermsAKGLQMELSraqEARRRQqqqtASAEEQLKFVVNA 409
|
330 340
....*....|....*....|..
gi 1583180519 657 VRLREADSMAAVAEMRQRIAEL 678
Cdd:pfam07111 410 MSSTQIWLETTMTRVEQAVARI 431
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
441-685 |
2.90e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 441 AEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvarLQEELK 520
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-----LSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 521 ALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLvLGELQDELMTVRLREAQALADGREWRQRVVELETQ 600
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA-GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 601 dnihRNLLNRVEAERAALQEKLQylaaqnkGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEI 680
Cdd:pfam07888 198 ----RNSLAQRDTQVLQLQDTIT-------TLTQKLTTAHRKEAENE-ALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
....*
gi 1583180519 681 QREEG 685
Cdd:pfam07888 266 QRDRT 270
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
509-718 |
3.54e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 509 ENNVARLQEELKALKvREGEAVASARELKLQLQELsdtwQAHLSrGGRWKEsprklvlgeLQDELMTVRLREAQALADGR 588
Cdd:TIGR02168 192 EDILNELERQLKSLE-RQAEKAERYKELKAELREL----ELALL-VLRLEE---------LREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 589 EWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEckSKEEVMAVRLREADSM--- 665
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE--RQLEELEAQLEELESKlde 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1583180519 666 --AAVAEMRQRIAELEIQREEGRIQGQLNHS---DSSQYIRELKDQIEELKTEVRLLK 718
Cdd:TIGR02168 335 laEELAELEEKLEELKEELESLEAELEELEAeleELESRLEELEEQLETLRSKVAQLE 392
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-507 |
3.75e-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: 40.88 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 348 LKAYQVKYNPKKMKRLEKEYAA----MKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEEN 423
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERARemerVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 424 Y-----------VIKRELAvVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLEtelEQSRLretETLGALREM 492
Cdd:pfam17380 505 KqamieeerkrkLLEKEME-ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRL---EAMEREREM 577
|
170
....*....|....*
gi 1583180519 493 QDKVLDMEKRNSSLP 507
Cdd:pfam17380 578 MRQIVESEKARAEYE 592
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
592-717 |
3.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 592 QRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSmaAVAEM 671
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP--DVIAL 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1583180519 672 RQRIAELE--IQREEGRIQGQLNHSDSSQYIRE--LKDQIEELKTEVRLL 717
Cdd:COG3206 297 RAQIAALRaqLQQEAQRILASLEAELEALQAREasLQAQLAQLEARLAEL 346
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
580-713 |
4.86e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.39 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 580 EAQALADGREWRQRVvELETQdnihrNLLNRVEAEraalQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSkeevmavRL 659
Cdd:PTZ00491 667 AARHQAELLEQEARG-RLERQ-----KMHDKAKAE----EQRTKLLELQAESAAVESSGQSRAEALAEAEA-------RL 729
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1583180519 660 READSMAAVAEMR---QRI---AELEIQREegRIQGQLNHSDSS-----QYIRELKDqIEELKTE 713
Cdd:PTZ00491 730 IEAEAEVEQAELRakaLRIeaeAELEKLRK--RQELELEYEQAQneleiAKAKELAD-IEATKFE 791
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
361-713 |
5.49e-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: 40.54 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 361 KRLEKEYAAMKSKEMEEqieiKRLRTENRLLKQRIEtlekESAALADRLIQGQVTRAQEAEENYVikrELAVVRQQCSSt 440
Cdd:pfam01576 531 KKLEEDAGTLEALEEGK----KRLQRELEALTQQLE----EKAAAYDKLEKTKNRLQQELDDLLV---DLDHQRQLVSN- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 441 aedLQKAQSTIRQLQEQQENprLTEDFVAHLETELEQSRLRETETLG---ALREMQDKVLDMEKRNSSLPDE-------- 509
Cdd:pfam01576 599 ---LEKKQKKFDQMLAEEKA--ISARYAEERDRAEAEAREKETRALSlarALEEALEAKEELERTNKQLRAEmedlvssk 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 510 ----NNVARLQEELKALKvregeavASARELKLQLQELSDTWQAH----------------------LSRGGRWKESPRK 563
Cdd:pfam01576 674 ddvgKNVHELERSKRALE-------QQVEEMKTQLEELEDELQATedaklrlevnmqalkaqferdlQARDEQGEEKRRQ 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 564 LV--LGELQDELMTVRLREAQALADGREWRQRVVELETQdnIHRNLLNRVEAERaalqeKLQYLAAQNKGLQTQLSESRR 641
Cdd:pfam01576 747 LVkqVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ--IDAANKGREEAVK-----QLKKLQAQMKDLQRELEEARA 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 642 KQAEAECKSKEEVMAVRLREADSMA-----AVAEMRQRIAELEiqREEgrIQGQLNHSDSSQYI-----RELKDQIEELK 711
Cdd:pfam01576 820 SRDEILAQSKESEKKLKNLEAELLQlqedlAASERARRQAQQE--RDE--LADEIASGASGKSAlqdekRRLEARIAQLE 895
|
..
gi 1583180519 712 TE 713
Cdd:pfam01576 896 EE 897
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-661 |
5.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 348 LKAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYviK 427
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--K 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 428 RELAVVRQQCSSTAEDLQKAQSTIRQLQEQQEN--------PRL-----TEDFVAHLETELEQSRLRETE--------TL 486
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkeSELiklkeLAEQLKELEEKLKKYNLEELEkkaeeyekLK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 487 GALREMQDKVLDMEKRNSSLPD--------ENNVARLQEELKALKVR-EGEAVASARELKLQLQELSDTWQAHLSRGGRW 557
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEElkkklaelEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 558 KESPRKL-VLGELQDELMTVRLREAQALADGREWRQRVVELETQ--DNIHRNL----------LNRVEAERAALQEKLQY 624
Cdd:PRK03918 612 KELEREEkELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELreeylelsreLAGLRAELEELEKRREE 691
|
330 340 350
....*....|....*....|....*....|....*....
gi 1583180519 625 LAAQNKGLQTQLSEsrRKQAEAECKSKEEVMA--VRLRE 661
Cdd:PRK03918 692 IKKTLEKLKEELEE--REKAKKELEKLEKALErvEELRE 728
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
480-719 |
5.69e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 480 LRETETLGALREMQDKVLDMEKRNSSLPDEnnVARLQEELKALKVREGEAVASARELKLQLQELSdtwQAHLSRGGRWKE 559
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSE--LRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 560 SPRKLvlGELQDELMTVRlREAQALAdgrewrQRVVELETQDNIHRNLLNRVEAERAalQEKLQYLAAQNKGLQTQLSES 639
Cdd:TIGR02169 742 LEEDL--SSLEQEIENVK-SELKELE------ARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 640 RRKQAEAECKSKEEvmavRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDssqyIRELKDQIEELKTEVRLLKG 719
Cdd:TIGR02169 811 EARLREIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLES 882
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
427-599 |
6.47e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 427 KRELAVVRQQCSSTAEDLQKAQSTIRQLqeqqenprltEDFVAHLETELEQSRLrETETLGALREMQDKVLDMekrnssL 506
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKL----------ESSIKQVEEELEELKE-QNEELEKQYKVKKKTLDL------L 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 507 PD-ENNVARLQEELKALKVRegeavasarelklqLQELSDTWQAH----------LSRGGRWKESPRKLVLGELQDelMT 575
Cdd:pfam05667 397 PDaEENIAKLQALVDASAQR--------------LVELAGQWEKHrvplieeyraLKEAKSNKEDESQRKLEEIKE--LR 460
|
170 180
....*....|....*....|....*.
gi 1583180519 576 VRLREAQALADGRE--WRQRVVELET 599
Cdd:pfam05667 461 EKIKEVAEEAKQKEelYKQLVAEYER 486
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
358-459 |
7.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSK-EMEEQIEIKRL---RTENRLlKQRIETLEKESAALADRliqgqvtraqeaeenyviKRELAVV 433
Cdd:PRK12704 55 KKEALLEAKEEIHKLRnEFEKELRERRNelqKLEKRL-LQKEENLDRKLELLEKR------------------EEELEKK 115
|
90 100
....*....|....*....|....*.
gi 1583180519 434 RQQCSSTAEDLQKAQSTIRQLQEQQE 459
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQL 141
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-713 |
8.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKesaaladrliqgqvtRAQEAEEnyvIKRELAVVRQQC 437
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE---------------LKEEIEE---LEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 438 SSTAEDLQKAQSTIRQLQEQQENprlTEDFVAHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQE 517
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL--EEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 518 ELKALKVREGEavasARELKLQLQELSDtwqahlsrggrwkespRKLVLGELQDELMTVRLREAQAladgREWRQRVVEL 597
Cdd:PRK03918 329 RIKELEEKEER----LEELKKKLKELEK----------------RLEELEERHELYEEAKAKKEEL----ERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 598 ETQDNIhrNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRR-----KQAEAEC---------KSKEEVMAVRLREad 663
Cdd:PRK03918 385 TPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCpvcgrelteEHRKELLEEYTAE-- 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1583180519 664 sMAAVAEMRQRIAELE--IQREEGRIQGQLNHSDSSQYIRELKDQIEELKTE 713
Cdd:PRK03918 461 -LKRIEKELKEIEEKErkLRKELRELEKVLKKESELIKLKELAEQLKELEEK 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
358-545 |
8.19e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 358 KKMKRLEKEyaamksKEMEEQiEIKRLRTENRLLKQRIETLEKESAALA------DRLIQGQVTRAQEAEENY-VIKREL 430
Cdd:TIGR04523 412 EQIKKLQQE------KELLEK-EIERLKETIIKNNSEIKDLTNQDSVKEliiknlDNTRESLETQLKVLSRSInKIKQNL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583180519 431 AVVRQQCSSTAEDLQKAQSTIRQLQEQQENprLTEDfVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEN 510
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKD--LTKK-ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
170 180 190
....*....|....*....|....*....|....*
gi 1583180519 511 NVARLQEELKALKVREGEAVASARELKLQLQELSD 545
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| |
