|
Name |
Accession |
Description |
Interval |
E-value |
| MRVI1 |
pfam05781 |
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the ... |
1013-1488 |
1.02e-83 |
|
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the lymphoid-restricted membrane protein (JAW1) and the IP3 receptor associated cGMP kinase substrates A and B (IRAGA and IRAGB). The function of MRVI1 is unknown although mutations in the Mrvi1 gene induces myeloid leukaemia by altering the expression of a gene important for myeloid cell growth and/or differentiation so it has been speculated that Mrvi1 is a tumour suppressor gene. IRAG is very similar in sequence to MRVI1 and is an essential NO/cGKI-dependent regulator of IP3-induced calcium release. Activation of cGKI decreases IP3-stimulated elevations in intracellular calcium, induces smooth muscle relaxation and contributes to the antiproliferative and pro-apoptotic effects of NO/cGMP. Jaw1 is a member of a class of proteins with COOH-terminal hydrophobic membrane anchors and is structurally similar to proteins involved in vesicle targeting and fusion. This suggests that the function and/or the structure of the ER in lymphocytes may be modified by lymphoid-restricted resident ER proteins.
Pssm-ID: 461738 Cd Length: 521 Bit Score: 284.86 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 1013 PDKHKTGSKKTVVTSDSNS----TGSADS-LKDPSEKVKDMTFDPAASEdNIPTVPA----TQSPKKDPLASRNK----L 1079
Cdd:pfam05781 49 SPGHTSSSKSTVTSSDSRSpilrMASWDLdCKELCEKEEEKRFASKAGE-KQGKSPAfkdiQIQVSEEHILMRNKnlvgL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 1080 K-KEMSsmEVIEEQKAQEDGEPTVVTEKEgDTSVSSENASDStkddkNSLSPSDKEIEAEFHRLSLGFKCDMFTLEKRLR 1158
Cdd:pfam05781 128 EaPEES--ETAEQERKESAAGEDVMSSIP-DVLVKKVNFHQS-----LNTSANEKEVEAEFLRLSLAFKCDWFTLEKRVK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 1159 LEERSRDLAEENVRKEVISCKALLQALIPRCEEDNQSMEIIHRVQKNLEILVQSMTRVSSRSEMLGAIHQETRVGKTVEV 1238
Cdd:pfam05781 200 LEERSRDLAEENLKKEITNCLKLLESLTPLCEHDNQAQEIYKKLEKSIAVLSQCAARVASRAEMLGAINQESRVSKAVEV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 1239 MIQHVENLRRMYTKEHAELLELRENLTPNERSFGSHSERDDFRNKKQTTSNIFKTTS-RRISIATIPRSIGgqthfDMPK 1317
Cdd:pfam05781 280 MIQHVENLKRMYAKEHAELEELKQLLLQNSRSFNPLEDEDDCQIKKRSMSLNSKPSSlRRVSIASLPRNIG-----NSGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 1318 DMAETEVERLSRRSP-WNM-----AAKRPPLKRFVSSGTWADIDEPTLMNRYGYDTESHSEE-----------ERKEEPA 1380
Cdd:pfam05781 355 ASGMENNDRLSRRSSsWRIlgnkqSEHRPSLHRFISTYSWSDAEEESCEVKAKDEEEPYGEEgvektrkpslsEKKNNPS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 1381 SDRRTSLTElgiKITSFIMPAKiptpsptdnappslmegrPAVSRGARGIWIWVALFVVLAVLLALLASLMLQPAVDAAP 1460
Cdd:pfam05781 435 KWDVSSIYE---TLASWLTNLY------------------PSLRKANKVLWLSVAAIVLFAALMSFLTGQFFQSCVEAAP 493
|
490 500
....*....|....*....|....*...
gi 1207171629 1461 VGTGDSWMTIQQLLWPYTGLRHNGQPPV 1488
Cdd:pfam05781 494 TQEGDSWCSLEHILWPFTGLQHEGPPPV 521
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
347-537 |
7.29e-62 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 209.65 E-value: 7.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 347 LETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSE 426
Cdd:pfam14662 1 METSDLLTCVEDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 427 ESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQM 506
Cdd:pfam14662 81 EARRSLLAQNKQLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQI 160
|
170 180 190
....*....|....*....|....*....|.
gi 1207171629 507 DELKVAVVEYSSVTELLRADKNKLESQMQMM 537
Cdd:pfam14662 161 EELKSTVEEYSSIEEELRAEKSRLESQLPDM 191
|
|
| EF-hand_9 |
pfam14658 |
EF-hand domain; |
230-295 |
3.83e-14 |
|
EF-hand domain;
Pssm-ID: 405361 Cd Length: 66 Bit Score: 68.61 E-value: 3.83e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171629 230 DTIFQACDTQCRGKVYVSHIVDFLRHTTCRSSEDSGLEELCNMLDPERKDISIDLDTYHAIMKEWI 295
Cdd:pfam14658 1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDALVDLDTFLRVMRDWI 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
303-538 |
5.83e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 303 KDLKNDTQQESSKLRDSLSAKRSALlnmtsgsleafggeaSRADLETSDLVfcvADLQLNNQKLQEEVRKLKQAVENMED 382
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQEL---------------SDASRKIGEIE---KEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 383 TNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSS--EESRAQAAAQRKQMERENQSLISKIAALQEENMKV 460
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 461 TL---EAEELQKKMNDLCDLNADLQVQIHSFDAILADKESliqeknkQMDELKVAVVEYSSVTELLRADKNKLESQMQMM 537
Cdd:TIGR02169 829 EYlekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-------ELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
.
gi 1207171629 538 Q 538
Cdd:TIGR02169 902 E 902
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-758 |
6.31e-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: 60.84 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 364 QKLQEEVRKLKQAVENM---EDtnqkLIEENEE----LKTQAKMGQQLLQkekmLKEEVEEMKLSL-----TSSEESRAQ 431
Cdd:TIGR02168 172 ERRKETERKLERTRENLdrlED----ILNELERqlksLERQAEKAERYKE----LKAELRELELALlvlrlEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 432 AAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLcdlnadlQVQIHSFDAILADKESLIQEKNKQMDELKV 511
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-------QKELYALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 512 AVVEYSSVTELLRADKNKLESQMQMMQPDVTipglslsvayrlnqtssgSLQTELALAQNPLEGLEhlSTSVCFASSLD- 590
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLE------------------ELKEELESLEAELEELE--AELEELESRLEe 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 591 -----ETLDREVLLLLQgpTPEQLSLEFKSLISRLK-----REFKEDGLTFLTAIRSLTENSETQEANTDLKMQglEVQL 660
Cdd:TIGR02168 377 leeqlETLRSKVAQLEL--QIASLNNEIERLEARLErledrRERLQQEIEELLKKLEEAELKELQAELEELEEE--LEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 661 EQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLsvkvqeqENQKQQLREEVDRLKTPLDNReasSQTPDHL 740
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-------ERLQENLEGFSEGVKALLKNQ---SGLSGIL 522
|
410
....*....|....*...
gi 1207171629 741 QQVVEeldgpSLEWDEEY 758
Cdd:TIGR02168 523 GVLSE-----LISVDEGY 535
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
357-531 |
1.06e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 357 ADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQR 436
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 437 KQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQ-MDELKVAVVE 515
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEElLEALRAAAEL 398
|
170
....*....|....*.
gi 1207171629 516 YSSVTELLRADKNKLE 531
Cdd:COG1196 399 AAQLEELEEAEEALLE 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-533 |
1.29e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 330 MTSGSLEAFGGEA-SRADLETSDLVfcVADLQ-LNNQK--LQEEVRKLKQAvenMEDTNQKLIEENEELKTQAKMGQQLL 405
Cdd:TIGR02169 655 MTGGSRAPRGGILfSRSEPAELQRL--RERLEgLKRELssLQSELRRIENR---LDELSQELSDASRKIGEIEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 406 QKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKvtLEA-------EELQKKMNDLCDLN 478
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--LEArlshsriPEIQAELSKLEEEV 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207171629 479 ADLQVQIHSFDAILADK-------ESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQ 533
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-805 |
3.68e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 310 QQESSKLRDSLSAKRSALLNMTSGSLEAFGGEASRADLEtsdlvfcvADLQLNNQKLQEEVRKLKQAVENMEdtnQKLIE 389
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--------RELEERLEELEEELAELEEELEELE---EELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 390 ENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQK 469
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 470 KMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTipgLSLS 549
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---LLLE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 550 VAYRLNQTSSGSLQTELALAQNPLEGLEHLSTSVCFAsslDETLDREVLLLLQGPTPEQLSLEFKSLISRLKREfKEDGL 629
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA---YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA-KAGRA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 630 TFL--TAIRSLTENSETQEANTDLKMQGLEVQLEQR--------------RTDWIRSLEQLDQYRDSLEREL----LKMA 689
Cdd:COG1196 575 TFLplDKIRARAALAAALARGAIGAAVDLVASDLREadaryyvlgdtllgRTLVAARLEAALRRAVTLAGRLrevtLEGE 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 690 SNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREASSQTPDHLQQVVEELDGPSLEWDEEYVLSEsppLQEL 769
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE---EQLE 731
|
490 500 510
....*....|....*....|....*....|....*.
gi 1207171629 770 GPDQQMLEELCCDEEVLQALKQEEEEPTETVSDKEK 805
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-722 |
6.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 356 VADLQLNNQKLQEEVRKLKQAVENMEDTNQK---------LIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSE 426
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELealeaelaeLPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 427 ESRAQAAAQR-KQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLcdlnadlqvqihsfdailaDKESLIQEKNKQ 505
Cdd:COG4717 184 EQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL-------------------ENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 506 MDELKVAVVEYSSVTELLRADKNKLESQmqmmqpdVTIPGLSLSVA--------YRLNQTSSGSLQTELALAQNPLEGLE 577
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLI-------LTIAGVLFLVLgllallflLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 578 HLS-TSVCFASSLDETLDREVLL-----------LLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTAIRSLTENSETQ 645
Cdd:COG4717 318 EEElEELLAALGLPPDLSPEELLelldrieelqeLLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 646 EANTDlKMQGLEVQLEQRRTDWIRS------------LEQLDQYRDSLERELLKMASNMRRSRTEILHL------SVKVQ 707
Cdd:COG4717 398 QELKE-ELEELEEQLEELLGELEELlealdeeeleeeLEELEEELEELEEELEELREELAELEAELEQLeedgelAELLQ 476
|
410
....*....|....*
gi 1207171629 708 EQENQKQQLREEVDR 722
Cdd:COG4717 477 ELEELKAELRELAEE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
360-729 |
1.78e-07 |
|
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: 55.80 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 360 QLNNQ--KLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKekmLKEEVEEMKLSLTSSEESRAQAAAQRK 437
Cdd:TIGR04523 325 EIQNQisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK---LKKENQSYKQEIKNLESQINDLESKIQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 438 QMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKvavVEYS 517
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS---RSIN 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 518 SVTELLRADKNKLESQMQMM-QPDVTIPGLSLSVAYrLNQTSSGSLQTELALAQNPLEGLEHLSTSVCFASSLDETLDRE 596
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELkKLNEEKKELEEKVKD-LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 597 VLlllqgptpEQLSLEFKSLISRLKREFKEdgltfltairSLTENSETQEantdlkmqgLEVQLEQRRTDWIRSLEQLDQ 676
Cdd:TIGR04523 558 NL--------EKEIDEKNKEIEELKQTQKS----------LKKKQEEKQE---------LIDQKEKEKKDLIKEIEEKEK 610
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1207171629 677 YRDSLERELLKMASNMRRSRTEILHLsvkvqeqENQKQQLREEVDRLKTPLDN 729
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNI-------KSKKNKLKQEVKQIKETIKE 656
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
357-883 |
4.25e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 357 ADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELK-TQAKMGQQLLQKEKMLKEEvEEMKLSLTSSEESRAQAAAQ 435
Cdd:TIGR00618 201 LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEELRAQEAVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 436 RKQMERENQS-----LISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSfDAILADKESLIQEKNKQMDELK 510
Cdd:TIGR00618 280 EETQERINRArkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 511 VAVVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQ-TSSGSLQTELALAQNPLEG-LEHLSTSvcfass 588
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIlQREQATIDTRTSAFRDLQGqLAHAKKQ------ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 589 ldETLDREVLLLLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTA----IRSLTENSETQEANTDLKMQGLEVQLEQRR 664
Cdd:TIGR00618 433 --QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 665 TDWIRSLEQLDQyRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDN----REASSQTPDHL 740
Cdd:TIGR00618 511 IHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqcDNRSKEDIPNL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 741 QQVVEELD--GPSLEWDEEYVLSESPPLQELGPDQQMLEELC-----CDEEVLQALKQEEEEPTETVSDKEKITAKSEGE 813
Cdd:TIGR00618 590 QNITVRLQdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlhlqqCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207171629 814 GEATYDSGVENeEPQRDFTLSHMCLPDKKSERESNEAP-----FVGEGGEQRPCMSLKEEDRLPECTGPEDAHEQ 883
Cdd:TIGR00618 670 LPKELLASRQL-ALQKMQSEKEQLTYWKEMLAQCQTLLreletHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
355-729 |
4.28e-07 |
|
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: 54.80 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 355 CVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLieENEELKTQAKM------------GQQLLQKE-KMLKEEVEEMKLS 421
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL--QLEKVTTEAKIkkleedillledQNSKLSKErKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 422 LTSSEESraqaAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKM----NDLCDLNADLQVQIHSFDAILADKES 497
Cdd:pfam01576 168 LAEEEEK----AKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLegesTDLQEQIAELQAQIAELRAQLAKKEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 498 LIQEKNKQMDElkvavvEYSSVTELLRADKnKLESQMQMMQPDVTipglslsvAYRLNQTSSGSLQTELAlaqnplEGLE 577
Cdd:pfam01576 244 ELQAALARLEE------ETAQKNNALKKIR-ELEAQISELQEDLE--------SERAARNKAEKQRRDLG------EELE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 578 HLSTsvcfasSLDETLDrevllllqgPTPEQLSLEFK--SLISRLKREFKEDGLTFLTAIRSLTENSETQeantdlkMQG 655
Cdd:pfam01576 303 ALKT------ELEDTLD---------TTAAQQELRSKreQEVTELKKALEEETRSHEAQLQEMRQKHTQA-------LEE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 656 LEVQLEQRRtdwiRSLEQLDQYRDSLERELLKMASNMR---RSRTEILH-----------LSVKVQEQENQKQQLREEVD 721
Cdd:pfam01576 361 LTEQLEQAK----RNKANLEKAKQALESENAELQAELRtlqQAKQDSEHkrkklegqlqeLQARLSESERQRAELAEKLS 436
|
....*...
gi 1207171629 722 RLKTPLDN 729
Cdd:pfam01576 437 KLQSELES 444
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
358-792 |
8.06e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 358 DLQLNNQKLQEEVRKLKQAVE-NMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEM---KLSLTSSEESRAQAA 433
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDLT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 434 AQRKQMERENQSLISKIAALQEenmKVTLEAEELQKKMNDLCDLNaDLQVQIHSFDAILADKESLIQEKNKQMDELKVAV 513
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKLRS---RVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 514 VEYSSVTELLRADKNKLESQMQMMQPDVTipglslsvAYRLNQTSSGSLQTELALAQNPLEgLEhlstSVCFASSLDETL 593
Cdd:pfam15921 579 GQHGRTAGAMQVEKAQLEKEINDRRLELQ--------EFKILKDKKDAKIRELEARVSDLE-LE----KVKLVNAGSERL 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 594 dREVLLLLQgpTPEQLSLEFKSLISRLKrEFKEDGLTFLTAIRSLTENSETQEANTDLKMQGLEVQLEQRRTDwIRSLEQ 673
Cdd:pfam15921 646 -RAVKDIKQ--ERDQLLNEVKTSRNELN-SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNT-LKSMEG 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 674 LDQYRdslerelLKMASNMRRS----RTEILHLSVKVQEQENQKQQLREEVDRLKtpldnrEASSQTPDHLQQVVEELDG 749
Cdd:pfam15921 721 SDGHA-------MKVAMGMQKQitakRGQIDALQSKIQFLEEAMTNANKEKHFLK------EEKNKLSQELSTVATEKNK 787
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1207171629 750 PSLEWD----EEYVLSESPPLQELGPDQQMLEELCCdEEVLQALKQE 792
Cdd:pfam15921 788 MAGELEvlrsQERRLKEKVANMEVALDKASLQFAEC-QDIIQRQEQE 833
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
364-811 |
1.07e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 364 QKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMG------------------QQLLQKEKMLKEEVEEMKLSLTSS 425
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENArlemhfklkedhekiqhlEEEYKKEINDKEKQVSLLLIQITE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 426 EESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKmnDLCDLNADLQVQIHSFDAILADKE-------SL 498
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK--ELEDIKMSLQRSMSTQKALEEDLQiatkticQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 499 IQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQTSSGSLQTELALAQNPLEGLEH 578
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 579 LSTsvcfassldeTLDREVLLLLQGPTPEQLSLEFKSlisrlkrefKEDGLTFLTAIRsltensetqeantDLKMQGLEV 658
Cdd:pfam05483 410 LKK----------ILAEDEKLLDEKKQFEKIAEELKG---------KEQELIFLLQAR-------------EKEIHDLEI 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 659 QLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQE-----------QENQKQQLREEVDRLKTPL 727
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtlelkkhQEDIINCKKQEERMLKQIE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 728 DNREASSQTPDHLQQVVEELDGP------SLEWDEEYVLSESPPLQELGPDQQMLEELCCD--EEVLQALKQEEEEPTET 799
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQKgdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQEN 617
|
490
....*....|..
gi 1207171629 800 VSDKEKITAKSE 811
Cdd:pfam05483 618 KALKKKGSAENK 629
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-795 |
1.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 368 EEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLsltssEESRAQAAAQRKQMERENQSLI 447
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 448 SKIAALQEENmkvtLEAEELQKKMNDLCDLNADLQVQIHS-FDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRAD 526
Cdd:COG4717 146 ERLEELEERL----EELRELEEELEELEAELAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 527 KNKLESQMQMMQPDVTIPGLSLSVAYRLNQTSSGSLQTELALAqnpleGLEHLSTSVCFAssldetldrEVLLLLQGPTP 606
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGL-----GGSLLSLILTIA---------GVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 607 EQLSLEFKSLISRLKREFKEDGLTFLTAIrsltensETQEANTDLKMQGLEVQLEQRRT----DWIRSLEQLDQYRDSLE 682
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEEL-------EEEELEELLAALGLPPDLSPEELlellDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 683 RELLKMASNMRR----------SRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREASSQ--TPDHLQQVVEELDGP 750
Cdd:COG4717 361 EELQLEELEQEIaallaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEE 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1207171629 751 SLEWDEEY-VLsesppLQELGPDQQMLEELCCDEEvLQALKQEEEE 795
Cdd:COG4717 441 LEELEEELeEL-----REELAELEAELEQLEEDGE-LAELLQELEE 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-817 |
1.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 371 RKlKQAVENMEDTNQKL---------IEEN-EELKTQAKmgqqllQKEK--MLKEEVEEMKLSLT-------SSEESRAQ 431
Cdd:COG1196 173 RK-EEAERKLEATEENLerledilgeLERQlEPLERQAE------KAERyrELKEELKELEAELLllklrelEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 432 AAAQRKQMEREnqSLISKIAALQEENMKVTLEAEELQKKMNdlcDLNADLQVQIHSFDAILADKESLIQEKNkqmdELKV 511
Cdd:COG1196 246 AELEELEAELE--ELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLEQDIARLEERRR----ELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 512 AVVEYSSVTELLRADKNKLESQMQmmqpdvtipglslsvayrlnqtssgSLQTELALAQNPLEGLEHLstsvcfASSLDE 591
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELE-------------------------ELEEELEEAEEELEEAEAE------LAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 592 TLDREVLLLLQGptpEQLSLEFKSLISRLKREfkedgltfLTAIRSLTENSETQEANTDLKMQGLEVQLEQRRtdwiRSL 671
Cdd:COG1196 366 ALLEAEAELAEA---EEELEELAEELLEALRA--------AAELAAQLEELEEAEEALLERLERLEEELEELE----EAL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 672 EQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREASSQTpdhLQQVVEELDGPS 751
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL---LLEAEADYEGFL 507
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171629 752 LEWDEEYVLSESPPLQELGPDQQMLEELC--CDEEVLQALKQEEEEPTETVSDKEKITAKSEGEGEAT 817
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
408-753 |
1.94e-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: 52.81 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 408 EKMLKE---EVEEMKLSLTSSEEsraqaaAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQ 484
Cdd:pfam15921 77 ERVLEEyshQVKDLQRRLNESNE------LHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 485 IHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLR--------ADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQ 556
Cdd:pfam15921 151 VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRsilvdfeeASGKKIYEHDSMSTMHFRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 557 TSSGSLQTELALAQNPLEGLEHLSTSvcfassldetlDREVLLLLQGPTPEQLSLEFKSLISRLKRE---FKEDGLTFLT 633
Cdd:pfam15921 231 TEISYLKGRIFPVEDQLEALKSESQN-----------KIELLLQQHQDRIEQLISEHEVEITGLTEKassARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 634 AIRSLTENSETQEANTDLKMQGLEVQLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQK 713
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1207171629 714 QQL------RE-----EVDRLKTPLDNREASSQTPDHLQQvveELDGPSLE 753
Cdd:pfam15921 380 QKLladlhkREkelslEKEQNKRLWDRDTGNSITIDHLRR---ELDDRNME 427
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-747 |
3.04e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 358 DLQLNNQKLQEEVRKLKQAVENmedtnqkLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQR- 436
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEl 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 437 KQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLcdlnadlqvqihsfdailaDKESLIQEKNKQMDELKVAVVEY 516
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL-------------------ENELEAAALEERLKEARLLLLIA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 517 SSVTELLRADKNKLESQmqmmqpdVTIPGLSLSVA--------YRLNQTSSGSLQTELALAQNPLEGLEHLS-TSVCFAS 587
Cdd:COG4717 256 AALLALLGLGGSLLSLI-------LTIAGVLFLVLgllallflLLAREKASLGKEAEELQALPALEELEEEElEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 588 SLDETLDREVLL-----------LLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTAIRSLTENSETQEANTDlKMQGL 656
Cdd:COG4717 329 GLPPDLSPEELLelldrieelqeLLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE-ELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 657 EVQLEQRRTDWIRSLEQLDqyRDSLErellkmasnmrrsrTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREaSSQT 736
Cdd:COG4717 408 EEQLEELLGELEELLEALD--EEELE--------------EELEELEEELEELEEELEELREELAELEAELEQLE-EDGE 470
|
410
....*....|.
gi 1207171629 737 PDHLQQVVEEL 747
Cdd:COG4717 471 LAELLQELEEL 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
332-518 |
5.40e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 332 SGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQ-AKMGQQLLQKEKM 410
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEiDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 411 LKEEVEEMK----------------LSLTSSEE-----SRAQAaaqRKQMERENQSLISKIAALQEEnmkVTLEAEELQK 469
Cdd:COG3883 81 IEERREELGeraralyrsggsvsylDVLLGSESfsdflDRLSA---LSKIADADADLLEELKADKAE---LEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207171629 470 KMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSS 518
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-535 |
5.54e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 330 MTSGSLEAFGGEASRaDLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKek 409
Cdd:TIGR02168 661 ITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 410 mLKEEVEEMKLSLTSSEESRAQAAAQR--------------KQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLC 475
Cdd:TIGR02168 738 -LEAEVEQLEERIAQLSKELTELEAEIeeleerleeaeeelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 476 DLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQ 535
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-538 |
8.18e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 295 IEDCRNQ-GKDLKNDTQQESS--KLRDSLSAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVR 371
Cdd:TIGR02168 191 LEDILNElERQLKSLERQAEKaeRYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 372 KLKQAVENMEDTNQKLIEENEELKtqakmgqQLLQKekmLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIA 451
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALA-------NEISR---LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 452 ALQEenmkvtlEAEELQKKMndlcdlnADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLE 531
Cdd:TIGR02168 341 ELEE-------KLEELKEEL-------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
....*..
gi 1207171629 532 SQMQMMQ 538
Cdd:TIGR02168 407 ARLERLE 413
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
299-675 |
8.96e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 299 RNQGKDLKNDTQQESSKLRDSLSAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVA-DLQLNNQKLQEEVRKLKQAV 377
Cdd:COG5022 858 KKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLL 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 378 ENMEDTNQKLIEeneelKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLiskiAALQEEN 457
Cdd:COG5022 938 NNIDLEEGPSIE-----YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL----AELSKQY 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 458 MKVTLEAEELQKKMNDLCDLNADLQV--QIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKnKLESQMQ 535
Cdd:COG5022 1009 GALQESTKQLKELPVEVAELQSASKIisSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDD-KQLYQLE 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 536 mmqpdvTIPGLSLSVAYRLNQTSSGSL-----QTELALAQNPLEGLEHLSTSvcFASSLDETL-----DREVLLLLQGPT 605
Cdd:COG5022 1088 ------STENLLKTINVKDLEVTNRNLvkpanVLQFIVAQMIKLNLLQEISK--FLSQLVNTLepvfqKLSVLQLELDGL 1159
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207171629 606 PEQLSLEFKSLISRL-----KREFKEDGLTFltairsltENSETQEANTDLKMQgLEVQLEQRRTDWIRSLEQLD 675
Cdd:COG5022 1160 FWEANLEALPSPPPFaalseKRLYQSALYDE--------KSKLSSSEVNDLKNE-LIALFSKIFSGWPRGDKLKK 1225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-532 |
1.16e-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: 50.06 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 304 DLKNDTQQESSKLRDSLSAKRSALLNMTS------GSLEAFGGEASRADletsdlvfcvADLQLNNQKLQEEVRKLKQAV 377
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEeieelqKELYALANEISRLE----------QQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 378 ENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLtssEESRAQAAAQRKQMERENqsliSKIAALQEEN 457
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL---EELESRLEELEEQLETLR----SKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 458 MKVTLEAEELQKKMNDLCDLNADLQVQI---------HSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKN 528
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIeellkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
....
gi 1207171629 529 KLES 532
Cdd:TIGR02168 476 ALDA 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
365-533 |
1.26e-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: 50.07 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 365 KLQEEVRKLKQAVENMEDTNQKLieENEELKTQAKMGQQLLQKEKmLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQ 444
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDA--EERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 445 SLISKIAALQEENMKVTLEAEELQKKMNDL---CDLNADLQVQIHSFDA-ILADKESLIQEKNKQMDELKVAVVEYSSVT 520
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELkreLDRLQEELQRLSEELAdLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
170
....*....|....*.
gi 1207171629 521 ---ELLRADKNKLESQ 533
Cdd:TIGR02169 455 wklEQLAADLSKYEQE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-532 |
1.38e-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: 50.06 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 342 ASRADLETSdLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLS 421
Cdd:TIGR02168 309 ERLANLERQ-LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 422 LTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKK--MNDLCDLNADLQVQIHSFDAILADKESL- 498
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelQAELEELEEELEELQEELERLEEALEELr 467
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207171629 499 --IQEKNKQMDELKVAVVEYSSVTELLRADKNKLES 532
Cdd:TIGR02168 468 eeLEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
408-536 |
1.65e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 408 EKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEenmkvtlEAEELQKKMNDlcDLNADLQVQIHS 487
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEE-------KARLALEKGRE--DLAREALERKAE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207171629 488 FDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQM 536
Cdd:COG1842 96 LEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKA 144
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
363-504 |
2.14e-05 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 49.29 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 363 NQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTqakmgqQLLQKEKMLkeevEEMKLSLTSSEESRAQAAAQRKQMERE 442
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKS------QLQESEQLI----AELRSELASLKESNSLAETQLKCMAES 752
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 443 NQSLISKIAALQEE----NMKV-TLEAeELQKKMNDLCDLNA---DLQVQIHSFDAILADKESLIQEKNK 504
Cdd:pfam05911 753 YEDLETRLTELEAElnelRQKFeALEV-ELEEEKNCHEELEAkclELQEQLERNEKKESSNCDADQEDKK 821
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
364-474 |
2.70e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.98 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 364 QKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEE-MKLSLTSSEESRAQAAAQRKqmere 442
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEkAQAALTKGNEELAREALAEK----- 92
|
90 100 110
....*....|....*....|....*....|..
gi 1207171629 443 nQSLISKIAALQEENMKVTLEAEELQKKMNDL 474
Cdd:pfam04012 93 -KSLEKQAEALETQLAQQRSAVEQLRKQLAAL 123
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
357-507 |
3.12e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 357 ADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQR 436
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207171629 437 KQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLcdlnaDLQVQIHSFDAILADKESLIQEKNKQMD 507
Cdd:COG4372 132 KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAE 197
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-506 |
3.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 304 DLKNDTQQESSKLRDSLSAKRsALLNMTSGSLEAFGGEASRADLETSDLVfcvADLQLNNQKLQEEVRKLKQAVENMEDT 383
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 384 NQKLIEENEELKTQA----KMGQQ-----------LLQKEKML----------KEEVEEMKLSLTSSEESRAQAAAQRKQ 438
Cdd:COG4942 96 RAELEAQKEELAELLralyRLGRQpplalllspedFLDAVRRLqylkylaparREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171629 439 MERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQM 506
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
265-511 |
5.02e-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: 48.14 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 265 GLEELCNMLDPERKDISIDLDTYHAIMKEW---IEDCRNQGKDLKNDTQQESSKLRDS---LSAKRSALLNMtsgsleaf 338
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDAsrkIGEIEKEIEQLEQEEEKLKERLEELeedLSSLEQEIENV-------- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 339 ggEASRADLETSdlvfcVADLQLNNQKLQEEVRKLKQA-----VENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKE 413
Cdd:TIGR02169 757 --KSELKELEAR-----IEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 414 EVEEMKLSLtssEESRAQAAAQRKQMERENQSLISKIAALQEEnmkvtleAEELQKKMNDLCDLNADLQVQIHSFDAILA 493
Cdd:TIGR02169 830 YLEKEIQEL---QEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250
....*....|....*...
gi 1207171629 494 DKESLIQEKNKQMDELKV 511
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRK 917
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
364-533 |
6.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 364 QKLQEEVRKLK--------QAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKM-LKEEVEEMKLSLTSSEESRAQAAA 434
Cdd:COG1196 216 RELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEeLRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 435 QRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVV 514
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170
....*....|....*....
gi 1207171629 515 EYSSVTELLRADKNKLESQ 533
Cdd:COG1196 376 EAEEELEELAEELLEALRA 394
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
267-505 |
8.93e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 267 EELCNMLDPERKDISiDLDTYHAIMKEWIEDCRNQGKDLKndTQQESSKLRDSLSAKRSALLNMTSGSLEAfggeasrad 346
Cdd:pfam05483 439 QELIFLLQAREKEIH-DLEIQLTAIKTSEEHYLKEVEDLK--TELEKEKLKNIELTAHCDKLLLENKELTQ--------- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 347 lETSDLVFCVADLQ--LNNQKLQEEvRKLKQaVENMEDTNQKLIEENEELKtqakmgqqllqkeKMLKEEVEEMKLSLTS 424
Cdd:pfam05483 507 -EASDMTLELKKHQedIINCKKQEE-RMLKQ-IENLEEKEMNLRDELESVR-------------EEFIQKGDEVKCKLDK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 425 SEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDaILADKESLIQEKNK 504
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE-IKVNKLELELASAK 649
|
.
gi 1207171629 505 Q 505
Cdd:pfam05483 650 Q 650
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
421-831 |
8.93e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 421 SLTSSEESRAQAAAQRKQMERENQSLI----SKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKE 496
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIeeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 497 SLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQmmQPDVTIPGLSLSVAYRLNQTSS-----GSLQTELAL--- 568
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA--EAEAEIEELEAQIEQLKEELKAlrealDELRAELTLlne 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 569 -AQNPLEGLEHLSTSVCFASSLDETLDREVllllqgptpEQLSLEfkslISRLKREFKEDGltfltaiRSLTENSETQEA 647
Cdd:TIGR02168 818 eAANLRERLESLERRIAATERRLEDLEEQI---------EELSED----IESLAAEIEELE-------ELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 648 NTDLKMQgLEVQLEQRRTDwirsleqldqyRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPL 727
Cdd:TIGR02168 878 LLNERAS-LEEALALLRSE-----------LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 728 dnREASSQTPDHLQQVVEELDGPSLEWDEEYVLSESpPLQELGPDQQM-LEELCCDEEVLQALKQEEEEPTETVSDKEKI 806
Cdd:TIGR02168 946 --SEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN-KIKELGPVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
410 420
....*....|....*....|....*..
gi 1207171629 807 TAKSEGEGEATYDSGVE--NEEPQRDF 831
Cdd:TIGR02168 1023 IEEIDREARERFKDTFDqvNENFQRVF 1049
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-531 |
1.01e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 356 VADLQLNNQKLQEEVRKLkqaVENMEDTNQKLIEENEELKtqAKMGQQLLQkekmLKEEVEEMKLSLTSSEESRAQAAAQ 435
Cdd:TIGR02169 246 LASLEEELEKLTEEISEL---EKRLEEIEQLLEELNKKIK--DLGEEEQLR----VKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 436 RKQMERENQSLISKIAALQEEnmkvtleAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVE 515
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170
....*....|....*.
gi 1207171629 516 YSSVTELLRADKNKLE 531
Cdd:TIGR02169 390 YREKLEKLKREINELK 405
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
400-553 |
1.72e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 44.67 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 400 MGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEElqkkmndlcDLNA 479
Cdd:pfam04012 16 GLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNE---------ELAR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171629 480 DLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKL--ESQMQMMQPDV--TIPGLSLSVAYR 553
Cdd:pfam04012 87 EALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkaRLKAAKAQEAVqtSLGSLSTSSATD 164
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
341-534 |
1.75e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.36 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 341 EASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQ-AKMGQQLLQKEKMLKEEVEEMK 419
Cdd:cd00176 20 EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiQERLEELNQRWEELRELAEERR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 420 LSLtssEESRAQAAAQRkQMERENQSLISKIAALQeeNMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLI 499
Cdd:cd00176 100 QRL---EEALDLQQFFR-DADDLEQWLEEKEAALA--SEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207171629 500 Q--------EKNKQMDELKVAvveYSSVTELLRADKNKLESQM 534
Cdd:cd00176 174 EeghpdadeEIEEKLEELNER---WEELLELAEERQKKLEEAL 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
376-538 |
2.26e-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: 45.14 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 376 AVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQE 455
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 456 E----------------------NMKVTLEAE-----------------ELQKKMNDLCDLNADLQVQIHSFDAILADKE 496
Cdd:COG4942 98 EleaqkeelaellralyrlgrqpPLALLLSPEdfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207171629 497 SLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQ 538
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
299-805 |
2.54e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 299 RNQGKDLKNDTQQESSKLRDSLSAKRSAL-------LNMTSGSLEAFGGEASRADLETSDLVFCVADLQL---NNQKLQE 368
Cdd:pfam12128 296 DDQWKEKRDELNGELSAADAAVAKDRSELealedqhGAFLDADIETAAADQEQLPSWQSELENLEERLKAltgKHQDVTA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 369 EVRKLKQAVE-----NMEDTNQKLIEENEELKTQAKMGQQLLQK-EKMLKEEVEEMKLSLTSSEESRAQAAAQRKQmeRE 442
Cdd:pfam12128 376 KYNRRRSKIKeqnnrDIAGIKDKLAKIREARDRQLAVAEDDLQAlESELREQLEAGKLEFNEEEYRLKSRLGELKL--RL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 443 NQSLISKIAALQEENMKVTLEA--EELQKKMNDLCDLNADLQVQIHSFDailadkesliqeknKQMDELKVAVVEYSSVt 520
Cdd:pfam12128 454 NQATATPELLLQLENFDERIERarEEQEAANAEVERLQSELRQARKRRD--------------QASEALRQASRRLEER- 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 521 ellradKNKLESQMQMMQPDvtipglSLSVAYRLNQTSSGSLQTELALAQNPLEGLEHLSTSVCFASSLDE-TLDREVLL 599
Cdd:pfam12128 519 ------QSALDELELQLFPQ------AGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElNLYGVKLD 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 600 LLQGPTPEQLSLEfKSLISRLKReFKEDgltfLTAIRSLTENSETQEA-------NTDLKMQGLEVQLEQRRTDWIRSLE 672
Cdd:pfam12128 587 LKRIDVPEWAASE-EELRERLDK-AEEA----LQSAREKQAAAEEQLVqangeleKASREETFARTALKNARLDLRRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 673 QLDQYRDSLERELlkmASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRlktplDNREASSQTPDHLQQVVEELDGPSL 752
Cdd:pfam12128 661 EKQSEKDKKNKAL---AERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE-----QKREARTEKQAYWQVVEGALDAQLA 732
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207171629 753 EWDEEYVLSESPPLQEL-GPDQQM---LEELCCDEEVLQALKQEEEEPTETVSDKEK 805
Cdd:pfam12128 733 LLKAAIAARRSGAKAELkALETWYkrdLASLGVDPDVIAKLKREIRTLERKIERIAV 789
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
366-535 |
2.71e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 366 LQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQ----KEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMER 441
Cdd:pfam01576 361 LTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 442 ENQSLISKIAALQEENMKVTLEA---------------EELQKKMN------DLCDLNADLQVQIHSFDAILADKESLIQ 500
Cdd:pfam01576 441 ELESVSSLLNEAEGKNIKLSKDVsslesqlqdtqellqEETRQKLNlstrlrQLEDERNSLQEQLEEEEEAKRNVERQLS 520
|
170 180 190
....*....|....*....|....*....|....*
gi 1207171629 501 EKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQ 535
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
366-768 |
2.77e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 366 LQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVeemklsltsSEESRAQAAAQRKQMerenqs 445
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDM---------LEDSNTQIEQLRKMM------ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 446 lISKIAALQEENMKVTLEAEELQKKMNDlcdlnADLQVQIHsFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRA 525
Cdd:pfam15921 180 -LSHEGVLQEIRSILVDFEEASGKKIYE-----HDSMSTMH-FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 526 D-KNKLESQMQMMQP---------DVTIPGLSLSVAYRLNQtsSGSLQTELALAQNplEGLEHLSTSVCFASSLDETldr 595
Cdd:pfam15921 253 EsQNKIELLLQQHQDrieqlisehEVEITGLTEKASSARSQ--ANSIQSQLEIIQE--QARNQNSMYMRQLSDLEST--- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 596 evllllqgptpeqlslefkslISRLKREFKEDGLTFLTAIRSLTE-----NSETQEA------------NTDLKMQGLEV 658
Cdd:pfam15921 326 ---------------------VSQLRSELREAKRMYEDKIEELEKqlvlaNSELTEArterdqfsqesgNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 659 QLEQRRTDWirSLEQLDQYR------------DSLERELLKmaSNMRRSRTEILHLSVKVQEQENQKQQLR--------- 717
Cdd:pfam15921 385 DLHKREKEL--SLEKEQNKRlwdrdtgnsitiDHLRRELDD--RNMEVQRLEALLKAMKSECQGQMERQMAaiqgknesl 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1207171629 718 EEVDRLKTPLDNreassqTPDHLQQVVEELDGP--SLEWDEEYVLSESPPLQE 768
Cdd:pfam15921 461 EKVSSLTAQLES------TKEMLRKVVEELTAKkmTLESSERTVSDLTASLQE 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
420-738 |
2.78e-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: 45.14 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 420 LSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIhsfdailADKESLI 499
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-------AALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 500 QEKNKQMDElkvavveyssvtelLRADKNKLESQMQMMqpdvtipglsLSVAYRLNQtssgslqtelalaQNPLEGLEHl 579
Cdd:COG4942 86 AELEKEIAE--------------LRAELEAQKEELAEL----------LRALYRLGR-------------QPPLALLLS- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 580 stsvcfASSLDETLDREVLLllqgptpEQLSLEFKSLISRLKREFKEdgltfltairsLTENSETQEANTDLKMQGLEVQ 659
Cdd:COG4942 128 ------PEDFLDAVRRLQYL-------KYLAPARREQAEELRADLAE-----------LAALRAELEAERAELEALLAEL 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207171629 660 LEQRrtdwiRSLEQLDQYRDSLERELlkmasnmrrsRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREASSQTPD 738
Cdd:COG4942 184 EEER-----AALEALKAERQKLLARL----------EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
360-471 |
2.99e-04 |
|
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: 45.50 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 360 QLNNQKLQEEVRKLKQAVENMEDTNQKLIEE------NEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAA 433
Cdd:pfam17380 461 QVERLRQQEEERKRKKLELEKEKRDRKRAEEqrrkilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207171629 434 AQRKQMERENQSLIskiaalQEENMKVT-----LEAEELQKKM 471
Cdd:pfam17380 541 ERRKQQEMEERRRI------QEQMRKATeersrLEAMEREREM 577
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
358-451 |
3.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 358 DLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEM------KL----SLTSSE- 426
Cdd:PRK12704 76 ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELieeqlqELerisGLTAEEa 155
|
90 100 110
....*....|....*....|....*....|....*
gi 1207171629 427 ----------ESRAQAAAQRKQMERENQSLISKIA 451
Cdd:PRK12704 156 keillekveeEARHEAAVLIKEIEEEAKEEADKKA 190
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
292-811 |
4.00e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 292 KEWIEDCRNQGKDLKNDTQQESSKLRDSLSAKRS---ALlnmtsGSLEAFGGEASRADletSDLVFCVADLQLNNQKLQ- 367
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqAY-----QLVRKIAGEVSRSE---AWDVARELLRRLREQRHLa 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 368 EEVRKLKQAVENMEdtnQKLIEEN--EELKTQAKMGQQL-LQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQ 444
Cdd:PRK04863 513 EQLQQLRMRLSELE---QRLRQQQraERLLAEFCKRLGKnLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 445 SLISKIAalqeENMKVTLEAEELQKKMNDLCDlnadlqvqihSFDAILADKESLIQeknkQMDELKVAVVEYSSVTELLR 524
Cdd:PRK04863 590 QLQARIQ----RLAARAPAWLAAQDALARLRE----------QSGEEFEDSQDVTE----YMQQLLERERELTVERDELA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 525 ADKNKLESQM-QMMQPDvtipGLSLSVAYRLNQTSSGSLQTEL---------------------ALAQNPLEGL-EHLST 581
Cdd:PRK04863 652 ARKQALDEEIeRLSQPG----GSEDPRLNALAERFGGVLLSEIyddvsledapyfsalygparhAIVVPDLSDAaEQLAG 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 582 svcfassLDETLdrEVLLLLQGPtPEQlsleFKSliSRLKREFKEDGLTfltairsltenseTQEANTDLKMQGL-EVQL 660
Cdd:PRK04863 728 -------LEDCP--EDLYLIEGD-PDS----FDD--SVFSVEELEKAVV-------------VKIADRQWRYSRFpEVPL 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 661 ------EQRrtdwirsLEQLDQYRDSLERELLKMASN------------------------------MRRSRTEILHLSV 704
Cdd:PRK04863 779 fgraarEKR-------IEQLRAEREELAERYATLSFDvqklqrlhqafsrfigshlavafeadpeaeLRQLNRRRVELER 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 705 KVQEQENQKQQLREEVDRLKTPLD--NR---EASSQTPDHLQQVVEELDGP--SLEWDEEYVLSESPPLQELGPDQQMLE 777
Cdd:PRK04863 852 ALADHESQEQQQRSQLEQAKEGLSalNRllpRLNLLADETLADRVEEIREQldEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
570 580 590
....*....|....*....|....*....|....*
gi 1207171629 778 ElccDEEVLQALKQEEEEPTETVSD-KEKITAKSE 811
Cdd:PRK04863 932 S---DPEQFEQLKQDYQQAQQTQRDaKQQAFALTE 963
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
360-470 |
4.25e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 360 QLNNQKLQEEVRKlKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQM 439
Cdd:PRK09510 70 QQKSAKRAEEQRK-KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAK 148
|
90 100 110
....*....|....*....|....*....|.
gi 1207171629 440 ERENQSLISKIAALQEENMKVtLEAEELQKK 470
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKK-KAEAEAAKK 178
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
283-811 |
4.93e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 283 DLDTYHAIMKEWIEDCRNQGKDLKNDTQQessklrdslsaKRSALLNMTSGSLEAFggeASRADLETSDLVFCVADLQLN 362
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESQN-----------KIELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 363 NQKLQEEVRKLKQAVENMEDTNQKLIEENEElkTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERE 442
Cdd:pfam15921 294 ANSIQSQLEIIQEQARNQNSMYMRQLSDLES--TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 443 NQSLISK----IAALQEENMKVTLEAEElQKKMNDLCDLNA-----------DLQVQIHSFDAILADKES---------- 497
Cdd:pfam15921 372 SGNLDDQlqklLADLHKREKELSLEKEQ-NKRLWDRDTGNSitidhlrreldDRNMEVQRLEALLKAMKSecqgqmerqm 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 498 -LIQEKNKQMDELKVAVVEYSSVTELLRADKNKLES-QMQMMQPDVTIPGL--SLSVAYRLNQTSSGSLQTELALAQNPL 573
Cdd:pfam15921 451 aAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSERTVSDLtaSLQEKERAIEATNAEITKLRSRVDLKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 574 EGLEHLST---------SVCFASSLDETLDREVLLLLQ-------------GPTPEQLSLEfkslISRLKREFKEDGLTf 631
Cdd:pfam15921 531 QELQHLKNegdhlrnvqTECEALKLQMAEKDKVIEILRqqienmtqlvgqhGRTAGAMQVE----KAQLEKEINDRRLE- 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 632 LTAIRSLTENSETQEANTDLKMQGLE---VQLEQRRTDWIRSLEQLDQYRDSLERELlkmasnmRRSRTEILHLS----V 704
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKDIKQERDQLLNEV-------KTSRNELNSLSedyeV 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 705 KVQEQENQKQQLREEVDRLKTPLDNREASSQTPDHLQQVVEELDGPSLEWD---EEYVLSESPPLQELGPDQQMLEELCC 781
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDALQSKIQFLEEAMT 758
|
570 580 590
....*....|....*....|....*....|....*
gi 1207171629 782 DEEVLQALKQEE-----EEPTETVSDKEKITAKSE 811
Cdd:pfam15921 759 NANKEKHFLKEEknklsQELSTVATEKNKMAGELE 793
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
291-747 |
4.97e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 291 MKEWIEdcRNQGKDLKNDTQQESSKLRDSLSAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEV 370
Cdd:pfam05557 71 LREQAE--LNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 371 RKLKQAVENME-------DTNQKLIEENEELKTQA-------KMGQQL-----LQKEK------------------MLKE 413
Cdd:pfam05557 149 SEAEQLRQNLEkqqsslaEAEQRIKELEFEIQSQEqdseivkNSKSELaripeLEKELerlrehnkhlnenienklLLKE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 414 EVEEMKLSLTSSEESRAQAaaqrkqmerenqsliskiAALQEENMKVTLEAEELQKKMNDLC-------DLNADLqVQIH 486
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEA------------------ATLELEKEKLEQELQSWVKLAQDTGlnlrspeDLSRRI-EQLQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 487 SFDAILADK----ESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVtipgLSLSVAYRLNQTSSGSL 562
Cdd:pfam05557 290 QREIVLKEEnsslTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV----LLLTKERDGYRAILESY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 563 QTELALAQNPLEGLEHLSTSvcfASSLDETLDREVLLLLQGPTPEQLSLEFKSLISRLKREfkedgLTFLTAIRSLTENS 642
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEA---EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE-----LQALRQQESLADPS 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 643 ETQEANTDLKMQGLEVQLEQRRTDwirslEQLDQYRDSLERELLKMASNMrrSRTEILHLS-----VKVQEQENQKQQLR 717
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLR-----EQKNELEMELERRCLQGDYDP--KKTKVLHLSmnpaaEAYQQRKNQLEKLQ 510
|
490 500 510
....*....|....*....|....*....|
gi 1207171629 718 EEVDRLKTPLDNREASSQTPDHLQQVVEEL 747
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPETTSTM 540
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
366-488 |
5.30e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 366 LQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEmklSLTSSEESRAQAAAQRKQMERENQS 445
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIK---ALQALREELNELKAEIAELKAEAES 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207171629 446 LISKIAALQE--ENMKVTLEAE--ELQKKMNDLCDLNADLQVQIHSF 488
Cdd:pfam07926 83 AKAELEESEEswEEQKKELEKElsELEKRIEDLNEQNKLLHDQLESL 129
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
364-515 |
5.67e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 364 QKLQEEVRK---LKQAVENMEDTNQKLIEENEELKTQA----KMGQQLLQKEKMLKEEVEEMKLS--LTSSEESRAQAAA 434
Cdd:PTZ00121 1640 KKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAeeakKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAE 1719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 435 QRKQMERENQSLISKIAALQEENMKvtlEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVV 514
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKK---KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
|
.
gi 1207171629 515 E 515
Cdd:PTZ00121 1797 D 1797
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
361-474 |
8.51e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 361 LNNQKLQEEVRKLKQAVENMEDTNQ----KLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKlsltSSEESRAQAAAQR 436
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQerqkKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK----QAEQAAKQAEEKQ 118
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207171629 437 KQMEREnqsliskiAALQEENMKVTLEAEELQKKMNDL 474
Cdd:TIGR02794 119 KQAEEA--------KAKQAAEAKAKAEAEAERKAKEEA 148
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
262-799 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 262 EDSGLEELCNMLDPERKDISIDLDTY--------------------HAIMKEWIEDCRNQGKDLKND---TQQESSKLRD 318
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYeeqreqaretrdeadevleeHEERREELETLEAEIEDLRETiaeTEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 319 SLSAKRSALLNMTSgSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQA 398
Cdd:PRK02224 280 EVRDLRERLEELEE-ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 399 KMgqqllqkekmLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLN 478
Cdd:PRK02224 359 EE----------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 479 ADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQmmqpdvtipglslsvayrlnqts 558
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE----------------------- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 559 sgSLQTELALAQNPLEGLEHLSTSVCFASSLDETLDREVLLLLQGPTpeqlSLEFKSLISRLKREFKEDgltfltairSL 638
Cdd:PRK02224 486 --DLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRE----TIEEKRERAEELRERAAE---------LE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 639 TENSETQEANTDLKMQGLEVQ-----LEQRRTDWIRSLEQLDQYRDSLE------------RELLKMASNMRRSRTEilh 701
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAReevaeLNSKLAELKERIESLERIRTLLAaiadaedeierlREKREALAELNDERRE--- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 702 lsvKVQEQENQKQQLREEVD--RLKTPLDNREassQTPDHLQQVVEELDGPSLEWDE-----EYVLSESPPLQELGPDQQ 774
Cdd:PRK02224 628 ---RLAEKRERKRELEAEFDeaRIEEAREDKE---RAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEELRERRE 701
|
570 580
....*....|....*....|....*
gi 1207171629 775 MLEELCcdeEVLQALKQEEEEPTET 799
Cdd:PRK02224 702 ALENRV---EALEALYDEAEELESM 723
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-482 |
1.42e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 292 KEWIEDCRNQGKDLKNDTqqessKLRDSLSAKRSALLNmtsGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVR 371
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDL-----KEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 372 KLKQAVENMEDTNQKLIEENEELKTQAkmgQQLLQKEKMLKEEVEEMKlSLTSSEESRAQAAAQRKQMEREnqsliskIA 451
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEE-------IR 968
|
170 180 190
....*....|....*....|....*....|.
gi 1207171629 452 ALQEENMKVTLEAEELQKKMNDLCDLNADLQ 482
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
366-530 |
1.48e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.57 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 366 LQEEVRKLKQAVENMEDTNQKLIEENEELK-----TQAKMGQQLLQKEKMLKEEVEEMKLSLtssEESRAQAAAQRKQME 440
Cdd:pfam15665 51 LKRRIQTLEESLEQHERMKRQALTEFEQYKrrveeRELKAEAEHRQRVVELSREVEEAKRAF---EEKLESFEQLQAQFE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 441 REnqslisKIAALQEENMKVTLEAEELQKKMNDLcdlnadlqvqihsfdailadKESLIQEKNKQMDELKVAVVEYSSVT 520
Cdd:pfam15665 128 QE------KRKALEELRAKHRQEIQELLTTQRAQ--------------------SASSLAEQEKLEELHKAELESLRKEV 181
|
170
....*....|
gi 1207171629 521 ELLRADKNKL 530
Cdd:pfam15665 182 EDLRKEKKKL 191
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
373-541 |
1.58e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 373 LKQAVENMEDTNQKLIEENEELKTQAKMgQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMEREN-QSLISKIA 451
Cdd:TIGR01612 1535 IKNKFAKTKKDSEIIIKEIKDAHKKFIL-EAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfENKFLKIS 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 452 ALQEENMKVTLEAEELQKKMNDLC--------DLNADLQVQIHSFDAILADKESLIQEKNKQMDEL-------------- 509
Cdd:TIGR01612 1614 DIKKKINDCLKETESIEKKISSFSidsqdtelKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELdseiekieidvdqh 1693
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207171629 510 ----KVAVVEysSVTELLRADKNKLESQMQMMQPDV 541
Cdd:TIGR01612 1694 kknyEIGIIE--KIKEIAIANKEEIESIKELIEPTI 1727
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
356-472 |
2.49e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.61 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 356 VADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELK-----TQAKMGQQLLQKEKM-----LKEEVEEMKLSLtss 425
Cdd:pfam15294 128 SALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalkdLQKEQGAKKDVKSNLkeisdLEEKMAALKSDL--- 204
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207171629 426 EESRAQAAAQRKQMERENQSLISKIAALQEEnmkVTLEAEELQKKMN 472
Cdd:pfam15294 205 EKTLNASTALQKSLEEDLASTKHELLKVQEQ---LEMAEKELEKKFQ 248
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
341-457 |
2.85e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 341 EASRADLETSDLVFCVADLQLNNQKLQEEVRK----LKQAVENMEDTNQK---LIEENEELKTQAKMGQQLLQKekmLKE 413
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaeiAREAQQNYERELVLhaeDIKALQALREELNELKAEIAE---LKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207171629 414 EVEEMKLSLTSSEESraqAAAQRKQMERENQSLISKIAALQEEN 457
Cdd:pfam07926 79 EAESAKAELEESEES---WEEQKKELEKELSELEKRIEDLNEQN 119
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
365-510 |
2.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 365 KLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAqaaaqrkqMERENQ 444
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA--------LQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 445 SLISKIAALQEENMKVTLEAEELQKKM----NDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELK 510
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELaeleAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
356-473 |
2.98e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 356 VADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIE-ENEELKTQAkmgqqlLQKEKMLKEEVEEMklsltssEESRAQAAA 434
Cdd:COG1842 46 LAQVIANQKRLERQLEELEAEAEKWEEKARLALEkGREDLAREA------LERKAELEAQAEAL-------EAQLAQLEE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207171629 435 QRKQMERENQSLISKIAAL--QEENMKVTLEAEELQKKMND 473
Cdd:COG1842 113 QVEKLKEALRQLESKLEELkaKKDTLKARAKAAKAQEKVNE 153
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
366-729 |
3.14e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 366 LQEEVRKLKQAVENMEDTNQKliEENEELKTQAKMGQQLLQKEKMLKE------EVEEMKLSLTSSEESRAQAAAQRKQM 439
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAK--KEEELQAALARLEEETAQKNNALKKireleaQISELQEDLESERAARNKAEKQRRDL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 440 ERENQSLISKI-------AALQEENMKVTLEAEELQKKMNDLCDlNADLQVQ---IHSFDAILADKESLIQ--------E 501
Cdd:pfam01576 298 GEELEALKTELedtldttAAQQELRSKREQEVTELKKALEEETR-SHEAQLQemrQKHTQALEELTEQLEQakrnkanlE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 502 KNKQM-----DELKVAVVEYSSVTELLRADKNKLESQMQMMQpdvtipgLSLSVAYRLNQT---SSGSLQTELALAQNPL 573
Cdd:pfam01576 377 KAKQAlesenAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ-------ARLSESERQRAElaeKLSKLQSELESVSSLL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 574 EGLE-HLSTSVCFASSLDETLdREVLLLLQGPTPEQLSLEfksliSRLkREFKEDGltflTAIRSLTENSETQEANTDLK 652
Cdd:pfam01576 450 NEAEgKNIKLSKDVSSLESQL-QDTQELLQEETRQKLNLS-----TRL-RQLEDER----NSLQEQLEEEEEAKRNVERQ 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207171629 653 MQGLEVQLeqrrTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDN 729
Cdd:pfam01576 519 LSTLQAQL----SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDH 591
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
363-510 |
3.30e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 363 NQKLQEEVRKLKQAVENMEDTNQK---LIEENEELKTQAKmgqQLLQKEKMLKEEVEEMKLSLTSSEE-SRAQAAAQRKQ 438
Cdd:COG1340 49 NAQVKELREEAQELREKRDELNEKvkeLKEERDELNEKLN---ELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQ 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171629 439 M------ERENQsLISKIAALQEEnMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELK 510
Cdd:COG1340 126 QtevlspEEEKE-LVEKIKELEKE-LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
342-500 |
3.45e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 342 ASRADLETsDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIE---ENEELKTQAKMGQQllqKEKMLKEEVEEM 418
Cdd:pfam01576 770 AAKKKLEL-DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEaraSRDEILAQSKESEK---KLKNLEAELLQL 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 419 KLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEEnmKVTLEA---------EELQKKMNDLCDLNADLQVQIHSFD 489
Cdd:pfam01576 846 QEDLAASERARRQAQQERDELADEIASGASGKSALQDE--KRRLEAriaqleeelEEEQSNTELLNDRLRKSTLQVEQLT 923
|
170
....*....|.
gi 1207171629 490 AILADKESLIQ 500
Cdd:pfam01576 924 TELAAERSTSQ 934
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
368-535 |
3.47e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.24 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 368 EEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQllQKEKMLKEEVEEMklsltsseesraqaAAQRKQMErenqsli 447
Cdd:pfam15818 14 EELRMRREAETQYEEQIGKIIVETQELKWQKETLQN--QKETLAKQHKEAM--------------AVFKKQLQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 448 SKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQ-------EKNKQMDELKVAVVEYSSVT 520
Cdd:pfam15818 71 MKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQlhllakeDHHKQLNEIEKYYATITGQF 150
|
170
....*....|....*
gi 1207171629 521 ELLRADKNKLESQMQ 535
Cdd:pfam15818 151 GLVKENHGKLEQNVQ 165
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
345-505 |
3.52e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 345 ADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVEnmedTNQKLIEEneelktQAKMGQQLLQKEKMLKEEveemKLSLTS 424
Cdd:TIGR00606 813 AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE----LNRKLIQD------QQEQIQHLKSKTNELKSE----KLQIGT 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 425 SEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKmndlcdlNADLQVQIHSFDAILADKESLIQEKNK 504
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE-------KEELISSKETSNKKAQDKVNDIKEKVK 951
|
.
gi 1207171629 505 Q 505
Cdd:TIGR00606 952 N 952
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
357-774 |
4.58e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 357 ADLQLNNQKLQEEVRKL----KQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQA 432
Cdd:TIGR00606 415 ADLQSKERLKQEQADEIrdekKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 433 AAQRKQMErenqsliskIAALQEENMKVTLEAEELQKKMNDLcDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVA 512
Cdd:TIGR00606 495 LTETLKKE---------VKSLQNEKADLDRKLRKLDQEMEQL-NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 513 VVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAyrlnQTSSGSLQTELALAQNPLEGLEHLSTSVCFASSLDET 592
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 593 LDR---------EVLLLLQGPTP------EQLSLEFKSLISRLKREFKEDG--LTFLTAIRSLTENSETQEANTDLKMQg 655
Cdd:TIGR00606 641 LERlkeeiekssKQRAMLAGATAvysqfiTQLTDENQSCCPVCQRVFQTEAelQEFISDLQSKLRLAPDKLKSTESELK- 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 656 levQLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQ--------------------KQQ 715
Cdd:TIGR00606 720 ---KKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesakvcltdvtiMER 796
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207171629 716 LREEVDRLKTPLDNREASSQTPDhLQQVVEELDGPSLEWDEEY--VLSESPPLQELGPDQQ 774
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSD-LDRTVQQVNQEKQEKQHELdtVVSKIELNRKLIQDQQ 856
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
360-535 |
5.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 360 QLNNQ--KLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKmgqQLLQKEKMLKEEVEEMKLSLTSSEE-SRAQAAAQR 436
Cdd:COG1340 47 ELNAQvkELREEAQELREKRDELNEKVKELKEERDELNEKLN---ELREELDELRKELAELNKAGGSIDKlRKEIERLEW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 437 KQM------ERENQsLISKIAALQE--ENMKVTL-----------EAEELQKKMNDLCDLNADLQVQIHSFDAILADKES 497
Cdd:COG1340 124 RQQtevlspEEEKE-LVEKIKELEKelEKAKKALekneklkelraELKELRKEAEEIHKKIKELAEEAQELHEEMIELYK 202
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207171629 498 LIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQ 535
Cdd:COG1340 203 EADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
364-469 |
6.08e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 364 QKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMlkeeveemklSLTSSEESRAQAAAQRKQMEren 443
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAA----------TLSEAAREKKEKELQKKVQE--- 73
|
90 100
....*....|....*....|....*.
gi 1207171629 444 qsLISKIAALQEENMKvtLEAEELQK 469
Cdd:smart00935 74 --FQRKQQKLQQDLQK--RQQEELQK 95
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
359-403 |
6.49e-03 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 36.87 E-value: 6.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1207171629 359 LQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQ 403
Cdd:COG3074 23 LQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQE 67
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
335-538 |
8.20e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.27 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 335 LEAFGGEASRADLEtsdlvfcVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKmlkee 414
Cdd:pfam05010 10 LEKARNEIEEKELE-------INELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 415 veemklsltsseesrAQAAAQRKQMERENQSLISKIaalqeENMKVTLEA----EELQKKmndlC--DLNADLQVQIHSF 488
Cdd:pfam05010 78 ---------------DQALADLNSVEKSFSDLFKRY-----EKQKEVISGykknEESLKK----CaqDYLARIKKEEQRY 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207171629 489 DAILADKESLIQEKNKQMDELKvavVEYSSVTELLRADKNKLESQMQMMQ 538
Cdd:pfam05010 134 QALKAHAEEKLDQANEEIAQVR---SKAKAETAALQASLRKEQMKVQSLE 180
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
403-742 |
8.27e-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: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 403 QLLQK--EKMLKEEVEEMKLSLTSS---EESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDL 477
Cdd:pfam07888 30 ELLQNrlEECLQERAELLQAQEAANrqrEKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 478 NADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTipglSLSVAYRLNQT 557
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK----QLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 558 SSGSLQTEL-----ALAQNPLEGLEHLSTSVCFASSLDETLDREVLLllqgptpEQLSLEFKSLISRL-----KREFKED 627
Cdd:pfam07888 186 ELRSLSKEFqelrnSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-------EALLEELRSLQERLnaserKVEGLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 628 GLTFLTAIRSLTE----NSETQEANTDLKMQGLEVQLEQRRTDWIRSLEQLDQYRDSLERELLKMAsnmrrsrTEILHLS 703
Cdd:pfam07888 259 ELSSMAAQRDRTQaelhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLS-------AELQRLE 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 1207171629 704 VKVQEQENQKQQLREEVDRLKTplDNREASSQTPDHLQQ 742
Cdd:pfam07888 332 ERLQEERMEREKLEVELGREKD--CNRVQLSESRRELQE 368
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
365-533 |
8.46e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 365 KLQEEVRK-LKQAVENMEDTNQKLIEENEELKTQAkmgQQLLQKEKMLKEEVEEMKlSLTSSEESRAQAaaqrkqmerEN 443
Cdd:smart00787 140 KLLEGLKEgLDENLEGLKEDYKLLMKELELLNSIK---PKLRDRKDALEEELRQLK-QLEDELEDCDPT---------EL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171629 444 QSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIqEKNKQMDELKVavveyssvtELL 523
Cdd:smart00787 207 DRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL-EQCRGFTFKEI---------EKL 276
|
170
....*....|
gi 1207171629 524 RADKNKLESQ 533
Cdd:smart00787 277 KEQLKLLQSL 286
|
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