|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
171-481 |
1.88e-146 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 425.49 E-value: 1.88e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 171 EKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQDQKCAR-SNLDPLFDNYITSLRRQLEVLVSDQARLQAERNHMQ 249
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 250 DILEGFKKKYEEEVGCRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKALYLEEIQLLQSHISETSVIVKMD 329
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 330 NSRDLNLDGIIAEVKAQYEEVARRSRADVEAWYQTKYEEMRVTAGQHCDNLRNTRDEINELTRLIQRLKTEIEHSKAQCA 409
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 344249344 410 KLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGLDIEIATYRQLLEGEEIR 481
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-167 |
5.27e-46 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 159.44 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 16 SFSSCSAMTPqNLNRFQASSVSCRSGSGFRGLGC------FGSRSV-NFG---SSSPRIAVGCSRPIrYGVGFGAGNGMA 85
Cdd:pfam16208 1 GFSSCSAVVP-SRSRRSYSSVSSSRRGGGGGGGGggggggFGSRSLyNLGgskSISISVAGGGSRPG-SGFGFGGGGGGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 86 FGSGDGCGVGLGFRASSGVGLGFGAGSSLGYGFGGPAFGGPgfgyriGGIGGPSAPS--ITTVTVNQSLLTPLNLEIDPN 163
Cdd:pfam16208 79 FGGGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGR------GGFGGPPCPPggIQEVTVNQSLLQPLNLEIDPE 152
|
....
gi 344249344 164 AQRV 167
Cdd:pfam16208 153 IQRV 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
157-413 |
1.37e-10 |
|
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: 64.27 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 157 NLEIDPNAQRVKKDEKE-QIKTLNNKFASFIDKVRFLEQQNKLLETKwsfLQDQKcarsNLDPLFDNYITSLRRQLEVLV 235
Cdd:TIGR04523 353 NSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE----KLNQQKDEQIKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 236 SDQARLQAERN----------------------------HMQDILEGFKKKYEEEvgcRANAEN---EFVALKKDVDTAF 284
Cdd:TIGR04523 426 KEIERLKETIIknnseikdltnqdsvkeliiknldntreSLETQLKVLSRSINKI---KQNLEQkqkELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 285 LNKSDLEANVDALAQEVEFLKalylEEIQLLQSHI----SETSVIVKMDNSRDLNLDgiiaevKAQYEEVARRSRADVEA 360
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLK----EKIEKLESEKkekeSKISDLEDELNKDDFELK------KENLEKEIDEKNKEIEE 572
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 344249344 361 WYQT------KYEEMRVTAGQHCDNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEA 413
Cdd:TIGR04523 573 LKQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-457 |
4.80e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 169 KDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQDQKCARSNLDPLFDNYITSLRRQLEVLVSDQARLQAERNHM 248
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 249 QDILEGFKKKYEEEVGCRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKALYLEEIQLLQSHISETSVIVKM 328
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 329 -----DNSRDLNLDGIIAEVK-AQYEEVARRSRADVEAWYQtKYEEMRVTAGQHCDNLRNTRDEINELTRLIQRLKTEIE 402
Cdd:TIGR02168 840 ledleEQIEELSEDIESLAAEiEELEELIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344249344 403 HSKAQCAKLEAAVAEAEQQ-----------GEAALNDAKCKLADLEGALQQAKQDMARQLREYQEL 457
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-501 |
1.24e-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: 61.62 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 156 LNLEIDPNAQRVKKDEKEQIKtlnnkfasfidKVRFLEQQNKLLETK-WSFLQDQKCARSNLDPLfDNYITSLRRQLEVL 234
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREK-----------AERYQALLKEKREYEgYELLKEKEALERQKEAI-ERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 235 VSDQARLQAERNHMQDILEGFKKKYEEEvgcranAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKalylEEIQL 314
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE----ERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 315 LQSHISETSvivkmdnSRDLNLDGIIAEVKAQYEEVARRSRADveawyQTKYEEMRVTAGQHCDNLRNTRD--------- 385
Cdd:TIGR02169 327 LEAEIDKLL-------AEIEELEREIEEERKRRDKLTEEYAEL-----KEELEDLRAELEEVDKEFAETRDelkdyrekl 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 386 -----EINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQ---QGEAALNDAKCKLADLEGALQQAKQDMARQLREY--- 454
Cdd:TIGR02169 395 eklkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydl 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 344249344 455 --------QELMNAKLGLDIEIATYRQLLEGEeiricEGVGPVNISVSSSRGGVL 501
Cdd:TIGR02169 475 keeydrveKELSKLQRELAEAEAQARASEERV-----RGGRAVEEVLKASIQGVH 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
224-482 |
1.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 224 ITSLRRQLEVLvSDQARlQAERnhmqdilegfKKKYEEEvgcranaenefvALKKDVDTAFLNKSDLEANVDALAQEVEF 303
Cdd:COG1196 195 LGELERQLEPL-ERQAE-KAER----------YRELKEE------------LKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 304 LKAlyleEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRADVEAWYQTKYEEMRVTAGqhcdnLRNT 383
Cdd:COG1196 251 LEA----ELEELEAELAE--------------LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD-----IARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 384 RDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAA---LNDAKCKLADLEGALQQAKQDMARQLREYQELMNA 460
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260
....*....|....*....|..
gi 344249344 461 KLGLDIEIATYRQLLEGEEIRI 482
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAE 409
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
267-590 |
1.69e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 267 ANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKALY---LEEIQLLQSHISETSVivkmdnsrdlNLDGIIAEV 343
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 344 KAQYEEVARRSRADVEAWYQTKYEEMRVTAG------QHCDNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAE 417
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 418 AEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGLDIEIATYRQLLEGEEIRICEGVGPVNISVSSSR 497
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 498 GGVLCGPESLVSGSSLSRNCGVTFSSSSGIRTTGGVLTSSCLRAGGDLLSSGARGGSVLVSDTCAPSIPCPLPTEGGFSS 577
Cdd:COG3883 242 AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGA 321
|
330
....*....|...
gi 344249344 578 CSGGRGNRSSSVR 590
Cdd:COG3883 322 VVGGASAGGGGGS 334
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-482 |
4.62e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 175 IKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQDQKCARSNLDPLFDNYITSLRRQLEVLVSDQARLQAERNHMQDILEg 254
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT- 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 255 fkkkyeeevgcraNAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKalylEEIQLLQSHISETSVIVkmdnsRDL 334
Cdd:TIGR02168 758 -------------ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK----EELKALREALDELRAEL-----TLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 335 NLDGiiaevkAQYEEVARRSRADVEAWYQTkyeemrvtagqhcdnLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAA 414
Cdd:TIGR02168 816 NEEA------ANLRERLESLERRIAATERR---------------LEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344249344 415 VAEAEQ---QGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNaklgldiEIATYRQLLEGEEIRI 482
Cdd:TIGR02168 875 LEALLNeraSLEEALALLRSELEELSEELRELESKRSELRRELEELRE-------KLAQLELRLEGLEVRI 938
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
227-493 |
1.06e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 227 LRRQLEVLvsdQARL-QAERNhmqdiLEGFKKKyeeevgcranaeNEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLK 305
Cdd:COG3206 180 LEEQLPEL---RKELeEAEAA-----LEEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 306 ALYleeiQLLQSHISETSvivkmDNSRDLNLDGIIAEVKAQYEEVARRsRADVEAWYQTKYEEMRvtagqhcdnlrNTRD 385
Cdd:COG3206 240 ARL----AALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVI-----------ALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 386 EINELTRLIQRLKTEIEhskaqcAKLEAAVAEAEQQgeaalndakckLADLEGALQQAKQ---DMARQLREYQELMNakl 462
Cdd:COG3206 299 QIAALRAQLQQEAQRIL------ASLEAELEALQAR-----------EASLQAQLAQLEArlaELPELEAELRRLER--- 358
|
250 260 270
....*....|....*....|....*....|....
gi 344249344 463 glDIEIA--TYRQLLEG-EEIRICEGVGPVNISV 493
Cdd:COG3206 359 --EVEVAreLYESLLQRlEEARLAEALTVGNVRV 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
267-484 |
1.13e-07 |
|
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: 53.00 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 267 ANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKALyLEEIQLLQSHISetsvivkmdNSRDLnlDGIIAEVkaq 346
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVR---------NNKEY--EALQKEI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 347 yeEVARRSRADVEawyqtkyeemrvtagqhcdnlrntrDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAAL 426
Cdd:COG1579 99 --ESLKRRISDLE-------------------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344249344 427 NDAKCKLADLEGALQQAKQDM-ARQLREYQELMNAKLGL---------------DIEIATYRQLLEGEEIRICE 484
Cdd:COG1579 152 AELEAELEELEAEREELAAKIpPELLALYERIRKRKNGLavvpveggacggcfmELPPQELNEIRAADEIVRCP 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
224-457 |
4.34e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 224 ITSLRRQLEVLVSDQARLQAERNHMQDILEGFKKKYEEevgcranAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEF 303
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 304 LKAlyleEIQLLQSHISE-TSVIVKM-----DNSRDLN---LDGIIAEVKAQYEEVAR-RSR-ADVEA-----WYQTKYE 367
Cdd:TIGR02169 756 VKS----ELKELEARIEElEEDLHKLeealnDLEARLShsrIPEIQAELSKLEEEVSRiEARlREIEQklnrlTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 368 EmrvtagqhcDNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEqqgeAALNDAKCKLADLEGALQQAKQDM 447
Cdd:TIGR02169 832 E---------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE----AALRDLESRLGDLKKERDELEAQL 898
|
250
....*....|
gi 344249344 448 ARQLREYQEL 457
Cdd:TIGR02169 899 RELERKIEEL 908
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-480 |
5.71e-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: 52.72 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 153 LTPLNLEIDPNAQRVKKDE------KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQDQKcarSNLDplfdNYITS 226
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEvelnklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK---EELE----NELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 227 LRRQLEVLVS--DQARLQAER-NHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEF 303
Cdd:TIGR04523 178 LEKEKLNIQKniDKIKNKLLKlELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 304 LKALYLEEIQLLQSHISEtsviVKMDNSRDLNLDGIIAEVKAQYEEVARRSRAD----VEAWYQTKYEEMRVTAGQhcdn 379
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkeLKSELKNQEKKLEEIQNQ---- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 380 LRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEgALQQAKQDMARQLREYQELMN 459
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQ 408
|
330 340
....*....|....*....|....
gi 344249344 460 AKlglDIEIATYRQ---LLEgEEI 480
Cdd:TIGR04523 409 QK---DEQIKKLQQekeLLE-KEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-479 |
6.12e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 190 RFLEQQNKLLETKWSFLQDQkcarsnldplfdnyITSLRRQLEVLVSDQARLQAERNHMQDILEGFKKKYEEEVGCRANA 269
Cdd:TIGR02168 214 RYKELKAELRELELALLVLR--------------LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 270 ENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFLKALYLE---EIQLLQSHISETSVIVKMdnsrdlnLDGIIAEVKAQ 346
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAE-------LEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 347 YEEVarrsRADVEAwYQTKYEEMRVTAGQHCDNLRNTRDEINELTR-------LIQRLKTEIEHSKAQCAKLEAAVAEAE 419
Cdd:TIGR02168 353 LESL----EAELEE-LEAELEELESRLEELEEQLETLRSKVAQLELqiaslnnEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344249344 420 QQGEAA--------LNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGLDIEIATYRQLLEGEE 479
Cdd:TIGR02168 428 KKLEEAelkelqaeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
380-460 |
6.77e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 380 LRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQ---GEAALNDAKCKLADLEGALQQAKQDMARQLREYQE 456
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 344249344 457 LMNA 460
Cdd:COG4942 109 LLRA 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-442 |
9.93e-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: 48.90 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 150 QSLLTPLNLEIdpnaqRVKKDEKEQIKTLNNKFASFIDKvrfLEQQNKLLETKWSFLQDQKCARSNldplfdnYITSLRR 229
Cdd:TIGR02168 266 EEKLEELRLEV-----SELEEEIEELQKELYALANEISR---LEQQKQILRERLANLERQLEELEA-------QLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 230 QLEVLVSDQARLQAERNHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDT------------AFLN---------KS 288
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaqlelqiASLNneierlearLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 289 DLEANVDALAQEVEFL-KALYLEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRsradveawyqtkye 367
Cdd:TIGR02168 411 RLEDRRERLQQEIEELlKKLEEAELKELQAELEE--------------LEEELEELQEELERLEEA-------------- 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344249344 368 emrvtagqhcdnLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAE--QQGEAALNDAKCKLADLEGALQQ 442
Cdd:TIGR02168 463 ------------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfSEGVKALLKNQSGLSGILGVLSE 527
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
170-479 |
1.44e-05 |
|
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: 48.25 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 170 DEKEQIKTLN---NKFASFI----------DKVRF-LEQQNKLLETKWSFLQDQKCARSNLdplfdnyITSLRRQL---- 231
Cdd:pfam01576 170 EEEEKAKSLSklkNKHEAMIsdleerlkkeEKGRQeLEKAKRKLEGESTDLQEQIAELQAQ-------IAELRAQLakke 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 232 EVLVSDQARLQAERNH----------MQDILEGFKKKYEEEVGCRANAENEFVALKKDVDTAflnKSDLEANVDALA--- 298
Cdd:pfam01576 243 EELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKAEKQRRDLGEELEAL---KTELEDTLDTTAaqq 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 299 -------QEVEFLK-ALYLE----EIQLLQSHISETSVIVKMdnsrdlnldgiiaevkAQYEEVARRSRADVEAWYQTky 366
Cdd:pfam01576 320 elrskreQEVTELKkALEEEtrshEAQLQEMRQKHTQALEEL----------------TEQLEQAKRNKANLEKAKQA-- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 367 eemrvtagqhcdnLRNTRDEINELTRLIQRLKTEIEHSK----AQCAKLEAAVAEAEQQ----------GEAALNDAKCK 432
Cdd:pfam01576 382 -------------LESENAELQAELRTLQQAKQDSEHKRkkleGQLQELQARLSESERQraelaeklskLQSELESVSSL 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344249344 433 LADLEGALQQAKQDMAR---QLREYQELMN----AKLG-------LDIEIATYRQLLEGEE 479
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSlesQLQDTQELLQeetrQKLNlstrlrqLEDERNSLQEQLEEEE 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
220-461 |
1.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 220 FDNyitslRRQLEVLVSDQARLQAERNHMQDILEGFKKKyeeevgcRANAENEFVALKKDVDTAFlnksdLEANVDALAQ 299
Cdd:COG4913 606 FDN-----RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQERREALQRLAEYSW-----DEIDVASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 300 EVEFLKalylEEIQLLQShisetsvivkmdNSRDLnldgiiAEVKAQYEEVARRsradveawyqtkyeemrvtagqhcdn 379
Cdd:COG4913 669 EIAELE----AELERLDA------------SSDDL------AALEEQLEELEAE-------------------------- 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 380 LRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAALN---DAKCKLADLEGALQQAKQDMARQLREYQE 456
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVERELRENLEERIDALRA 780
|
....*
gi 344249344 457 LMNAK 461
Cdd:COG4913 781 RLNRA 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
221-555 |
2.04e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 221 DNYITSLRRQLEVLVSDQARLQAERNHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDTAflnKSDLEANVDALAqe 300
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 301 vEFLKALYLEEIQ------LLQSH-----ISETSVIVKMdNSRDLNldgIIAEVKAQYEEVARRsRADVEAwyqtKYEEM 369
Cdd:COG3883 90 -ERARALYRSGGSvsyldvLLGSEsfsdfLDRLSALSKI-ADADAD---LLEELKADKAELEAK-KAELEA----KLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 370 RVTAGQHCDNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMAR 449
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 450 QLREYQELMNAKLGLDIEIATYRQLLEGEEIRICEGVGPVNISVSSSRGGVLCGPESLVSGSSLSRNCGVTFSSSSGIRT 529
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGA 319
|
330 340
....*....|....*....|....*.
gi 344249344 530 TGGVLTSSCLRAGGDLLSSGARGGSV 555
Cdd:COG3883 320 GAVVGGASAGGGGGSGGGGGSSGGGS 345
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
225-466 |
3.91e-05 |
|
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: 46.71 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 225 TSLRRQLEVLVSDQARLQAERNHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEFL 304
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 305 KalylEEIQllqshisetSVIVKMDNSRDL--NL-------DGIIAEVK---AQYEEvaRRSRADVEAwyqtKYEEMRVT 372
Cdd:pfam01576 579 Q----QELD---------DLLVDLDHQRQLvsNLekkqkkfDQMLAEEKaisARYAE--ERDRAEAEA----REKETRAL 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 373 AGQH-CDNLRNTRDEINELTRLiqrLKTEIE---HSKAQCAK----LEAAVAEAEQQGEaalnDAKCKLADLEGALQQAK 444
Cdd:pfam01576 640 SLARaLEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKnvheLERSKRALEQQVE----EMKTQLEELEDELQATE 712
|
250 260
....*....|....*....|..
gi 344249344 445 qdmarqlreyqelmNAKLGLDI 466
Cdd:pfam01576 713 --------------DAKLRLEV 720
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
241-467 |
4.49e-05 |
|
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: 46.71 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 241 LQAERNHMQDILEGFKKKYEEEVGCRANAENEFVAL----KKDVDTAFLnksdLEANVDALAQEveflKALYLEEIQLLQ 316
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTeakiKKLEEDILL----LEDQNSKLSKE----RKLLEERISEFT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 317 SHISETSVIVKMDNSRDLNLDGIIA--EVKAQYEEvarRSRADVEAWYqtkyeemrvtagqhcdnlRNTRDEINELTRLI 394
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEE---KGRQELEKAK------------------RKLEGESTDLQEQI 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344249344 395 QRLKTEIEHSKAQCAK----LEAAVAEAEQQGeAALNDAKCKLADLEGALQQAKQDMA--RQLREYQELMNAKLGLDIE 467
Cdd:pfam01576 225 AELQAQIAELRAQLAKkeeeLQAALARLEEET-AQKNNALKKIRELEAQISELQEDLEseRAARNKAEKQRRDLGEELE 302
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-458 |
9.67e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 223 YITSLRRQLEVLVSDQARLQAERnHMQDILEGFKKKYEEEVGCRANAENEFV-ALKKDVDTAFlnksDLEANVDALAQEV 301
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALP-ALEELEEEELEELLAALGLPPDLSPEELlELLDRIEELQ----ELLREAEELEEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 302 EfLKALYLEEIQLLQShisetsviVKMDNSRDLNLdgiIAEVKAQYEEVARRsRADVEAWYQTKYEEMRVTAGQHcdNLR 381
Cdd:COG4717 364 Q-LEELEQEIAALLAE--------AGVEDEEELRA---ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEE 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344249344 382 NTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEaalndakckLADLEGALQQAKQDMARQLREYQELM 458
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAELRELAEEWAALK 496
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
275-462 |
1.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 275 ALKKDVDTAFLNKSDLEANVDALAQEVEFLKalylEEIQLLQSHIsetsvivkmdnsrdlnldgiiAEVKAQYEEVARRS 354
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAR----EELEQLEEEL---------------------EQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 355 RAdveawYQTKYEEMRVTAGQHCDNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQgeaaLNDAKCKLA 434
Cdd:COG4372 83 EE-----LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELK 153
|
170 180
....*....|....*....|....*...
gi 344249344 435 DLEGALQQAKQDMARQLREYQELMNAKL 462
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-484 |
1.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 221 DNYITSLRRQLEVLvsdqARLQAERNHMQDILegfkkKYEEEVGCR-ANAENEFVALKKDVDTAFLNKSDLEANVDALAQ 299
Cdd:PRK03918 158 DDYENAYKNLGEVI----KEIKRRIERLEKFI-----KRTENIEELiKEKEKELEEVLREINEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 300 EVEFLKALYlEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVaRRSRADVEA--WYQTKYEEMRvtagqhc 377
Cdd:PRK03918 229 EVKELEELK-EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKElkEKAEEYIKLS------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 378 DNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQgEAALNDAKCKLADLEG---ALQQAKQDMAR--QL- 451
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-KKKLKELEKRLEELEErheLYEEAKAKKEEleRLk 378
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 344249344 452 ------------REYQELMNAKLGLDIEIATYRQLLEGEEIRICE 484
Cdd:PRK03918 379 krltgltpekleKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
224-473 |
1.46e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 224 ITSLRRQLEvlvsdqaRLQAERNHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDT-----AFLNK--SDLEANVDA 296
Cdd:COG4942 22 AAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelAALEAelAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 297 LAQEVEFLKALYLEEIQLLQ--SHISETSVIVKMDNSRDLNLDGIIaevkaqYEEVARRSRADVEAwyqtkyeemrvtag 374
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEE-------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 375 qhcdnLRNTRDEINELTRLIQRLKteiehskaqcAKLEAAVAEAEQQG---EAALNDAKCKLADLEGALQQAKQDMARQL 451
Cdd:COG4942 155 -----LRADLAELAALRAELEAER----------AELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|..
gi 344249344 452 REYQELMNAKLGLDIEIATYRQ 473
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAE 241
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
161-479 |
1.54e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 161 DPNAQRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQDQKCARSNLdplFDNYITSLRRQLEVLVSDQAR 240
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIN---EYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 241 LQAERNhmqdilegfkkKYEEevgcranAENEFVALK-KDVD---TAFLNKSDLEANVDalaqeveflkalyleeIQLLQ 316
Cdd:PRK01156 541 LKDKHD-----------KYEE-------IKNRYKSLKlEDLDskrTSWLNALAVISLID----------------IETNR 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 317 SHISETSVIVKMDNSRdlnldgiIAEVKAQYEevarrsraDVEAWYQTKYEEMRvtagQHCDNLRNTRDEINELTRLIQR 396
Cdd:PRK01156 587 SRSNEIKKQLNDLESR-------LQEIEIGFP--------DDKSYIDKSIREIE----NEANNLNNKYNEIQENKILIEK 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 397 LKTEIEHSKAQCAKLEaAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGLDIEIATYRQLLE 476
Cdd:PRK01156 648 LRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLE 726
|
...
gi 344249344 477 GEE 479
Cdd:PRK01156 727 SMK 729
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
378-482 |
2.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 378 DNLRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQ---GEAALNDAKCKLADLEGALQQAKQDMARQLREY 454
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100
....*....|....*....|....*...
gi 344249344 455 QELMNAKLGLDIEIATYRQLLEGEEIRI 482
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
163-482 |
3.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 163 NAQRVKKDEKEQIKTLNNKFASFIDKvrfLEQQNKLLETKwsfLQDQKCARSNLdplfdnyiTSLRRQLEVLVSDQARLQ 242
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEE---LEELNEQLQAA---QAELAQAQEEL--------ESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 243 AERNHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDtaflnksDLEANVDALAQEVEFLKALYLEE--IQLLQSHIS 320
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE-------SLQEELAALEQELQALSEAEAEQalDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 321 ETSVIVKMDNSRDLN---LDGIIAEVKAQYEEVARRSRADVEAWYQTKYEEMRVTAGQHCDNLRNTRDEINELTRLIQRL 397
Cdd:COG4372 195 NAEKEEELAEAEKLIeslPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 398 KTEIEHSKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGLDIEIATYRQLLEG 477
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....*
gi 344249344 478 EEIRI 482
Cdd:COG4372 355 VLELL 359
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
380-461 |
4.45e-04 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 41.40 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 380 LRNTRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGE---AALNDAKCKLADLEGALQQAKQDMARQlreYQE 456
Cdd:pfam05335 61 VEQLEQELREAEAVVQEESASLQQSQANANAAQRAAQQAQQQLEaltAALKAAQANLENAEQVAAGAQQELAEK---TQL 137
|
....*
gi 344249344 457 LMNAK 461
Cdd:pfam05335 138 LEAAK 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
306-478 |
5.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 306 ALYLEEIQLLQSHISE-TSVIVKMDNSRDLnldgiIAEVKAQYEEVARRSRADVEAWYqtkYEEMRVTAGQHCDNLRNTR 384
Cdd:COG4913 613 AALEAELAELEEELAEaEERLEALEAELDA-----LQERREALQRLAEYSWDEIDVAS---AEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 385 DEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQgeaaLNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGL 464
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170
....*....|....
gi 344249344 465 DIEIATYRQLLEGE 478
Cdd:COG4913 761 DAVERELRENLEER 774
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
388-450 |
6.82e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.38 E-value: 6.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344249344 388 NELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQ---GEAALNDAKCKLADLEGALQQAKQDMARQ 450
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-325 |
1.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 165 QRVKKDEKEQIKTLNNKFASFIDKVRFLEQQ-----NKLLETKWSFLQDQKCARSNLDPLFDNYIT------SLRRQLEV 233
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEElaellKELEELGFESVEELEERLKELEPFYNEYLElkdaekELEREEKE 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 234 LVSDQARLQAERNHMQDI----------LEGFKKKYEEEVgcRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEF 303
Cdd:PRK03918 621 LKKLEEELDKAFEELAETekrleelrkeLEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
170 180
....*....|....*....|....*...
gi 344249344 304 LKA------LYLEEIQLLQSHISETSVI 325
Cdd:PRK03918 699 LKEeleereKAKKELEKLEKALERVEEL 726
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
375-462 |
1.17e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 375 QHCDNLRNTRDEINELTR----LIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEaalndakcklaDLEGALQQAKQDMA-- 448
Cdd:pfam13851 5 NHEKAFNEIKNYYNDITRnnleLIKSLKEEIAELKKKEERNEKLMSEIQQENK-----------RLTEPLQKAQEEVEel 73
|
90
....*....|....*....
gi 344249344 449 -RQLREY----QELMNAKL 462
Cdd:pfam13851 74 rKQLENYekdkQSLKNLKA 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
224-457 |
1.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 224 ITSLRRQLEVLVSDQARlQAERNHMQ-DILEGFKKKYEEEVGCRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVE 302
Cdd:COG4717 48 LERLEKEADELFKPQGR-KPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 303 FLKALylEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRAdvEAWYQTKYEEMRVTAGQHCDNLRN 382
Cdd:COG4717 127 LLPLY--QELEALEAELAE--------------LPERLEELEERLEELRELEEE--LEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344249344 383 -TRDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAALNdakckladlegalQQAKQDMARQLREYQEL 457
Cdd:COG4717 189 aTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-------------ELEAAALEERLKEARLL 251
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
378-457 |
2.05e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.22 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 378 DNLRNTRDEINELTRLIQRLKT-------EIEHSKAQCAKLEAAVAEAEQQgeaaLNDAKCKLADLEGALQQAK----QD 446
Cdd:pfam11559 59 ETIRTLEAEIERLQSKIERLKTqledlerELALLQAKERQLEKKLKTLEQK----LKNEKEELQRLKNALQQIKtqfaHE 134
|
90
....*....|.
gi 344249344 447 MARQLREYQEL 457
Cdd:pfam11559 135 VKKRDREIEKL 145
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
333-479 |
2.10e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 333 DLNLDGIIAEVKAQ--YEEVARRSRADVEAWYQTKYEEMRVTAGQHCDNLRNTRDEINELTR-------LIQRLKTE--- 400
Cdd:PHA02562 187 DMKIDHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMdiedpsaALNKLNTAaak 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 401 IEHSKAQCAKLEA---------AVAEAEQQGEAALNDAKCKLADLEGALQQAK---QDMARQLREYQELMNAKLGLDIEI 468
Cdd:PHA02562 267 IKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNEQSKKLLELKNKI 346
|
170
....*....|.
gi 344249344 469 ATYRQLLEGEE 479
Cdd:PHA02562 347 STNKQSLITLV 357
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
346-475 |
3.60e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.66 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 346 QYEEVARRSRADVEAWYQTKYEEMRVTAGQHCDNLRntrDEINELTRLIQRLKTEIEHSKAQCAKLEAAVAEAEQQGEAA 425
Cdd:cd22656 92 YYAEILELIDDLADATDDEELEEAKKTIKALLDDLL---KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDL 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 344249344 426 LND-----AKCKLADLEGALQQAKQDMARQLREYQELMNAKLG-LDIEIATYRQLL 475
Cdd:cd22656 169 LTDeggaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAdDEAKLAAALRLI 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-476 |
3.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 150 QSLLTPLNLEIDPNAQRVKKDE--KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQDQKcarSNLDPLFdNYITSL 227
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELK-EEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 228 RRQLEVLVSDQARLQAERNHMQDILEGFKKKYEE------EVGCRANAENEFVALKKdvdtaFLNKSdleanVDALaQEV 301
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSE-----FYEEY-----LDEL-REI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 302 EFLKALYLEEIQLLQSHISETSvivkMDNSRDLNLDGIIAEVKAQYEEVARRSRA------------------------D 357
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkkrltgltpeK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 358 VEAwyqtKYEEMRVTAGQHCDNLRNTRDEINELTRLIQRLKTEIEHSKAqcAKLEAAVAEA---EQQGEAALNDAKCKLA 434
Cdd:PRK03918 389 LEK----ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK--AKGKCPVCGReltEEHRKELLEEYTAELK 462
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 344249344 435 DLEGALQQAKqDMARQLREYQELMNAKLGLDIEIATYRQLLE 476
Cdd:PRK03918 463 RIEKELKEIE-EKERKLRKELRELEKVLKKESELIKLKELAE 503
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
397-476 |
4.15e-03 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 36.79 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 397 LKTEIEhskaqcaKLEAAVAEAEQQgeaaLNDAKCKLADLEGALQQAKQDMARQLREYQELMNAKLGLDIEIATYRQLLE 476
Cdd:pfam08647 1 LQTELV-------KLEQAFEELSEQ----LDKKVKDLTILEEKKLRLEAEKAKADQKYFAAMRSKDALENENKKLNTLLS 69
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
337-482 |
4.22e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 337 DGIIAEVKAQY-------EEVARRSradveawyqtkyEEMRVTAGQHcdnLRNTRDEINELTRLIQRLKTEIEhskAQCA 409
Cdd:PRK00409 501 ENIIEEAKKLIgedkeklNELIASL------------EELERELEQK---AEEAEALLKEAEKLKEELEEKKE---KLQE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 410 KLEAAVAEAEQQGEAALNDAK----------CKLADLEGALQQAKQ--DMARQLREYQELMNAKlgLDIEIATYRQLLEG 477
Cdd:PRK00409 563 EEDKLLEEAEKEAQQAIKEAKkeadeiikelRQLQKGGYASVKAHEliEARKRLNKANEKKEKK--KKKQKEKQEELKVG 640
|
....*
gi 344249344 478 EEIRI 482
Cdd:PRK00409 641 DEVKY 645
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
224-321 |
6.16e-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: 37.23 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344249344 224 ITSLRRQLEVLVSDQARLQAERNHMQDILEGFKKKYEEEVGCRANAENEFVALKKDVDTAFLNKSDLEANVDALAQEVEF 303
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEAESAKAELEE 89
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90
....*....|....*...
gi 344249344 304 LKALYLEEIQLLQSHISE 321
Cdd:pfam07926 90 SEESWEEQKKELEKELSE 107
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| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
378-450 |
7.09e-03 |
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F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.03 E-value: 7.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344249344 378 DNLRNTRDEINELTRLIQRLKTEIEHSKAQCAK-LEAAVAEAEQQGEAALNDAKcklADLEGALQQAKQDMARQ 450
Cdd:cd06503 37 ESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAK---EEAERILEQAKAEIEQE 107
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