|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
113-320 |
8.94e-72 |
|
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: 234.12 E-value: 8.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 113 VRRGIPHHFRAIVWQQLSGASD----GDKKQYAEYIKATSACEKV----IRRDIARTYPEVEFFKEKDGPGQEALFNVIK 184
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPmdtsADKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 185 AYSLHDREVGYCQGSGFIVGLLLMQMP-EEEAFAVLVQIMQQHRMRhMFKPSMSELGLCMYQLENLVQEQIPDMHIHFQQ 263
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 281360709 264 QGFQTTMYASSWFLTLYTTTLNVNLSCRIMDVFLSEGMEFIFKVALALLLTGKDTLL 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 ... |
154-320 |
3.09e-53 |
|
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: 182.45 E-value: 3.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 154 IRRDIARTYPEVEFFKekDGPGQEALFNVIKAYSLHDREVGYCQGSGFIVGLLLMQ-MPEEEAFAVLVQIMQQHRMRHMF 232
Cdd:pfam00566 12 IEKDVPRTFPHSFFFD--NGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRDFY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 233 KPSMSELGLCMYQLENLVQEQIPDMHIHFQQQGFQTTMYASSWFLTLYTTTLNVNLSCRIMDVFLSEGMEF-IFKVALAL 311
Cdd:pfam00566 90 TPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAI 169
|
....*....
gi 281360709 312 LLTGKDTLL 320
Cdd:pfam00566 170 LKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
109-328 |
4.74e-42 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 160.74 E-value: 4.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 109 VSELVRRGIPHHFRAIVWQQLSGASDGDKKQ----------YAEYIKATSACEKVIRRDIARTYPEVEFFKEKDGPGQEA 178
Cdd:COG5210 205 LRELIRKGIPNELRGDVWEFLLGIGFDLDKNpglyerllnlHREAKIPTQEIISQIEKDLSRTFPDNSLFQTEISIRAEN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 179 LFNVIKAYSLHDREVGYCQGSGFIVGLLLMQMPEEE-AFAVLVQIMQQHRMRHMFKPSMSELGLCMYQLENLVQEQIPDM 257
Cdd:COG5210 285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281360709 258 HIHFQQQGFQTTMYASSWFLTLYTTTLNVNLSCRIMDVFLSEGMEFIFKVALALLLTGKDTLLCLDMEAML 328
Cdd:COG5210 365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELL 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-755 |
5.14e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKE------YQDLKKKEQEEMAELRRLRRENC-----LLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAI 426
Cdd:COG1196 200 RQLEPLERQaekaerYRELKEELKELEAELLLLKLRELeaeleELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 427 QTELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQ 506
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 507 IRNLKAKVEELEEDKktlrettpdnsvAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNA 586
Cdd:COG1196 360 LAEAEEALLEAEAEL------------AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 587 vdstpkklltnffdsskssEHTQKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEM 666
Cdd:COG1196 428 -------------------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 667 AVTREKDMSNKAREQQHRYSDLESRMKdelmnvKIKFTEQSQTVAELKQEISRLETKNSEMLAEGELRANLDDSDKVRDL 746
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALL------LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
....*....
gi 281360709 747 QDRLADMKA 755
Cdd:COG1196 563 IEYLKAAKA 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-763 |
2.61e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 435 RSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVS----CLLEELVKVRQGLAESEDQIRNL 510
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeieQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 511 KAKVEELEEDKKTLRETTPDNsvahlqdELIASKLREAEASLSLKDLKQRVQELSSQWQRQlaENQRSESERTTNAVDST 590
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEEL-------EEDLHKLEEALNDLEARLSHSRIPEIQAELSKL--EEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 591 PKKLLTNFFDSSKSSEHTQKL-------------EEELMTTRIREMETltELKELRLKVMELETQ-------VQVSTNQL 650
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQridlkeqiksiekEIENLNGKKEELEE--ELEELEAALRDLESRlgdlkkeRDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 651 RRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQS--QTVAELKQEISRLETKNseML 728
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqAELQRVEEEIRALEPVN--ML 976
|
330 340 350
....*....|....*....|....*....|....*
gi 281360709 729 AEGELRANLDDSDkvrDLQDRLADMKAELTALKSR 763
Cdd:TIGR02169 977 AIQEYEEVLKRLD---ELKEKRAKLEEERKAILER 1008
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-665 |
7.60e-11 |
|
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: 65.85 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKkkeqeemAELRRLRREncLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSY 437
Cdd:TIGR02168 206 ERQAEKAERYKELK-------AELRELELA--LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 LEVS-------HQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNL 510
Cdd:TIGR02168 277 SELEeeieelqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 511 KAKVEELEEDKKTLRettpdNSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAvdst 590
Cdd:TIGR02168 357 EAELEELEAELEELE-----SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---- 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281360709 591 PKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELE 665
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
379-719 |
1.46e-10 |
|
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: 65.08 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 379 AELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLSLRL 458
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 459 QENNNSRQSSIDELCMKEEALKQrdemvscLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRE--TTPDNSVAHL 536
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAE-------AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 537 QDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERttnavdstpkKLLTNFFDSSKSSEHTQKLEEELM 616
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----------EALLNERASLEEALALLRSELEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 617 TTRIREMET-----LTELKELRLKVMELETQVQVSTNQLRRQDEehkKLKEE----LEMAVTREKDMSNKAREQQHRYSD 687
Cdd:TIGR02168 900 SEELRELESkrselRRELEELREKLAQLELRLEGLEVRIDNLQE---RLSEEysltLEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350
....*....|....*....|....*....|..
gi 281360709 688 LEsRMKDELMNVKIKFTEQSQTVAELKQEISR 719
Cdd:TIGR02168 977 LE-NKIKELGPVNLAAIEEYEELKERYDFLTA 1007
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
338-780 |
1.34e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 338 RVEADVEGFFNLAYSIKLNTKRMKKMEKEYQDLKKKEQEemaelrrLRRENCLLKQRNELLEaESAELADRLVRgqVSRA 417
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE-------LEKRLEELEERHELYE-EAKAKKEELER--LKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 418 EEEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLSLRLQEnnnsRQSSIDEL---------CMKEEALKQRDEMVSC 488
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKKAIEELkkakgkcpvCGRELTEEHRKELLEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 489 LLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTPDNSVA----HLQDELIASKLREAEA-SLSLKDLKQRVQE 563
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkELEEKLKKYNLEELEKkAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 564 LSSQWQRQLAENQR-----SESERTTNAVDSTPKKLltnffdssksSEHTQKLEEELMTTRIREMETLTELKELRLKVME 638
Cdd:PRK03918 537 LKGEIKSLKKELEKleelkKKLAELEKKLDELEEEL----------AELLKELEELGFESVEELEERLKELEPFYNEYLE 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 639 LETQVQvstnQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRM-KDELMNVKIKFTEQSQTVAELKQEI 717
Cdd:PRK03918 607 LKDAEK----ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAEL 682
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360709 718 SRLETKNSEMLAEGE-LRANLDDSDKVRDLQDRLADMKAELTALKSRGKFPGAKLRSSSIQSIE 780
Cdd:PRK03918 683 EELEKRREEIKKTLEkLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
363-642 |
2.29e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 363 MEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYLEVSH 442
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 443 QLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKK 522
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 523 TLRETTPDNSVAHLQDELIASKLREA--EASLSLKDLKQRVQELSSQWQrQLAENQRSESERTTNAVDSTPKKLLtnfFD 600
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRREleELREKLAQLELRLEGLEVRID-NLQERLSEEYSLTLEEAEALENKIE---DD 966
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 281360709 601 SSKSSEHTQKLEEELmtTRIRE--METLTELKELRLKVMELETQ 642
Cdd:TIGR02168 967 EEEARRRLKRLENKI--KELGPvnLAAIEEYEELKERYDFLTAQ 1008
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-737 |
5.75e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRsy 437
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK-- 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 levSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEalKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEEL 517
Cdd:PTZ00121 1554 ---AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 518 EEDKKTLRETTPDNSvahlQDELIASKLREAEASLSLK--DLKQRVQElssqwQRQLAENQRSESERTTNAVDSTPKKLl 595
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEA----EEKKKAEELKKAEEENKIKaaEEAKKAEE-----DKKKAEEAKKAEEDEKKAAEALKKEA- 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 596 tnffDSSKSSEHTQKLEEElmttRIREMETLTELKELRlkvmeletqvQVSTNQLRRQDEEHKKLKEELEMAVTREKDMS 675
Cdd:PTZ00121 1699 ----EEAKKAEELKKKEAE----EKKKAEELKKAEEEN----------KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281360709 676 NKAREQQHRysdLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAEGELRANL 737
Cdd:PTZ00121 1761 HLKKEEEKK---AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNL 1819
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
379-763 |
9.88e-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: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 379 AELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEEtsyaiqtelmqlrrsYLEVSHQLENAneEVRGLSLRL 458
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER---------------YQALLKEKREY--EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 459 QENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAkvEELEEDKKTLRETTPDnsVAHLQD 538
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGELEAE--IASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 539 ELIASKLReaeaslsLKDLKQRVQELSSQWQRQLAEnqrseserttnavdstpkklltnffdsskssehTQKLEEELMTT 618
Cdd:TIGR02169 309 SIAEKERE-------LEDAEERLAKLEAEIDKLLAE---------------------------------IEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 619 RIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMaVTREKDMSNKAR-----EQQHRYSDLEsRMK 693
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK-LKREINELKRELdrlqeELQRLSEELA-DLN 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281360709 694 DELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLA--EGELRANLDDSDKVRDLQDRLADMKAELTALKSR 763
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
359-700 |
1.67e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 359 RMKKMEKEYQDLKKKEQEEMAELRRLRRENCllkqRNELLEAESAElaDRLVRGQVSRAEEEETSYAIQTELMQLRRSYL 438
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELK----LQELKLKEQAK--KALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 439 EVSHQLENANEEVRGLSLRLQENNNS---RQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVE 515
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEklaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 516 ELEEDKKTLRETTPDNSVAHLQDELIASKLREAEASLSLKDLKQRvQELSSQWQRQLAENQRSESERTTNAVDSTPKKLL 595
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-QEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 596 TNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMS 675
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340
....*....|....*....|....*
gi 281360709 676 NKAREQQHRysDLESRMKDELMNVK 700
Cdd:pfam02463 479 LVKLQEQLE--LLLSRQKLEERSQK 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-763 |
2.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEaesaELADRLVRGQVSRAEEEETSYAIQTELMQLRRSY 437
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 LEVSHQLENANEEVRglslrlqennnsrqsSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEEL 517
Cdd:PRK03918 269 EELKKEIEELEEKVK---------------ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 518 EEDKKTLRETtpdnsvahlqdeliasKLREAEASLSLKDLKQRVQELssQWQRQLAENQRSESERTTNavdSTPKKLLTN 597
Cdd:PRK03918 334 EEKEERLEEL----------------KKKLKELEKRLEELEERHELY--EEAKAKKEELERLKKRLTG---LTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 598 FFDSSKSSEHTQKLEEELmTTRIREMEtlTELKELRLKVMELETQVQVSTNQLRRQDEEHKKlkeELEMAVTRE-KDMSN 676
Cdd:PRK03918 393 LEELEKAKEEIEEEISKI-TARIGELK--KEIKELKKAIEELKKAKGKCPVCGRELTEEHRK---ELLEEYTAElKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 677 KAREQQHRYSDLESRMK--DELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAEgelranldDSDKVRDLQDRLADMK 754
Cdd:PRK03918 467 ELKEIEEKERKLRKELRelEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK--------KAEEYEKLKEKLIKLK 538
|
....*....
gi 281360709 755 AELTALKSR 763
Cdd:PRK03918 539 GEIKSLKKE 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
364-763 |
2.76e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 364 EKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRlvRGQVSRAEEEetsyaIQTELMQLRRSYLEVSHQ 443
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR--REELEDRDEE-----LRDRLEECRVAAQAHNEE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 444 LENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKT 523
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 524 LREttpdnsvahlqdeliasklREAEASLSLKDLKQRVQELssqwQRQLAENQRSESERttnavdstpkklltnffdSSK 603
Cdd:PRK02224 424 LRE-------------------REAELEATLRTARERVEEA----EALLEAGKCPECGQ------------------PVE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 604 SSEHTQKLEEElmttRIREMETLTELKELRLKVMELETQVQvSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQH 683
Cdd:PRK02224 463 GSPHVETIEED----RERVEELEAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 684 RYSDLESRMKD---ELMNVKIKFTEQSQTVAELKQEISRLETKnsemlaEGELRANLDDSDKVRDLQDRLADMKAELTAL 760
Cdd:PRK02224 538 RAEELRERAAEleaEAEEKREAAAEAEEEAEEAREEVAELNSK------LAELKERIESLERIRTLLAAIADAEDEIERL 611
|
...
gi 281360709 761 KSR 763
Cdd:PRK02224 612 REK 614
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-763 |
3.49e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSY 437
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 LEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAK---- 513
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 514 VEELEEDKKTLRETTPDNSVAHLQDE---LIASKLREAEASLSLKDL----KQRVQELSSQWQRQLAENQRSESERTTNA 586
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAavdLVASDLREADARYYVLGDtllgRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 587 VDSTPKKLLTNFFDSSKSSEHTQKLEEELmttRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEM 666
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELE---ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 667 AVTREKdmsnkAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNseMLAEGELRAnldDSDKVRDL 746
Cdd:COG1196 731 EAEREE-----LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN--LLAIEEYEE---LEERYDFL 800
|
410
....*....|....*..
gi 281360709 747 QDRLADMKAELTALKSR 763
Cdd:COG1196 801 SEQREDLEEARETLEEA 817
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-694 |
4.39e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 353 IKLNTKRMKKMEKEYQDLKK------KEQEEM--------AELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAE 418
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKalaelrKELEELeeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 419 EEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNnsrqSSIDELcmkEEALKQRDEMVSCLLEELVKVRQ 498
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDEL---RAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 499 GLAESEDQIRNLKAKVEELEEDkktlrettpdnsVAHLQDELIASKLREAEASLSLKDLKQRVQelSSQWQRQLAENQRS 578
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSED------------IESLAAEIEELEELIEELESELEALLNERA--SLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 579 ESERTTNAVDSTPKKLLTnffDSSKSSEHTQKLEEELMTTRIREMETLTELKEL-RLKVMELETQVQVSTNQLRRQDEEH 657
Cdd:TIGR02168 898 ELSEELRELESKRSELRR---ELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 281360709 658 KKLKEELE------MAVTREkdmsnkAREQQHRYSDLESRMKD 694
Cdd:TIGR02168 975 KRLENKIKelgpvnLAAIEE------YEELKERYDFLTAQKED 1011
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
491-751 |
8.04e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 491 EELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLrettpDNSVAHLQDELIASKLREAEASLSLKDLKQRVQELssqwQR 570
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALARRIRALEQELAALEAELAELEKEIAEL----RA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 571 QLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHtqkleeelmttrIREMETLTELKELRLKVMEletqvqvstnQL 650
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA------------VRRLQYLKYLAPARREQAE----------EL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 651 RRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAE 730
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|.
gi 281360709 731 GELRANLDDSDKVRDLQDRLA 751
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKLP 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
356-577 |
1.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 356 NTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRR 435
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 436 SYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELcmkEEALKQRDEmvscLLEELVKVRQGLAESEDQIRNLKAKVE 515
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL---AELEEEEEE----EEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281360709 516 ELEEDKKTLREttpdnsvahLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQR 577
Cdd:COG1196 467 ELLEEAALLEA---------ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
357-566 |
1.28e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 357 TKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRS 436
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 437 YLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELV-----KVRQGLAESEDQIRNLK 511
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQ 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 281360709 512 AKVEELEEDKKTLREttpdnSVAHLQDELIASKLREAEASLSLKDLKQRVQELSS 566
Cdd:TIGR02168 454 EELERLEEALEELRE-----ELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-594 |
1.56e-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: 54.38 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQL---- 433
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 434 ----RRSYLEVSHQLENANEEVRGLSLrLQENNNSRQSSIDELCMKEEALKQrdemvscLLEELVKVRQGLAESEDQIRN 509
Cdd:COG4942 114 yrlgRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAA-------LRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 510 LKAKVEELEEDKKTLRETtpdnsvahlqdelIASKLREAEAslSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDS 589
Cdd:COG4942 186 ERAALEALKAERQKLLAR-------------LEKELAELAA--ELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 281360709 590 TPKKL 594
Cdd:COG4942 251 LKGKL 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-532 |
2.26e-07 |
|
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: 54.69 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 359 RMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYL 438
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 439 EVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELE 518
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
170
....*....|....
gi 281360709 519 EDKKTLRETTPDNS 532
Cdd:TIGR02169 497 AQARASEERVRGGR 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
494-763 |
2.60e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 494 VKVRQGLAESEDQIRNLKAKVEELEED-------KKTLRETTPD--NSVAHLQDELIASKLREAEASLSLKDLKQRVQEL 564
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKiaelekaLAELRKELEEleEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 565 SSQWQRQLAENQRSESERTTNAVDstpkklLTNFFDSSKSSEHTQKLEEELMTTRIREMETLTE-LKELRLKVMELETQV 643
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEER------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREaLDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 644 QVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLE---SRMKDELMNVKIKFTEQSQTVAELKQEISRL 720
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELESELEALLNERASLEEALALLRSELEEL 899
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 281360709 721 ETKNSEMlaEGELRANLDDSDKvrdLQDRLADMKAELTALKSR 763
Cdd:TIGR02168 900 SEELREL--ESKRSELRRELEE---LREKLAQLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
357-574 |
2.65e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 357 TKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRS 436
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 437 YLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEE 516
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 281360709 517 LEEDKKTLRETTpdnsvAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAE 574
Cdd:COG1196 440 EEEALEEAAEEE-----AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
391-577 |
3.16e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 391 LKQRNELLEAESAELADRL--VRGQVSRAEEEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSS 468
Cdd:COG3206 166 LELRREEARKALEFLEEQLpeLRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 469 IDELCMKEEALKQ--RDEMVSCLLEELVKVRQGLAE-----SED--QIRNLKAKVEELEEDKKTLRETTpdnsVAHLQDE 539
Cdd:COG3206 246 RAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAElsaryTPNhpDVIALRAQIAALRAQLQQEAQRI----LASLEAE 321
|
170 180 190
....*....|....*....|....*....|....*...
gi 281360709 540 LIASKLREAEASLSLKDLKQRVQELSSQwQRQLAENQR 577
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPEL-EAELRRLER 358
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
358-721 |
9.03e-07 |
|
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: 52.43 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAelrrlrREnclLKQRNELLEAESAELADrlvrgqvsrAEEEETSYAIQTELMQLRRSY 437
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKA------RE---VERRRKLEEAEKARQAE---------MDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 LEVSHQLEnaneevrglslRLQENNNSRQssiDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEdqirnlKAKVEEL 517
Cdd:pfam17380 350 LERIRQEE-----------RKRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVRQELEAAR------KVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 518 EEDKKTLRETTPDNSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKklltn 597
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR----- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 598 ffDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMElETQVQVSTNQLRRQDEEHKKLKEELEmavtREKDMSNK 677
Cdd:pfam17380 485 --DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEME-ERQKAIYEEERRREAEEERRKQQEME----ERRRIQEQ 557
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 281360709 678 AREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLE 721
Cdd:pfam17380 558 MRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-763 |
1.21e-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: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 489 LLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLREttpdnSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQW 568
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRL-----ELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 569 QRQLAENQRSESERTTNAvdstpkklltnfFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTN 648
Cdd:COG1196 312 RELEERLEELEEELAELE------------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 649 QLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSEml 728
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE-- 457
|
250 260 270
....*....|....*....|....*....|....*
gi 281360709 729 AEGELRANLDDSDKVRDLQDRLADMKAELTALKSR 763
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
354-760 |
1.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 354 KLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRenclLKQRNELLEAESAELADRLvrgqvSRAEEEETSYAIQTELMQL 433
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREEL-----EKLEKLLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 434 RRSYLEVSHQLENANEEVRGLSlRLQENNNSRQSSIDEL------CMKEEALKQRDEMVScLLEELVKVRQGLAESEDQI 507
Cdd:COG4717 138 EAELAELPERLEELEERLEELR-ELEEELEELEAELAELqeeleeLLEQLSLATEEELQD-LAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 508 RNLKAKVEELEEDKKTLRETTPDNSVAHLQDELIASKLREAE------ASLSLKDLKQRVQEL------------SSQWQ 569
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllallgLGGSLLSLILTIAGVlflvlgllallfLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 570 RQLAENQRSESERTTNAVDSTPKKLLTNFFDSskssehtQKLEEELMTTRIRE-METLTELKELRLKVMELETQVQVSTN 648
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAA-------LGLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 649 QLRRQ---DEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQ-SQTVAELKQEISRLETKN 724
Cdd:COG4717 369 EQEIAallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEEL 448
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 281360709 725 SEMLAE-GELRA---NLDDSDKVRDLQDRLADMKAELTAL 760
Cdd:COG4717 449 EELREElAELEAeleQLEEDGELAELLQELEELKAELREL 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
357-757 |
2.49e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 357 TKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRS 436
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 437 YLEVSHQLENA---NEEVRGLSLRLQENNNSRQSSIDEL------------------CMKE-------EALKQRDEMVSC 488
Cdd:PRK02224 400 FGDAPVDLGNAedfLEELREERDELREREAELEATLRTArerveeaealleagkcpeCGQPvegsphvETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 489 LLEElvkvrqgLAESEDQIRNLKAKVEELEEDKKTLRETTPDNSVAHLQDELIASKLREAEA-SLSLKDLKQRVQELSS- 566
Cdd:PRK02224 480 LEAE-------LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkRERAEELRERAAELEAe 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 567 -QWQRQLAENQRSESERTTNAVDSTPKKLLTNffdssksSEHTQKLE--EELMTTRIREMETLTELKELRLKVMELETQv 643
Cdd:PRK02224 553 aEEKREAAAEAEEEAEEAREEVAELNSKLAEL-------KERIESLEriRTLLAAIADAEDEIERLREKREALAELNDE- 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 644 qvSTNQLRRQDEEHKKLKEELEMAVTREkdmsnkAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETK 723
Cdd:PRK02224 625 --RRERLAEKRERKRELEAEFDEARIEE------AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
410 420 430
....*....|....*....|....*....|....*
gi 281360709 724 NSEMLAEGELRANLDD-SDKVRDLQDRLADMKAEL 757
Cdd:PRK02224 697 RERREALENRVEALEAlYDEAEELESMYGDLRAEL 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
362-757 |
2.77e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 362 KMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELL---EAESAELADRLVRGQVSRAEE----EETSYAIQTELM-QL 433
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrDTGNSITIDHLRRELDDRNMEvqrlEALLKAMKSECQgQM 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 434 RRSYLEVSHQLENAnEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAK 513
Cdd:pfam15921 447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 514 VEELEEDKKTLRetTPDNSVAHLQDELIASKLREAEASLSLKDLKQRVQ---ELSSQWQRQ----LAENQRSESERTTNA 586
Cdd:pfam15921 526 VDLKLQELQHLK--NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtQLVGQHGRTagamQVEKAQLEKEINDRR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 587 VDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREM--ETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLK--- 661
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAgsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnf 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 662 ----EELEMAVTREK-DMSNKAREQQHRYSDLES----------------------RMKDELMNVKIKFTEQSQTVA--- 711
Cdd:pfam15921 684 rnksEEMETTTNKLKmQLKSAQSELEQTRNTLKSmegsdghamkvamgmqkqitakRGQIDALQSKIQFLEEAMTNAnke 763
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 281360709 712 ---------ELKQEISRLETKNSEMLAEGELRANLDdsdkvRDLQDRLADMKAEL 757
Cdd:pfam15921 764 khflkeeknKLSQELSTVATEKNKMAGELEVLRSQE-----RRLKEKVANMEVAL 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
355-583 |
3.24e-06 |
|
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: 50.84 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 355 LNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELadrlvrgQVSRAEEEETSYAIQTELMQLR 434
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL-------EAEIDKLLAEIEELEREIEEER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 435 RSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKV 514
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281360709 515 EELEEDKKTLRETTPDNSVAHLQDELIASKLRE--AEASLSLKDLKQRVQELS---SQWQRQL--AENQRSESERT 583
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlSKYEQELYDLKEEYDRVEkelSKLQRELaeAEAQARASEER 505
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-726 |
4.65e-06 |
|
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: 50.36 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 354 KLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQV-SRAEEEETSYAIQTELMQ 432
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKeQREKEELKKLKLEAEELL 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 433 LRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKvrqglAESEDQIRNLKA 512
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL-----KVEEEKEEKLKA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 513 KVEELEEDKKTLRETtpdnsvAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPK 592
Cdd:pfam02463 799 QEEELRALEEELKEE------AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 593 KLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMavtrEK 672
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD----EK 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 281360709 673 DMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSE 726
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-762 |
7.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 401 ESAELADRLVRgQVSRAEEEETSY----AIQTELMQLRRSYLEVSHQLENANEEVRGLSLRLQEnnnsRQSSIDELCMKE 476
Cdd:PRK03918 142 ESDESREKVVR-QILGLDDYENAYknlgEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEE----VLREINEISSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 477 EALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLREttpdnsvahlqdeliasklREAEASLSLKD 556
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-------------------RIEELKKEIEE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 557 LKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNFfdSSKSSEHTQKLEE-ELMTTRIREMEtlTELKELRLK 635
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL--EEEINGIEERIKElEEKEERLEELK--KKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 636 VMELET---------QVQVSTNQL--RRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKD------ELMN 698
Cdd:PRK03918 354 LEELEErhelyeeakAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieELKK 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360709 699 VKIK-------FTEQ--SQTVAELKQEISRLETKNSEML-AEGELRANLDDSDKVRDLQDRLADMKAELTALKS 762
Cdd:PRK03918 434 AKGKcpvcgreLTEEhrKELLEEYTAELKRIEKELKEIEeKERKLRKELRELEKVLKKESELIKLKELAEQLKE 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
475-799 |
1.20e-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: 48.90 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 475 KEEALKQRDEMvsclLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKtlrettpdnsvahLQDELiasklREAEASLSL 554
Cdd:TIGR02168 174 RKETERKLERT----RENLDRLEDILNELERQLKSLERQAEKAERYKE-------------LKAEL-----RELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 555 KDLKQRVQELSsQWQRQLAENQRSESERTTNAVdstpkklltnffdsskssehtqkleeelmttriremETLTELKELRL 634
Cdd:TIGR02168 232 LRLEELREELE-ELQEELKEAEEELEELTAELQ------------------------------------ELEEKLEELRL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 635 KVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESR---MKDELMNVKIKFTEQSQTVA 711
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 712 ELKQEISRLETKNSEM-LAEGELRANLDD-SDKVRDLQDRLADMKAELTALKSRGKFPGAKL-RSSSIQSIESTEIDFND 788
Cdd:TIGR02168 355 SLEAELEELEAELEELeSRLEELEEQLETlRSKVAQLELQIASLNNEIERLEARLERLEDRReRLQQEIEELLKKLEEAE 434
|
330
....*....|.
gi 281360709 789 LNMVRRGSTEL 799
Cdd:TIGR02168 435 LKELQAELEEL 445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-763 |
1.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 361 KKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLE--AESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYL 438
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 439 EV-SHQLENANEEVRGLSlRLQENNNSRQSSIDELCMKEEALKQRDEMVScLLEELVKVRQGLAESEDqirnlKAKVEEL 517
Cdd:PTZ00121 1377 KKkADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEE-----AKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 518 E---EDKKTLRETTPDNSVAHLQDELiaskLREAEASLSLKDLKQRVQElssqwQRQLAENQRSESERTTNAvDSTPKKL 594
Cdd:PTZ00121 1450 KkkaEEAKKAEEAKKKAEEAKKADEA----KKKAEEAKKADEAKKKAEE-----AKKKADEAKKAAEAKKKA-DEAKKAE 1519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 595 LTNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELR-----LKVMELETQVQVSTNQLRRQDE----EHKKLKEELE 665
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaeekKKAEEAKKAEEDKNMALRKAEEakkaEEARIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 666 MAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAEGELRANLDDSDKVRD 745
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
410
....*....|....*...
gi 281360709 746 LQDRLADMKAELTALKSR 763
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKE 1697
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
365-763 |
1.63e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 365 KEYQDLKKKEQEEMAELRRLRRENclLKQRNELLEAESAELADRLVR--GQVSRAEEEETsyAIQTELMQLRRSYLEVSH 442
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARleAELERLEARLD--ALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 443 Q-LENANEEVRGLSLRLQENNNSRQ--------------SSIDELcmkEEALKQRDEMVSCLLEELVKVRQGLAESEDQI 507
Cdd:COG4913 338 DrLEQLEREIERLERELEERERRRArleallaalglplpASAEEF---AALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 508 RNLKAKVEELEEDKKTLReTTPDNSVAHLQD--ELIASKLREAEASLS-LKDLKQrVQELSSQWQ--------------- 569
Cdd:COG4913 415 RDLRRELRELEAEIASLE-RRKSNIPARLLAlrDALAEALGLDEAELPfVGELIE-VRPEEERWRgaiervlggfaltll 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 570 ---RQLAE-----NQRSESER-TTNAVDSTPKKLLTNFFD--------SSKSSEHTQKLEEELMTTRIRE-METLTELKE 631
Cdd:COG4913 493 vppEHYAAalrwvNRLHLRGRlVYERVRTGLPDPERPRLDpdslagklDFKPHPFRAWLEAELGRRFDYVcVDSPEELRR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 632 LRLKVMEletQVQVSTNQLRRQ------------------------DEEHKKLKEELEMAVTREKDMSNK---AREQQHR 684
Cdd:COG4913 573 HPRAITR---AGQVKGNGTRHEkddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEALEAEldaLQERREA 649
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360709 685 YSDLEsrmkdelmnvkiKFTEQSQTVAELKQEISRLETknsemlaegELRANLDDSDKVRDLQDRLADMKAELTALKSR 763
Cdd:COG4913 650 LQRLA------------EYSWDEIDVASAEREIAELEA---------ELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
364-729 |
2.75e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 364 EKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEetsyaiqtelmqlrrsylevshQ 443
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQE----------------------K 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 444 LENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKK- 522
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQl 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 523 -TLRETTPDNsVAHLQDELIAsklREAEASLSLKDLKQRVqelssqwqrQLAENQRSESERTTNAVDStpkklLTNFFDS 601
Cdd:PRK04863 430 cGLPDLTADN-AEDWLEEFQA---KEQEATEELLSLEQKL---------SVAQAAHSQFEQAYQLVRK-----IAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 602 SKSSEHTQKLEEELMTTRIRemetLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEmavtREKDMSNKAREQ 681
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHL----AEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD----DEDELEQLQEEL 563
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 281360709 682 QHRYSDLEsrmkDELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLA 729
Cdd:PRK04863 564 EARLESLS----ESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA 607
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
466-757 |
2.80e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 466 QSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTPD--NSVAHLQDElIAS 543
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDlrERLEELEEE-RDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 544 KLREAE-ASLSLKDLKQRVQELSSQWQ--RQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRI 620
Cdd:PRK02224 298 LLAEAGlDDADAEAVEARREELEDRDEelRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 621 REMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLE----------- 689
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpec 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281360709 690 ------SRMKDELMNVKIKFTEQSQTVAELKQEISRLETK--NSEMLAEGELRANlDDSDKVRDLQDRLADMKAEL 757
Cdd:PRK02224 458 gqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERleRAEDLVEAEDRIE-RLEERREDLEELIAERRETI 532
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
349-775 |
3.88e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 349 LAYSIKLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVS----RAEEEETSY 424
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnlQNITVRLQD 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 425 AIQTELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVScllEELVKVRQGLAESE 504
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR---EHALSIRVLPKELL 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 505 DQIRNLKAKVEELEEDKKTLRETTPDnsvahlqdelIASKLREAEASLslKDLKQRVQELSsqwqrQLAENQRSESERTT 584
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQ----------CQTLLRELETHI--EEYDREFNEIE-----NASSSLGSDLAARE 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 585 NAVDSTPKKLLTNFFDSSKSS--EHTQKLEEELMttrirEMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKE 662
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARteAHFNNNEEVTA-----ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 663 ELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAEGELRaNLDDSDK 742
Cdd:TIGR00618 814 SDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIK-IQFDGDA 892
|
410 420 430
....*....|....*....|....*....|...
gi 281360709 743 VRDLQDRLADMKAELTALKSRGKFPGAKLRSSS 775
Cdd:TIGR00618 893 LIKFLHEITLYANVRLANQSEGRFHGRYADSHV 925
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
466-675 |
4.01e-05 |
|
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: 46.94 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 466 QSSIDELCMKEEALKqrdemvscllEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRET-----TPDNSVAHLQDEL 540
Cdd:pfam05667 341 QEQLEDLESSIQELE----------KEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTldllpDAEENIAKLQALV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 541 IASKlreaeaslslkdlkQRVQELSSQW---QRQLAENQRSESERTTNavdstpkklltnffdssKSSEHTQKLEeelmt 617
Cdd:pfam05667 411 DASA--------------QRLVELAGQWekhRVPLIEEYRALKEAKSN-----------------KEDESQRKLE----- 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 281360709 618 triremetltELKELRlkvmeleTQVQVSTNQLRRQDEEHKKLKEELEmavTREKDMS 675
Cdd:pfam05667 455 ----------EIKELR-------EKIKEVAEEAKQKEELYKQLVAEYE---RLPKDVS 492
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
506-790 |
4.13e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 506 QIRNLKAKVEEleedKKTLRETTpDNSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSEserTTN 585
Cdd:COG5022 818 CIIKLQKTIKR----EKKLRETE-EVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQE---LKI 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 586 AVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVM-----ELETQVQVSTNQLRRQDEEHKKL 660
Cdd:COG5022 890 DVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDleegpSIEYVKLPELNKLHEVESKLKET 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 661 KEELEMAV---TREKDMSNKAREQQHRYSDLESRMKDELMnvkiKFTEQSQTVAELKQEISRLETKNSEMLAEGELRANL 737
Cdd:COG5022 970 SEEYEDLLkksTILVREGNKANSELKNFKKELAELSKQYG----ALQESTKQLKELPVEVAELQSASKIISSESTELSIL 1045
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 281360709 738 DDSDKV-RDLQDRLADMKAELTALKSRGkfPGAKLRSSSIQSIESTEIDFNDLN 790
Cdd:COG5022 1046 KPLQKLkGLLLLENNQLQARYKALKLRR--ENSLLDDKQLYQLESTENLLKTIN 1097
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
439-726 |
5.05e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 439 EVSHQLENANEEVRGLSLRLQENNNSrqssIDELcmkEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELE 518
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKI----ISQL---NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 519 EDKKTLRettpdNSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNF 598
Cdd:TIGR04523 384 QEIKNLE-----SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 599 FDSSKSSEHTQ--KLEEELMTTRiREMETLTelKELRLKVMELETQvqvsTNQLRRQDEEHKKLKEELEMAVTREKDMSN 676
Cdd:TIGR04523 459 LDNTRESLETQlkVLSRSINKIK-QNLEQKQ--KELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 281360709 677 KAREQQHRYSDLES---RMKDELMNVKIK--FTEQSQTVAELKQEISRLETKNSE 726
Cdd:TIGR04523 532 EKKEKESKISDLEDelnKDDFELKKENLEkeIDEKNKEIEELKQTQKSLKKKQEE 586
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-564 |
6.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 357 TKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLvrgqvsrAEEEETSYAIQTELMQLRRS 436
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI-------EELEEDLHKLEEALNDLEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 437 YL-----EVSHQLENANEEVRGLSLRLQE-------------------------------NNNSRQSSIDELCMKEEALK 480
Cdd:TIGR02169 788 LShsripEIQAELSKLEEEVSRIEARLREieqklnrltlekeylekeiqelqeqridlkeQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 481 QRDEMVSCLLEELVKVRQGLA----ESEDQIRNLKAKVEELEEDKKTLRETTPDNSVA--HLQDEL------IASKLREA 548
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKkerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKleALEEELseiedpKGEDEEIP 947
|
250
....*....|....*.
gi 281360709 549 EASLSLKDLKQRVQEL 564
Cdd:TIGR02169 948 EEELSLEDVQAELQRV 963
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-761 |
6.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSY 437
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 LEV--SHQLENANEEVRGLSLRLQENNNSRQSSiDELCMKEEALKQRDEMVScLLEELVKVRQGL--AESEDQIRNLKAK 513
Cdd:PTZ00121 1388 EEKkkADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKK-KAEEAKKADEAKkkAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 514 VEE---LEEDKKTLRETTPDNSVAHLQDELI--ASKLREA-EASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAV 587
Cdd:PTZ00121 1466 AEEakkADEAKKKAEEAKKADEAKKKAEEAKkkADEAKKAaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 588 ---DSTPKKLLTNFFDSSKSSEHTQKlEEELMTTRIREMETLTELKELRLK-VMELETQVQVSTNQLRRQDEEHKKLKEE 663
Cdd:PTZ00121 1546 kkaDELKKAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEeVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 664 LEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNvKIKFTEQSQTVAELKQEISRL-ETKNSEMLAEGELRANLDDSDK 742
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN-KIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKK 1703
|
410
....*....|....*....
gi 281360709 743 VRDLQDRLADMKAELTALK 761
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELK 1722
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
363-633 |
8.46e-05 |
|
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: 46.04 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 363 MEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQlrrsylevsh 442
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ---------- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 443 qlenANEEVRGLSLRLQENNNSR----------QSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKA 512
Cdd:pfam07888 183 ----TEEELRSLSKEFQELRNSLaqrdtqvlqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 513 KVEELEEDKKtlrettpdnsvaHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQ------RQLAENQRSESERTTNA 586
Cdd:pfam07888 259 ELSSMAAQRD------------RTQAELHQARLQAAQLTLQLADASLALREGRARWAqeretlQQSAEADKDRIEKLSAE 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 281360709 587 VDSTPKKLltnffdsSKSSEHTQKLEEELM----TTRIREMETLTELKELR 633
Cdd:pfam07888 327 LQRLEERL-------QEERMEREKLEVELGrekdCNRVQLSESRRELQELK 370
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
324-782 |
1.37e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 324 MEAMLKFFQKELPGRVEADVEGFFNLAYSIKLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRE-------NCLLKQRNE 396
Cdd:pfam15921 431 LEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSertvsdlTASLQEKER 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 397 LLEAESAELADRLVRGQVSRAE------EEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLS-LRLQENNNSRQSSI 469
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQElqhlknEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTqLVGQHGRTAGAMQV 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 470 DELCMKEEALKQRDEmvsclLEELVKVRQglaESEDQIRNLKAKVEELEEDKKTLrettpdnsVAHLQDELIASKLREAE 549
Cdd:pfam15921 591 EKAQLEKEINDRRLE-----LQEFKILKD---KKDAKIRELEARVSDLELEKVKL--------VNAGSERLRAVKDIKQE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 550 ASLSLKDLKQRVQELSSQWQ-----RQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREME 624
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEdyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 625 TLT----ELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRysdlESRMKDELMNVK 700
Cdd:pfam15921 735 QITakrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ----ERRLKEKVANME 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 701 IKFTEQSQTVAELKQEISRLETKNsemlaegeLRANLDDSDKVRDLQdrlADMKAELTALKSRGKFPGAKLRS-SSIQSI 779
Cdd:pfam15921 811 VALDKASLQFAECQDIIQRQEQES--------VRLKLQHTLDVKELQ---GPGYTSNSSMKPRLLQPASFTRThSNVPSS 879
|
...
gi 281360709 780 EST 782
Cdd:pfam15921 880 QST 882
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
351-763 |
1.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 351 YSIKLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTEL 430
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 431 MQLRRsyLEVSHQLENAN--------EEVR-GLSLRLQENNNSRQSS--IDELCMKEEALKQRDEMVSCLLEELVKVRQG 499
Cdd:PTZ00121 1161 EDARK--AEEARKAEDAKkaeaarkaEEVRkAEELRKAEDARKAEAArkAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 500 LAESE--DQIRNLKA--KVEELEEDKKTLRETTPDNSVAHLQDEL-------IASKLREAEASLSLKDLKQRVQEL-SSQ 567
Cdd:PTZ00121 1239 AEEAKkaEEERNNEEirKFEEARMAHFARRQAAIKAEEARKADELkkaeekkKADEAKKAEEKKKADEAKKKAEEAkKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 568 WQRQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMELEtqvqvST 647
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-----KA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 648 NQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDElmnvKIKFTEQSQTVAELKQEISRLETKNSEM 727
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
410 420 430
....*....|....*....|....*....|....*.
gi 281360709 728 LAEGELRANLDDSDKVRDLQDRLADMKAELTALKSR 763
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
354-726 |
2.35e-04 |
|
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: 44.63 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 354 KLNTKRMKKmEKEYQDLKKKEQeemaelrrlrRENCLLKQRNELlEAESAELADRLVRGQVSRAEEEETSYAIQTELMQL 433
Cdd:TIGR04523 191 KIKNKLLKL-ELLLSNLKKKIQ----------KNKSLESQISEL-KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 434 RRSYLEVSHQLENANEEVRGLSLRLQENNNSrqssIDELCMKEEALKQRDE--MVSCLLEELVKVRQGLAESEDQIRNLK 511
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQ----LNQLKSEISDLNNQKEqdWNKELKSELKNQEKKLEEIQNQISQNN 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 512 AKVEELEED----KKTLRETTPDNS-----VAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESER 582
Cdd:TIGR04523 335 KIISQLNEQisqlKKELTNSESENSekqreLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 583 TTNAVDstpKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETltELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKE 662
Cdd:TIGR04523 415 KKLQQE---KELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL--IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360709 663 ELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSE 726
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
348-765 |
2.77e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 348 NLAYSIKLNTKRMKKMEKEYQ-------DLKKKEQEEMAELRRLRRENCLLKQRnelLEAESAELaDRLVRGQVSRAEEE 420
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTE---FEATTCSL-EELLRTEQQRLEKN 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 421 ETSYAIQTELMQLRRSYLEVSHQLENANE-------EVRGLSLRLQENNNSRQSSIDELCMKEEAL----KQRDEMVSCL 489
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEveleelkKILAEDEKLLDEKKQFEKIAEELKGKEQELifllQAREKEIHDL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 490 LEELVKVRQGLAESEDQIRNLKAkveELEEDKKTLRETTPDNSVAHLQDELIASKlrEAEASLSLKDLKQRVQELSSQWQ 569
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKT---ELEKEKLKNIELTAHCDKLLLENKELTQE--ASDMTLELKKHQEDIINCKKQEE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 570 RQLA--ENQRSESERTTNAVDSTPKKLLtnffdsSKSSEHTQKLEEELMTTRIREMETLTELKELRLkvmeletqVQVST 647
Cdd:pfam05483 531 RMLKqiENLEEKEMNLRDELESVREEFI------QKGDEVKCKLDKSEENARSIEYEVLKKEKQMKI--------LENKC 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 648 NQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTvaeLKQEISRLETKNSEM 727
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN---YQKEIEDKKISEEKL 673
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 281360709 728 LAEGE-LRANLDDSDKVRDLQDRLADMK-AELTALKSRGK 765
Cdd:pfam05483 674 LEEVEkAKAIADEAVKLQKEIDKRCQHKiAEMVALMEKHK 713
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
361-757 |
3.32e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 361 KKMEKEYQDLKKKEQEEMAELRRLRRENC--------------LLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAI 426
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVtteakikkleedilLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 427 Q----------TELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKeeaLKQRDEMVSCLLEELVKV 496
Cdd:pfam01576 179 SklknkheamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQ---LAKKEEELQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 497 RQGLAESEDQIRNLKAKVEELEEDKKTLR--ETTPDNSVAHLQDELIASKlREAEASLslkDLKQRVQELSSQWQRQLAE 574
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERaaRNKAEKQRRDLGEELEALK-TELEDTL---DTTAAQQELRSKREQEVTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 575 NQRSESERTTNAVDSTpkklltnffdSSKSSEHTQKLEE--ELMTTRIREMETLTELKElRLKVMELETQVQVSTNQLRR 652
Cdd:pfam01576 332 LKKALEEETRSHEAQL----------QEMRQKHTQALEEltEQLEQAKRNKANLEKAKQ-ALESENAELQAELRTLQQAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 653 QDEEHKKLKEELEMAVTREKdmSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETK--NSEMLAE 730
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQAR--LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQlqDTQELLQ 478
|
410 420
....*....|....*....|....*..
gi 281360709 731 GELRANLDDSDKVRDLQDRLADMKAEL 757
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQL 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
353-541 |
3.99e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 353 IKLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNE---LLEAESAELADRLVR--GQVSRaeeeetsyAIQ 427
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalLLSPEDFLDAVRRLQylKYLAP--------ARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 428 TELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSsidelcmKEEALKQRDEMVSCLLEELVKVRQGLAESEDQI 507
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAA-------LEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
170 180 190
....*....|....*....|....*....|....
gi 281360709 508 RNLKAKVEELEEDKKTLRETTPDNSVAHLQDELI 541
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
364-693 |
4.53e-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: 44.17 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 364 EKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEetsyaiqtelmqlrrsylevshQ 443
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE----------------------K 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 444 LENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLaeSEDQIRNLKAK--VEELEEDK 521
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL--DVQQTRAIQYQqaVQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 522 KTLREttPDNSVAHLQDELIASKLREAEASLSLKDLKQRV---QELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNF 598
Cdd:COG3096 427 ALCGL--PDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 599 FDSSKSSEHTQKLEEELmttriREMETLTELKElrlKVMELETQVQVSTNQLRRQDEEHKKLKEELEmavTREKDMSNKA 678
Cdd:COG3096 505 RSQQALAQRLQQLRAQL-----AELEQRLRQQQ---NAERLLEEFCQRIGQQLDAAEELEELLAELE---AQLEELEEQA 573
|
330
....*....|....*
gi 281360709 679 REQQHRYSDLESRMK 693
Cdd:COG3096 574 AEAVEQRSELRQQLE 588
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
463-644 |
5.17e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 463 NSRQSSIDELcMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEdkkTLRETTpdNSVAHLQDELiA 542
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPA---KLRQAQ--AELEALKDDN-D 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 543 SKLREAEASLSLKDLKQRVQELSSQ---WQRQLAE------NQRSESERTTNAVDSTPK------KLLTNFFDSSKSSEH 607
Cdd:PRK11281 112 EETRETLSTLSLRQLESRLAQTLDQlqnAQNDLAEynsqlvSLQTQPERAQAALYANSQrlqqirNLLKGGKVGGKALRP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 281360709 608 TQK--LEEEL------MTTRIREME---TLTEL-----KELRLKVMELETQVQ 644
Cdd:PRK11281 192 SQRvlLQAEQallnaqNDLQRKSLEgntQLQDLlqkqrDYLTARIQRLEHQLQ 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
475-761 |
5.31e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 475 KEEALKQRDEMvsclleelvkvRQGLAESEDQIRNLKAKVEELEEDKKTLREttpdnsVAHLQDELiasKLREAE-ASLS 553
Cdd:COG1196 174 KEEAERKLEAT-----------EENLERLEDILGELERQLEPLERQAEKAER------YRELKEEL---KELEAElLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 554 LKDLKQRVQELSSQwqRQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLT----EL 629
Cdd:COG1196 234 LRELEAELEELEAE--LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleeRR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 630 KELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQT 709
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281360709 710 VAELKQEISRLETKNSEMLAEGELRANLDDSDKVRDLQDRLADMKAELTALK 761
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
364-747 |
6.31e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 364 EKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESA----------ELAD--RLVRGQVSRAEEEETSYAIQTELM 431
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkavvlarllELQEepCPLCGSCIHPNPARQDIDNPGPLT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 432 QLRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQirNLK 511
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK--LSE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 512 AKVEELEEDKKTLRETTPDnsvAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTP 591
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPE---QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 592 KKLltnffDSSKSSEHTQKLEEELMTTRIREMEtlTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEmavtRE 671
Cdd:TIGR00618 683 QKM-----QSEKEQLTYWKEMLAQCQTLLRELE--THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM----HQ 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 672 KDMSNKAREQQHRYSDLESRMK----DELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAEGELRANLDDSDKVRDLQ 747
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
442-722 |
7.25e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 442 HQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEElvkVRQGLAESEDQIRNLKAKVEELeEDK 521
Cdd:pfam12128 230 IQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEE---RQETSAELNQLLRTLDDQWKEK-RDE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 522 KTLRETTPDNSVAHLQDELiasKLREAEASLSLK-DLKQRVQELSS--QWQRQLAENQRSESERTTNAVDSTPKkllTNF 598
Cdd:pfam12128 306 LNGELSAADAAVAKDRSEL---EALEDQHGAFLDaDIETAAADQEQlpSWQSELENLEERLKALTGKHQDVTAK---YNR 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 599 FDSSKSSEHTQKLEE-ELMTTRIREmETLTELKELRLKVMELETQVQVSTNQ-LRRQDEEHKKLK--------------- 661
Cdd:pfam12128 380 RRSKIKEQNNRDIAGiKDKLAKIRE-ARDRQLAVAEDDLQALESELREQLEAgKLEFNEEEYRLKsrlgelklrlnqata 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360709 662 -EELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQS-------QTVAELKQEISRLET 722
Cdd:pfam12128 459 tPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASealrqasRRLEERQSALDELEL 527
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
397-800 |
9.27e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 397 LLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYLEVshQLE-NANEEVRGLSLRLQEN-NNSRQSSIDEL-- 472
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM--QMErDAMADIRRRESQSQEDlRNQLQNTVHELea 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 473 --CMKEEALKQRDEMVscllEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTpdnSVAHLQD--ELIASKLREA 548
Cdd:pfam15921 157 akCLKEDMLEDSNTQI----EQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM---STMHFRSlgSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 549 EASLSLkdLKQRVQELSSQWQRQLAENQ-------RSESERTTNAVDSTPKKL--LTNFFDSSKSSEHTQKLEEELMTTR 619
Cdd:pfam15921 230 DTEISY--LKGRIFPVEDQLEALKSESQnkielllQQHQDRIEQLISEHEVEItgLTEKASSARSQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 620 IREMETLtelkeLRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNV 699
Cdd:pfam15921 308 ARNQNSM-----YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 700 KIKFTEQSQTVAELKQEISRL---ETKNSemLAEGELRANLDDSD-KVRDLQDRLADMKAELTALKSR------GKFPGA 769
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLwdrDTGNS--ITIDHLRRELDDRNmEVQRLEALLKAMKSECQGQMERqmaaiqGKNESL 460
|
410 420 430
....*....|....*....|....*....|.
gi 281360709 770 KLRSSSIQSIESTEidfndlNMVRRGSTELS 800
Cdd:pfam15921 461 EKVSSLTAQLESTK------EMLRKVVEELT 485
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
348-763 |
9.28e-04 |
|
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: 42.70 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 348 NLAYSIKLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRREncLLKQRNELLEAESaeladrlvrgQVSRAEEEETSYaiQ 427
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE--IKKKEKELEKLNN----------KYNDLKKQKEEL--E 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 428 TELMQLRRSYLEVSHQLENANEEVRGLSLRL------QENNNSRQSSIDELcmkEEALKQRDEMVSCLLEELVKVRQGLA 501
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkIQKNKSLESQISEL---KKQNNQLKDNIEKKQQEINEKTTEIS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 502 ESEDQIRNLK-----------AKVEELEEDKKTLRETTpdNSVAHLQDELiaSKLREAEASLSLKDLKQRVQelSSQWQR 570
Cdd:TIGR04523 250 NTQTQLNQLKdeqnkikkqlsEKQKELEQNNKKIKELE--KQLNQLKSEI--SDLNNQKEQDWNKELKSELK--NQEKKL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 571 QLAENQRSESERTTNAVDSTPKKLLTNFFDS-SKSSEHTQKLEE---ELMTTRIREMETLTELKELRLKVMELETQVQVS 646
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSeSENSEKQRELEEkqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 647 TNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLE---SRMKDELMNVKIKFTEQSQTVAELKQEISR---- 719
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLKVLSRSINKikqn 483
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 281360709 720 -------LETKNSEMLAEGELRANLDdsDKVRDLQDRLADMKAELTALKSR 763
Cdd:TIGR04523 484 leqkqkeLKSKEKELKKLNEEKKELE--EKVKDLTKKISSLKEKIEKLESE 532
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
609-765 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 609 QKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQD-EEHKKLKEELEMAVTREKDMSNKAREQQHRYSD 687
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281360709 688 LESRMKDElmnvKIKFTEQSQTVAELKQEISRLETKNSEMLAEGElranlddsDKVRDLQDRLADMKAELTALKSRGK 765
Cdd:COG4913 371 LGLPLPAS----AEEFAALRAEAAALLEALEEELEALEEALAEAE--------AALRDLRRELRELEAEIASLERRKS 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
375-567 |
1.23e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 375 QEEMAELRRLRRENCLLKQRNELLE------------AESAELADRLV------RGQVSRAEEEETSYAIQTELMQLRRS 436
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEpirelaeryaaaRERLAELEYLRaalrlwFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 437 YLEVSHQLENANEEVRGLSLRLQENNNSRqssIDELcmkEEALKQRDemvscllEELVKVRQGLAESEDQIRNLKAKVEE 516
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDR---LEQL---EREIERLE-------RELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 281360709 517 LEEDKKTLRETTPDnSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQ 567
Cdd:COG4913 378 SAEEFAALRAEAAA-LLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-678 |
2.39e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 443 QLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEED-K 521
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 522 KTLRETTPDNSVAHLQDELIASKLREAEASLS-LKDLKQRVQELSSQWQRQLAENQRSESERTTNavdstpkklltnffd 600
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAE--------------- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360709 601 sskssehtQKLEEELMTTRIREMETLTELKELRLKVM-ELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKA 678
Cdd:COG4942 173 --------RAELEALLAELEEERAALEALKAERQKLLaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
394-597 |
2.52e-03 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 41.23 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 394 RNELLEAESA-ELADRLvrgqvsraEEEEtsyaiqtelmqlrrSYLEVSHQLENANEEVrglSLRLQENNNSRQSSIDEL 472
Cdd:PLN00181 272 RENLEEREAAmELRDRI--------EEQE--------------LLLEFLFLIQQRKQEA---ADKLQDTISLLSSDIDQV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 473 CMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTP-DNSVAHLQDELIASKLREAEAS 551
Cdd:PLN00181 327 VKRQLVLQQKGSDVRSFLASRKRIRQGAETLAAEEENDDNSSKLDDTLESTLLESSRlMRNLKKLESVYFATRYRQIKAA 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 281360709 552 LSLKDLKQRVQELSSqwqrqlaENQRSeSERTTNAVDSTPKKLLTN 597
Cdd:PLN00181 407 AAAEKPLARYYSALS-------ENGRS-SEKSSMSNPAKPPDFYIN 444
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
544-763 |
2.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 544 KLREAEASLSLKDLKQRVQELSSQWQRqlAENQRSESERTTNAVDSTpkklltnffdsskssehtqkLEEELMTTRIREM 623
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEE--AEAALEEFRQKNGLVDLS--------------------EEAKLLLQQLSEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 624 ETltELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREkdmsnkareqqhRYSDLESRMKDELMnvkiKF 703
Cdd:COG3206 225 ES--QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA------------QLAELEAELAELSA----RY 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 704 TEQSQTVAELKQEISRLETKNSEMLAEGELRANLDdsdkVRDLQDRLADMKAELTALKSR 763
Cdd:COG3206 287 TPNHPDVIALRAQIAALRAQLQQEAQRILASLEAE----LEALQAREASLQAQLAQLEAR 342
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
457-688 |
2.57e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 457 RLQENNnsrqSSIDELCMKEEALKQRDEMVSCLLEELVKVrqglaeSEDQIRNLKAKVEELEEDKKTLRettpdNSVAHL 536
Cdd:PHA02562 175 KIRELN----QQIQTLDMKIDHIQQQIKTYNKNIEEQRKK------NGENIARKQNKYDELVEEAKTIK-----AEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 537 QDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERT----TNAVDSTPKKLLTNffdSSKSSEHTQKLe 612
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptcTQQISEGPDRITKI---KDKLKELQHSL- 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281360709 613 EELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDL 688
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
359-730 |
3.10e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 359 RMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYL 438
Cdd:pfam01576 195 RLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 439 EVSHQLEN-------ANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCL---LEELVKVR----------- 497
Cdd:pfam01576 275 ELQEDLESeraarnkAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELkkaLEEETRSHeaqlqemrqkh 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 498 -QGLAESEDQIRNLKAKVEELEEDKKTLrettpDNSVAHLQDELIASKLREAEASLSLKDLKQRVQELS---SQWQRQLA 573
Cdd:pfam01576 355 tQALEELTEQLEQAKRNKANLEKAKQAL-----ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlSESERQRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 574 ENQ------RSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEEL---------MTTRIREMET-----LTELKELR 633
Cdd:pfam01576 430 ELAeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeetrqklnLSTRLRQLEDernslQEQLEEEE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 634 LKVMELETQVQVSTNQL----RRQDEE----------HKKLKEELEMAVTREKDMSnkarEQQHRYSDLESRMKDELMNV 699
Cdd:pfam01576 510 EAKRNVERQLSTLQAQLsdmkKKLEEDagtlealeegKKRLQRELEALTQQLEEKA----AAYDKLEKTKNRLQQELDDL 585
|
410 420 430
....*....|....*....|....*....|.
gi 281360709 700 KIKFTEQSQTVAELKQEisrlETKNSEMLAE 730
Cdd:pfam01576 586 LVDLDHQRQLVSNLEKK----QKKFDQMLAE 612
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
379-737 |
3.62e-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: 40.65 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 379 AELRRLRRENCLlKQRNELLEAESAELADRlvrgQVSRAEEEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLSLRL 458
Cdd:pfam07888 29 AELLQNRLEECL-QERAELLQAQEAANRQR----EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 459 QENNNSRQSSIDE---LCMKEEALKQR----DEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLrETTPDN 531
Cdd:pfam07888 104 KELSASSEELSEEkdaLLAQRAAHEARirelEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 532 SVAHLQDelIASKLREAEASLSLKDLK-QRVQELSSQWQRQLAENQRSESErttnavDSTPKKLLTNFFDSSKSSEHT-Q 609
Cdd:pfam07888 183 TEEELRS--LSKEFQELRNSLAQRDTQvLQLQDTITTLTQKLTTAHRKEAE------NEALLEELRSLQERLNASERKvE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 610 KLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRysdLE 689
Cdd:pfam07888 255 GLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQR---LE 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 281360709 690 SRMKDELMnvkikftEQSQTVAELKQEISRLETKNSEMLAE-GELRANL 737
Cdd:pfam07888 332 ERLQEERM-------EREKLEVELGREKDCNRVQLSESRRElQELKASL 373
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
492-696 |
3.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 492 ELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLREttpdnSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQ 571
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNE-----EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 572 LAENQRSESerTTNAVD-----STPKKLLTNFFDSSKSSEHTQKLeeelmttriremetLTELKELRLKVMELETQVQVS 646
Cdd:COG3883 92 ARALYRSGG--SVSYLDvllgsESFSDFLDRLSALSKIADADADL--------------LEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 281360709 647 TNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDEL 696
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
354-730 |
4.34e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 354 KLNTKRMK-KMEKEYQDLKKKEQEEMA---ELRRLRRENC-------LLK-------QRNELLEAESAELADRLVRG--- 412
Cdd:pfam10174 281 KSHSKFMKnKIDQLKQELSKKESELLAlqtKLETLTNQNSdckqhieVLKesltakeQRAAILQTEVDALRLRLEEKesf 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 413 ------QVSRAEEEETSYAIQTELMQ------------LRRSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCM 474
Cdd:pfam10174 361 lnkktkQLQDLTEEKSTLAGEIRDLKdmldvkerkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTT 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 475 KEEALKQRDEMVSCL-----------LEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTPDNSVAHLQDEliaS 543
Cdd:pfam10174 441 LEEALSEKERIIERLkeqreredrerLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD---S 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 544 KLREAEASlslkdLKQRVQElSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREM 623
Cdd:pfam10174 518 KLKSLEIA-----VEQKKEE-CSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 624 ETLTELKELRLKVMELETQVQV------STNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQ-HRYSDLESRMKDEL 696
Cdd:pfam10174 592 ENEKNDKDKKIAELESLTLRQMkeqnkkVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQlEELMGALEKTRQEL 671
|
410 420 430
....*....|....*....|....*....|....
gi 281360709 697 MNVKIKFTEQSQTVAELKQEISRLETKNSEMLAE 730
Cdd:pfam10174 672 DATKARLSSTQQSLAEKDGHLTNLRAERRKQLEE 705
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
490-722 |
5.07e-03 |
|
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: 40.34 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 490 LEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTPD------NSVAHLQDEL--IASKLREAEASLSLKDLKQRV 561
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCmpdtyhERKQVLEKELkhLREALQQTQQSHAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 562 QELSSQWQRQL---------AENQRSESERTTNAVDSTPKKLltNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKEL 632
Cdd:TIGR00618 252 QEEQLKKQQLLkqlrarieeLRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 633 RLKVM----------ELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQH--RYSDLESRMKDELMNVK 700
Cdd:TIGR00618 330 RAAHVkqqssieeqrRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTltQKLQSLCKELDILQREQ 409
|
250 260
....*....|....*....|..
gi 281360709 701 IKFTEQSQTVAELKQEISRLET 722
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKK 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
362-718 |
5.25e-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: 40.39 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 362 KMEKEYQDLKKKEQ--EEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYLE 439
Cdd:TIGR04523 351 LTNSESENSEKQREleEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 440 VSHQLENANEEVRglslRLQENNNSRQSSIDELCMKEEALKQRdemVSCLLEELVKVRQGLaesEDQIRNLKAKVEELEE 519
Cdd:TIGR04523 431 LKETIIKNNSEIK----DLTNQDSVKELIIKNLDNTRESLETQ---LKVLSRSINKIKQNL---EQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 520 DKKTLRETtpDNSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNff 599
Cdd:TIGR04523 501 LNEEKKEL--EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT-- 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 600 dsSKSSEHTQKLEEELmttrIREMETltELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELemavTREKDMSNKAR 679
Cdd:TIGR04523 577 --QKSLKKKQEEKQEL----IDQKEK--EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII----KNIKSKKNKLK 644
|
330 340 350
....*....|....*....|....*....|....*....
gi 281360709 680 EQQHrysdlesRMKDELMNVKIKFTEQSQTVAELKQEIS 718
Cdd:TIGR04523 645 QEVK-------QIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
358-791 |
5.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 358 KRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVsraeeeeTSYAIQTELMQLRRSY 437
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI-------DPDAIKKELNEINVKL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 438 LEVSHQLENANEEVRGLSLRLQE-NNNSRQSSIDELC----------MKEEALKQRDEMVSCLLEELVKVRQGLAESEDQ 506
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDElSRNMEMLNGQSVCpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 507 IRNLKaKVEELEEDKKTLRETTPDNSVAHLQDELIASKLREAEaslsLKDLKQRVQELSSQWQRQLAENQRSESERTTNA 586
Cdd:PRK01156 499 IVDLK-KRKEYLESEEINKSINEYNKIESARADLEDIKIKINE----LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNA 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 587 ---VDSTPKKLLTNFFDSSKSS-----EHTQKLEEEL------MTTRIREMEtlTELKELRLKVMELEtQVQVSTNQLRR 652
Cdd:PRK01156 574 lavISLIDIETNRSRSNEIKKQlndleSRLQEIEIGFpddksyIDKSIREIE--NEANNLNNKYNEIQ-ENKILIEKLRG 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 653 QDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVkikfTEQSQTVAELKQEISRLETKNSEMLAEGE 732
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANR----ARLESTIEILRTRINELSDRINDINETLE 726
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281360709 733 ----LRANLDDSDKVRDLQDrladmKAELTAL--KSRGKFPGAKLRsssiQSIESTEIDFNDLNM 791
Cdd:PRK01156 727 smkkIKKAIGDLKRLREAFD-----KSGVPAMirKSASQAMTSLTR----KYLFEFNLDFDDIDV 782
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
476-729 |
9.10e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.56 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 476 EEALKQRDEMVSCLLEELVKVRQGLAES----EDQIRNLKAKVEELEEDKKTLRETTPDNSVAHLQDEL--IASKLREAE 549
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENAESSKRLNENannlIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEqeLEESKRETE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 550 ASLslkdlkQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLT-- 627
Cdd:COG5185 336 TGI------QNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEIla 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 628 ----ELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKarEQQHRYSDLESRMKDELMNVKIKF 703
Cdd:COG5185 410 tledTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS--RLEEAYDEINRSVRSKKEDLNEEL 487
|
250 260
....*....|....*....|....*.
gi 281360709 704 TEQSQTVAELKQEISRLETKNSEMLA 729
Cdd:COG5185 488 TQIESRVSTLKATLEKLRAKLERQLE 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
356-789 |
9.77e-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: 39.39 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 356 NTKRMK-KMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLR 434
Cdd:pfam01576 367 QAKRNKaNLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 435 RSYLEVSHQLENANEEVRGLSLRLQENNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKV 514
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 515 EELeedKKTLREttpDNSVAHLQDELIASKLREAEAslslkdLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKKL 594
Cdd:pfam01576 527 SDM---KKKLEE---DAGTLEALEEGKKRLQRELEA------LTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 595 LTNFFDsSKSSEHTQKLEEELMTTRIREME---TLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTRE 671
Cdd:pfam01576 595 LVSNLE-KKQKKFDQMLAEEKAISARYAEErdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 672 KDMSNKAREQQHRYSDLESRMKDelMNVKIKFTEQSQTVAELKQeiSRLETKNSEMLAEGELRANLDD---SDKVRDLQD 748
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEE--MKTQLEELEDELQATEDAK--LRLEVNMQALKAQFERDLQARDeqgEEKRRQLVK 749
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 281360709 749 RLADMKAELTALKsrgkfpgaKLRSSSIQSIESTEIDFNDL 789
Cdd:pfam01576 750 QVRELEAELEDER--------KQRAQAVAAKKKLELDLKEL 782
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
459-749 |
9.90e-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: 39.34 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 459 QENNNSRQSSIDELCMKEEALKQ-RDEMVSCL-----LEELVKVRQGLAESEDQIRNLKAKVE-ELEEDKKTLRETTPDN 531
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQeKEEKAREVerrrkLEEAEKARQAEMDRQAAIYAEQERMAmERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 532 SVAHLQDELIA---SKLREAEA-SLSLKDLKQRV-QELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNffdssKSSE 606
Cdd:pfam17380 361 ELERIRQEEIAmeiSRMRELERlQMERQQKNERVrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-----ARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 607 HTQKLEEElmttRIREMEtltelkelRLKVMELETQVQVstnQLRRQDEEHKKlKEELEMavtrEKDMSNKAREQQHRYS 686
Cdd:pfam17380 436 EVRRLEEE----RAREME--------RVRLEEQERQQQV---ERLRQQEEERK-RKKLEL----EKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281360709 687 DLESRMKDElmnvKIKFTEQSQTVAELKQEisrLETKNSEMLAEGELRANLDDSDKVRDLQDR 749
Cdd:pfam17380 496 ILEKELEER----KQAMIEEERKRKLLEKE---MEERQKAIYEEERRREAEEERRKQQEMEER 551
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
355-563 |
9.98e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 38.85 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 355 LNTKRMKKMEKEYQDLKK-----KEQEEMAEL-----RRLRRENCLLKQRNELLEAESAELADRLVRGQ----------- 413
Cdd:pfam04849 53 LCSDRVSQMTKTYNDIEAvtrllEEKERDLELaarigQSLLKQNSVLTERNEALEEQLGSAREEILQLRhelskkddllq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 414 -VSRAEEEETSYAIQTELMQLRRSYLEVSH--QLENANEEVRGlslrLQENNNSRQSSIDELCMKEEALKQRDEM----- 485
Cdd:pfam04849 133 iYSNDAEESETESSCSTPLRRNESFSSLHGcvQLDALQEKLRG----LEEENLKLRSEASHLKTETDTYEEKEQQlmsdc 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360709 486 ----------VSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTPDnsvahLQDELIASKLREAEASLSLK 555
Cdd:pfam04849 209 veqlseanqqMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEE-----LQQHLQASKEAQRQLTSELQ 283
|
....*...
gi 281360709 556 DLKQRVQE 563
Cdd:pfam04849 284 ELQDRYAE 291
|
|
| |
