|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-543 |
1.95e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 337 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALSK---EKME 411
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEElesKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 412 LEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEE---RVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLpt 488
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-- 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777543 489 lEDHQKQTEQLKDAELKNT------ELQGRVAELETMLEDTQAACREKEVQLESLRQREAQ 543
Cdd:TIGR02168 413 -EDRRERLQQEIEELLKKLeeaelkELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
347-541 |
8.14e-10 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 60.60 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 347 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSKEKMELEKKLSAS 419
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 420 EVEIQLIRESLKVTL---QKHSEEGKKQ----EERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 492
Cdd:pfam15905 172 MKEVMAKQEGMEGKLqvtQKNLEHSKGKvaqlEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958777543 493 QKQTEQlkDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQRE 541
Cdd:pfam15905 252 LKEKND--EIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREY 298
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-544 |
1.14e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 381 LLRLQELQREntflRAQFAQKTEALSKEKMELEKKLSASEVEIQLIRESLKvTLQKHSEEGKKQEERVKGRdkhINNLKK 460
Cdd:COG1196 231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 461 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQR 540
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
....
gi 1958777543 541 EAQF 544
Cdd:COG1196 381 LEEL 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
282-543 |
3.85e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 282 ELSTCRQQLELIRLQMEQMQLQngaichhpaaftpslptlepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 361
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 362 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSKEKMELEKKLSASEVEIQLIRESLKVTLQKHSEEG 441
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 442 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQTEQLKDAELKntelqgRVAELETMLE 521
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE------ALEEAAEEEA 452
|
250 260
....*....|....*....|..
gi 1958777543 522 DTQAACREKEVQLESLRQREAQ 543
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAAL 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-543 |
9.87e-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: 58.54 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 338 KEKELLIDKQRKHISQLEQKVRE-SELQVhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSKEKMELEK-K 415
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDlSSLEQ-----------------EIENVKSELKELEARIEELEEDLHKLEEALNDlE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 416 LSASEVEIQLIRESLkvtlQKHSEEGKKQEERVKGRDKHINNLK-KKCQKESEQNREKQQRIETLERYLADLPTLEDHQK 494
Cdd:TIGR02169 786 ARLSHSRIPEIQAEL----SKLEEEVSRIEARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958777543 495 QTEQLkDAELKntELQGRVAELETMLEDTQAACREKEVQLESLRQREAQ 543
Cdd:TIGR02169 862 KKEEL-EEELE--ELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
334-517 |
1.71e-08 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 56.88 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 334 EHLLKEKELLIDKQRKHISQLEQKVRESELQVHSAllgrpapfgdvcllRLQELQRENT----FLRAQFAQKTEALSKEK 409
Cdd:COG4487 32 EKELAERLADAAKREAALELAEAKAKAQLQEQVAE--------------KDAEIAELRArleaEERKKALAVAEEKEKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 410 MELEKKLSASEVEIQ-LIRESLKVTLQKHSEEGKKQE---ERVKGRDKHINNLKKKCQKESEQNREKQQRIETLErYLAd 485
Cdd:COG4487 98 AALQEALAEKDAKLAeLQAKELELLKKERELEDAKREaelTVEKERDEELDELKEKLKKEEEEKQLAEKSLKVAE-YEK- 175
|
170 180 190
....*....|....*....|....*....|...
gi 1958777543 486 lpTLEDHQKQTEQLKD-AELKNTELQGRVAELE 517
Cdd:COG4487 176 --QLKDMQEQIEELKRkKEQGSTQLQGEVLELE 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-543 |
5.08e-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: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 339 EKELLIDKQRKHISQLEQKVRESELQVHSALLGRpapfgDVCLLRLQELQRENTFLRAQFAQKTEALSKEKMELEKKLSA 418
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKAL-----AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 419 SE-------------VEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLAD 485
Cdd:TIGR02168 742 VEqleeriaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777543 486 L-PTLEDHQKQTE----QLKDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQREAQ 543
Cdd:TIGR02168 822 LrERLESLERRIAaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-542 |
9.59e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 334 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSKEKMELE 413
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 414 KKLSASEVEIQLIRESLKvTLQKHSEEGKKQEERV---KGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-PTL 489
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeERI 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958777543 490 EDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAAcREKEVQLESLRQREA 542
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLT 382
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-543 |
3.89e-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: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 278 EQSCELSTCRQQLELIRLQMEQMQLQNgaichhpAAFTPSLPTLEpaqwiSILNSNEHLLKEKELLIDKQRKHISQLEQK 357
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEE-------EKLKERLEELE-----EDLSSLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 358 VRESELQVhSALLGRPAPFgdvcllRLQELQRENTFLRAQFAQKTEALSkekmELEKKLSASEVEIQLIRESLKvTLQKH 437
Cdd:TIGR02169 774 LHKLEEAL-NDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQ-ELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 438 SEEgkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhQKQTEQLKdAELKntELQGRVAELE 517
Cdd:TIGR02169 842 RID---LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL------KKERDELE-AQLR--ELERKIEELE 909
|
250 260
....*....|....*....|....*.
gi 1958777543 518 TMLEDTQAACREKEVQLESLRQREAQ 543
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
375-540 |
5.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 375 PFGDVCLLRLQELQRENTFLRAQFAQKTE--ALSKEKMELEKKLSASEVEIQLIRESLK-----VTLQKHSEEGKKQEER 447
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEkleklLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 448 VKGRDKHINNLKKKCQKESE---QNREKQQRIETLERYLADLPTLEDHQKQtEQLKDAELKNTELQGRVAELETMLEDTQ 524
Cdd:COG4717 141 LAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATE-EELQDLAEELEELQQRLAELEEELEEAQ 219
|
170
....*....|....*.
gi 1958777543 525 AACREKEVQLESLRQR 540
Cdd:COG4717 220 EELEELEEELEQLENE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
287-544 |
8.36e-07 |
|
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: 52.03 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 287 RQQLELIRLQME-QMQLQNGAICHHPAAFTPSLPTLEPAQWISILNSNEHLLKEKEL--LIDKQRKHISQLEQKVRESEL 363
Cdd:pfam05483 203 RVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtfLLEESRDKANQLEEKTKLQDE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 364 QVHSALLGRPAPFGDVCLLRLQeLQRENTFLRA-----QFAQKT-EALSKEKMELEKKLSASEVEIQLIRESLKVTLQKH 437
Cdd:pfam05483 283 NLKELIEKKDHLTKELEDIKMS-LQRSMSTQKAleedlQIATKTiCQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 438 SEEGKKQEERVKGRDKHINNLKKKCQKESEQNRE-------KQQRIETLERYLADLPTLEDHQKQTEQLKDaelkntELQ 510
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEELKKILAEDEKLLDEKKQFEKIAE------ELK 435
|
250 260 270
....*....|....*....|....*....|....
gi 1958777543 511 GRVAELETMLEDTQAACREKEVQLESLRQREAQF 544
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-543 |
1.30e-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: 51.60 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 338 KEKELLIDKQRKHISQLEQKVRESELQVHSalLGRPApfgdVCLLRLQELQRENTFLRA--------QFAQKTEALSKEK 409
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKS--LERQA----EKAERYKELKAELRELELallvlrleELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 410 MELEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKH---INNLKKKCQKESEQNREKQQRIETLERYLADL 486
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777543 487 P-TLEDHQKQTEQLKD--AELKN--TELQGRVAELETMLEDTQAACREKEVQLESLRQREAQ 543
Cdd:TIGR02168 329 EsKLDELAEELAELEEklEELKEelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
381-540 |
2.15e-06 |
|
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: 49.15 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 381 LLRLQELQREntflRAQFAQKTEALSKEKMELEKKLSASEVEIqlirESLKVTLQKHSEEGKKQEERVKGRDKHINNLKK 460
Cdd:COG1579 9 LLDLQELDSE----LDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 461 KcQKESEQNRE---KQQRIETLERYLADLptlEDHQKQ-TEQLKDAELKNTELQGRVAELETMLEDTQAACREKEVQLES 536
Cdd:COG1579 81 Q-LGNVRNNKEyeaLQKEIESLKRRISDL---EDEILElMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....
gi 1958777543 537 LRQR 540
Cdd:COG1579 157 ELEE 160
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-544 |
2.35e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 330 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPapfgdvcllRLQELQRENTFLRAQFAQKTEALSKEK 409
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE---------QLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 410 MELEKKLSASEVEIqlirESLKVTLQKHSEEGKKQEERvkgrdkhINNLKKKCQKESEQNREKQQRIETLERYLADLP-T 488
Cdd:TIGR02168 771 EEAEEELAEAEAEI----EELEAQIEQLKEELKALREA-------LDELRAELTLLNEEAANLRERLESLERRIAATErR 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 489 LEDHQKQTEQLKDAELKNT----ELQGRVAELETMLEDTQAACREKEVQLESLRQREAQF 544
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAaeieELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
325-537 |
2.71e-06 |
|
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: 50.40 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 325 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQ-------------VHSallgrpapfgdvcllRLQE 386
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISdlnnqkeqdwnkeLKS---------------ELKN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 387 LQRENTFLRAQFAQKTEALSKEKME---LEKKLSASEVEIQLIRESLKvtlQKHSE--------EGKKQEerVKGRDKHI 455
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQisqLKKELTNSESENSEKQRELE---EKQNEieklkkenQSYKQE--IKNLESQI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 456 NNLKKKCQKESEQNREKQQRIETLERylaDLPTLEdhqKQTEQLKDAELKN----TELQGRVAELETMLEDTQAACREKE 531
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQ---EKELLE---KEIERLKETIIKNnseiKDLTNQDSVKELIIKNLDNTRESLE 467
|
....*.
gi 1958777543 532 VQLESL 537
Cdd:TIGR04523 468 TQLKVL 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
336-529 |
2.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 336 LLKEKELLIDKQRKHISQLEQKVRE-----SELQVHSALLGRPAPfgdvcllRLQELQRENTFLRAQFAQKTEALsKEKM 410
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIREleeriEELKKEIEELEEKVK-------ELKELKEKAEEYIKLSEFYEEYL-DELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 411 ELEKKLSASEVEIQLIRESLKvTLQKHSEEGKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLpTLE 490
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGL-TPE 387
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958777543 491 DHQKQTEQLKDA----ELKNTELQGRVAELETMLEDTQAACRE 529
Cdd:PRK03918 388 KLEKELEELEKAkeeiEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
385-540 |
4.55e-06 |
|
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: 47.59 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 385 QELQRENTFLRAQFAQKT---EALSKEKMELEKKLSASEVEIQLIRESLKvTLQKHSEEGKKQEERVKGRDKHINNLKKk 461
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEklmSEIQQENKRLTEPLQKAQEEVEELRKQLE-NYEKDKQSLKNLKARLKVLEKELKDLKW- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 462 cqkeseQNREKQQRIETLERYLADLptledHQKQTEQLKD----AELKNTELQGRVAELETMLEdtqaacrEKEVQLESL 537
Cdd:pfam13851 107 ------EHEVLEQRFEKVERERDEL-----YDKFEAAIQDvqqkTGLKNLLLEKKLQALGETLE-------KKEAQLNEV 168
|
...
gi 1958777543 538 RQR 540
Cdd:pfam13851 169 LAA 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-533 |
7.52e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 381 LLRLQELQRENTFLRAQFAQKTEALSkekmELEKKLSASEVEIQLIRESLKVT---LQKHSEEGKKQEERVKGRDKHINN 457
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELE----QLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777543 458 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAACREKEVQ 533
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-540 |
1.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 334 EHLLKEKELLIDKQRKHISQLEQKVRES-ELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFA------------- 399
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieerikeleeke 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 400 QKTEALSKEKMELEKKLSASEVEIQLIRE--SLKVTLQKHSEE----------------GKKQEE--------------- 446
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEakAKKEELERLKKRltgltpeklekeleelEKAKEEieeeiskitarigel 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 447 --RVKGRDKHINNLKKKCQKESEQNRE--KQQRIETLERYLADLPTLEdhqkqtEQLKDAELKNTELQGRVAELETMLED 522
Cdd:PRK03918 418 kkEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEYTAELKRIE------KELKEIEEKERKLRKELRELEKVLKK 491
|
250 260
....*....|....*....|
gi 1958777543 523 TQAACREKEV--QLESLRQR 540
Cdd:PRK03918 492 ESELIKLKELaeQLKELEEK 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-543 |
1.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 383 RLQELQRENTFLRA---QFAQKTEALSKEKMELEKKLSASEVEIQLIR-------------ESLKVTLQKHSEEGKKQEE 446
Cdd:PRK03918 166 NLGEVIKEIKRRIErleKFIKRTENIEELIKEKEKELEEVLREINEISselpelreeleklEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 447 RVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQTEQLKdaELKNtELQGRVAELETMLEDTQAA 526
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS--EFYE-EYLDELREIEKRLSRLEEE 322
|
170
....*....|....*..
gi 1958777543 527 CREKEVQLESLRQREAQ 543
Cdd:PRK03918 323 INGIEERIKELEEKEER 339
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-521 |
1.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 327 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 401
Cdd:PRK03918 541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 402 -----TEALSKEKMELEK---KLSASEVEIQLIRESLKVTLQKHSEEgkkQEERVKGRDKHINNLKKKCQKESEQNREKQ 473
Cdd:PRK03918 613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEELEKRR 689
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958777543 474 QRIE-TLERYLADLPTLEDHQKQTEQLKDAELKNTELQGRVAELETMLE 521
Cdd:PRK03918 690 EEIKkTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-543 |
2.49e-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: 46.68 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 383 RLQELQRENTFLRAQFAQ---KTEALSKEKMELEKKLSASEVEIQLIRESLKVT---LQKHSEEGKKQEERVKGRDKHIN 456
Cdd:COG4942 28 ELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 457 NLKKKCQKESEQNREK----QQRIETLERYLADLPTLEDHQKqtEQLKDAELKNTELQGRVAELETMLEDTQAACREKEV 532
Cdd:COG4942 108 ELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARR--EQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170
....*....|.
gi 1958777543 533 QLESLRQREAQ 543
Cdd:COG4942 186 ERAALEALKAE 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-486 |
3.50e-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: 46.30 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 330 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVcLLRLQELQRENTFLRAQfaqkTEALSKEK 409
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQ----AEELRADL 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777543 410 MELEKKlsasEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL 486
Cdd:COG4942 160 AELAAL----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
331-521 |
3.50e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 331 NSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVhsallgrpapfgdvcllrlQELQRENtflrAQFAQKTEALSKEKM 410
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-------------------KDLTKKI----SSLKEKIEKLESEKK 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 411 ELEKKLSASEVEIqlirESLKVTLQKHSEEGKKQEervkgRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT-L 489
Cdd:TIGR04523 535 EKESKISDLEDEL----NKDDFELKKENLEKEIDE-----KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKeI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958777543 490 EDHQKQ----TEQLKDAELKNTELQGRVAELETMLE 521
Cdd:TIGR04523 606 EEKEKKisslEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
341-540 |
4.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 341 ELLIDKQRKHISQLEQKVRESELQ-VHSALLGRPAPFGDVC--LLRLQElQRENTFLRAQFAQKTEALSKEKMElekKLS 417
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHERLNGLESELAELDeeIERYEE-QREQARETRDEADEVLEEHEERRE---ELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 418 ASEVEIQLIRESLKVTLQK---HSEEGKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-------- 486
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREreeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrleecr 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777543 487 PTLEDHQKQTEQL----KDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQR 540
Cdd:PRK02224 335 VAAQAHNEEAESLredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
290-543 |
5.03e-05 |
|
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: 46.65 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 290 LELIRLQMEQM-QL--QNGAichhpaafTPSLPTLEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ-- 364
Cdd:pfam15921 564 IEILRQQIENMtQLvgQHGR--------TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkv 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 365 ------------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSKEKMELEKKLSASEVEIQLIRESL 430
Cdd:pfam15921 636 klvnagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 431 KvtlqkhSEEGKK---------QEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQT 496
Cdd:pfam15921 716 K------SMEGSDghamkvamgMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMA 789
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958777543 497 EQLKDAELKNTELQGRVAELETMLEdtQAACREKEVQleSLRQREAQ 543
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALD--KASLQFAECQ--DIIQRQEQ 832
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-540 |
5.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 334 EHLLKEKELLID-----KQRKHISQLEQKVRESELQVHsALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALS 406
Cdd:COG4913 215 EYMLEEPDTFEAadalvEHFDDLERAHEALEDAREQIE-LLEPIRELAERYaaARERLAELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 407 KEKME--------LEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKgrdKHINNLKKKcQKESEQNREK-QQRIE 477
Cdd:COG4913 294 EAELEelraelarLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE---REIERLERE-LEERERRRARlEALLA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777543 478 TLE-RYLADLPTLEDHQKQTEQLKDA--ELKNtELQGRVAELETMLEDTQAACREKEVQLESLRQR 540
Cdd:COG4913 370 ALGlPLPASAEEFAALRAEAAALLEAleEELE-ALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
275-540 |
6.50e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 275 HPGEQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFTPSLPTLEPAQWISILNSNEHLLKEKELL---------- 343
Cdd:pfam10174 66 QEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLrktleemelr 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 344 IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---------AQFA 399
Cdd:pfam10174 146 IETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelhrrnqlQPDP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 400 QKTEALSK-------EKMELEKKLSASEVEIQLIRESLKVTLQKHSEEgKKQEERVKGRDKHINN----LKKKCQ-KESE 467
Cdd:pfam10174 226 AKTKALQTviemkdtKISSLERNIRDLEDEVQMLKTNGLLHTEDREEE-IKQMEVYKSHSKFMKNkidqLKQELSkKESE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 468 -------------QNREKQQRIETLERYL-------ADLPT--------LEDHQ----KQTEQLKDAELKNTELQGRVAE 515
Cdd:pfam10174 305 llalqtkletltnQNSDCKQHIEVLKESLtakeqraAILQTevdalrlrLEEKEsflnKKTKQLQDLTEEKSTLAGEIRD 384
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958777543 516 LETML--------------EDTQAACREKEVQLESLRQR 540
Cdd:pfam10174 385 LKDMLdvkerkinvlqkkiENLQEQLRDKDKQLAGLKER 423
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
338-540 |
8.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 338 KEKELLIDKQRKHISQLEQKVRESELQVhSALLG--RPAPfgdVCLLRLQELQRENtfLRAQFAQKTEALSKEKMELEKK 415
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAI-EELKKakGKCP---VCGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 416 LS-----ASEVEIQL------------------IRESLKV----TLQKHSEEGKKQEERVKGRDKHINNLKKKCQKESEQ 468
Cdd:PRK03918 475 ERklrkeLRELEKVLkkeseliklkelaeqlkeLEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 469 NREK---QQRIETLERYLADLPT-------------------LEDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAA 526
Cdd:PRK03918 555 KKKLaelEKKLDELEEELAELLKeleelgfesveeleerlkeLEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
250
....*....|....
gi 1958777543 527 CREKEVQLESLRQR 540
Cdd:PRK03918 635 LAETEKRLEELRKE 648
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
348-544 |
1.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 348 RKHISQLEQKVRESELqvhsallgrpapfgdvcllRLQELQRENTFLraQFAQKTEALSKEKMELEKKLSASEVEIQLIR 427
Cdd:COG3206 181 EEQLPELRKELEEAEA-------------------ALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 428 ESLKvTLQKHSEEGKKQEERVkGRDKHINNLKkkcqkeSEQNREKQQRIETLERYLADLPTLEDHQKQTEQLKdaELKNT 507
Cdd:COG3206 240 ARLA-ALRAQLGSGPDALPEL-LQSPVIQQLR------AQLAELEAELAELSARYTPNHPDVIALRAQIAALR--AQLQQ 309
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958777543 508 ELQGRVAELETMLEDTQAACREKEVQLESLRQREAQF 544
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
403-539 |
1.16e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 403 EALSKEKmelEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 482
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777543 483 LADLptleDHQKQTEQLKDAELKNteLQGRVAELETMLEDTQAACREKEVQLESLRQ 539
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
330-522 |
1.31e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 330 LNSNEHLLKEKEL--LIDKQRKHISQLEQ-----KVRESELQvhsallgrpapfgdvclLRLQELQRENTFLRAQFAQKT 402
Cdd:TIGR04523 547 LNKDDFELKKENLekEIDEKNKEIEELKQtqkslKKKQEEKQ-----------------ELIDQKEKEKKDLIKEIEEKE 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 403 -----------------EALSKEKMELEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKhINNLKKKCQKE 465
Cdd:TIGR04523 610 kkisslekelekakkenEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKE 688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777543 466 SEQNREKqqRIETLERYlADLPTLEDHQKQTEQLkdaelkNTELQGRVAELETMLED 522
Cdd:TIGR04523 689 LSLHYKK--YITRMIRI-KDLPKLEEKYKEIEKE------LKKLDEFSKELENIIKN 736
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-543 |
1.83e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 383 RLQELQRENTFLRAQFAQKT----------EALSKEKMELEKKLSASEVEIQLIRESLKVTlQKHSEEGKKQE--ERVKG 450
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPvdlgnaedflEELREERDELREREAELEATLRTARERVEEA-EALLEAGKCPEcgQPVEG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 451 rDKHINNLKkkcqkeseqnrEKQQRIETLERYLADLPT----LEDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAA 526
Cdd:PRK02224 464 -SPHVETIE-----------EDRERVEELEAELEDLEEeveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
170
....*....|....*..
gi 1958777543 527 CREKEVQLESLRQREAQ 543
Cdd:PRK02224 532 IEEKRERAEELRERAAE 548
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-526 |
1.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 381 LLRLQELQRENTFLRAQ---FAQKTEALS---KEKMELEKKLSASEVEIQLIRESLKV--------TLQKHSEEGKKQEE 446
Cdd:COG4717 70 LKELKELEEELKEAEEKeeeYAELQEELEeleEELEELEAELEELREELEKLEKLLQLlplyqeleALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 447 RVKGRDKHINNLKKKCQKESEQNREKQQRIETLERY--LADLPTLEDHQKQ-----------TEQLKDAELKNTELQGRV 513
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEEleelqqrlaelEEELEEAQEELEELEEEL 229
|
170
....*....|...
gi 1958777543 514 AELETMLEDTQAA 526
Cdd:COG4717 230 EQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-543 |
2.45e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 383 RLQELQREntflRAQfAQKTEALSKEKMELEKKLSASEVEIQLireslkvtlqkhseegkKQEERVkgrDKHINNLKKKC 462
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEALE-----------------RQKEAI---ERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 463 QKESEQNREKQQRIETLERyladlpTLEDHQKQTEQLKDAELknTELQGRVAELETMLEDTQAACREKEVQLESLRQREA 542
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQ------LLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
.
gi 1958777543 543 Q 543
Cdd:TIGR02169 326 K 326
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-534 |
2.66e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 384 LQELQRENTFLRAQFAQKTEALS--KEKMELEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKHINNLKKK 461
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958777543 462 CQKESEQNREKQQRIETLERYLADLptledhQKQTEQLKD--AELKNTELQGRVAELETMLEDTQAACREKEVQL 534
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKEL------EKQLNQLKSeiSDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI 330
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-530 |
2.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 287 RQQLELIRLQMEQMQLQNGAICHHPAAFTPSlPTLEPAQWISILnsneHLLKEKELLIDKQRKHISQLEQKVRESELQvh 366
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLP-PDLSPEELLELL----DRIEELQELLREAEELEEELQLEELEQEIA-- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 367 sALLGRpAPFGDvcllrlqelqrentflRAQFAQKTEALsKEKMELEKKLSASEVEIQLIRESLKVTLQKHseegkkQEE 446
Cdd:COG4717 374 -ALLAE-AGVED----------------EEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEAL------DEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 447 RVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQTEQLKdAELKNTELQGRVAEL-ETMLEDTQA 525
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK-AELRELAEEWAALKLaLELLEEARE 507
|
....*
gi 1958777543 526 ACREK 530
Cdd:COG4717 508 EYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
399-543 |
3.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 399 AQKTEALSKEKMELEKKLSASEVEIQLIRESLKvTLQKHSEEGKKQEE------RVKGRDKHInnlkkkcqkeseqnREK 472
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEyswdeiDVASAEREI--------------AEL 673
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777543 473 QQRIETLERYLADLPTLEDHQKQTEQ-LKDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQREAQ 543
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAeLEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
337-543 |
4.15e-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: 43.63 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 337 LKEKELLIDKQRKHISQ-------LEQKVRESELQVHSALLGRPAPFGDVCLLRLQ--ELQRENTFLRAQfaqKTEALSK 407
Cdd:pfam01576 751 VRELEAELEDERKQRAQavaakkkLELDLKELEAQIDAANKGREEAVKQLKKLQAQmkDLQRELEEARAS---RDEILAQ 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 408 EKmELEKKLSASEVEIQLIRESLKVtlqkhSEEGKKQ--EERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLAD 485
Cdd:pfam01576 828 SK-ESEKKLKNLEAELLQLQEDLAA-----SERARRQaqQERDELADEIASGASGK-SALQDEKRRLEARIAQLEEELEE 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 486 LPT----LEDHQK----QTEQL------------------KDAELKNTELQGRVAELE----TMLEDTQAACREKEVQLE 535
Cdd:pfam01576 901 EQSntelLNDRLRkstlQVEQLttelaaerstsqksesarQQLERQNKELKAKLQEMEgtvkSKFKSSIAALEAKIAQLE 980
|
....*...
gi 1958777543 536 SLRQREAQ 543
Cdd:pfam01576 981 EQLEQESR 988
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-542 |
4.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 381 LLRLQELQRENTFLRAQFAQKTEALSKEkmELEKKLSASEVEIQLIRESLKVTLQKHSE--------EGKKQEERVKGRD 452
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEElqellreaEELEEELQLEELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 453 KHINNLKKKCQKESE-----------QNREKQQRIETLERYLADLPTLEDHQKQTEQLKDAELKNTELQGRVAELETMLE 521
Cdd:COG4717 370 QEIAALLAEAGVEDEeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
170 180
....*....|....*....|.
gi 1958777543 522 DTQAACREKEVQLESLRQREA 542
Cdd:COG4717 450 ELREELAELEAELEQLEEDGE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-516 |
5.11e-04 |
|
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: 43.12 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 330 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQV--HSALLGRPAPfgdvcllRLQELQREntflRAQFAQKTEALSK 407
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEA-------RLERLEDR----RERLQQEIEELLK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 408 EKMELEKKLSASEVEIqliRESLKVTLQKHSEEGKKQEERVKGRdkhINNLKKKCQKESEQNREKQQRIETLERYLADlp 487
Cdd:TIGR02168 429 KLEEAELKELQAELEE---LEEELEELQEELERLEEALEELREE---LEEAEQALDAAERELAQLQARLDSLERLQEN-- 500
|
170 180
....*....|....*....|....*....
gi 1958777543 488 tLEDHQKQTEQLKDAELKNTELQGRVAEL 516
Cdd:TIGR02168 501 -LEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
311-543 |
5.74e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 311 PAAFTPSLPTLEPAQ-WISILNSNEHLLKEKELL-------------IDKQRKHISQLEQKVRESelqvhsallgrPApf 376
Cdd:PRK11281 28 RAASNGDLPTEADVQaQLDALNKQKLLEAEDKLVqqdleqtlalldkIDRQKEETEQLKQQLAQA-----------PA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 377 gdvcllRLQELQRENTFLRAQFAQKT-EALSKEKM-ELEKKLSASEVEIQLIRE------SLKVTLQKHSEEGKKQEERV 448
Cdd:PRK11281 95 ------KLRQAQAELEALKDDNDEETrETLSTLSLrQLESRLAQTLDQLQNAQNdlaeynSQLVSLQTQPERAQAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 449 KGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTleDHQKQT----EQLKD-AELKNTELQGRVAELETMLEDT 523
Cdd:PRK11281 169 SQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN--DLQRKSlegnTQLQDlLQKQRDYLTARIQRLEHQLQLL 246
|
250 260
....*....|....*....|....*.
gi 1958777543 524 QAACREKEVQL------ESLRQREAQ 543
Cdd:PRK11281 247 QEAINSKRLTLsektvqEAQSQDEAA 272
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
346-540 |
5.89e-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: 42.85 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 346 KQRKHISQLeQKVRESELQVHSAllgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSKEKMELEKKLSASEVEIQL 425
Cdd:pfam01576 324 KREQEVTEL-KKALEEETRSHEA--------------QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 426 IRESLKVTLQKHSEegkkQEERVKGRDKHINNLKKKCqkeSEQNREKQQRIETLERYLADLPTLedhqkqTEQLKDAELK 505
Cdd:pfam01576 389 LQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL---SESERQRAELAEKLSKLQSELESV------SSLLNEAEGK 455
|
170 180 190
....*....|....*....|....*....|....*
gi 1958777543 506 NTELQGRVAELETMLEDTQAACREKEVQLESLRQR 540
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-543 |
6.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 393 FLRAQFAqktEALSKEKMELEKKL-SASEVEIQLIREslkvtLQKHSEEGKKQEERVKGRDKHINNLKKKCQKESEQNRE 471
Cdd:COG4717 42 FIRAMLL---ERLEKEADELFKPQgRKPELNLKELKE-----LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777543 472 KQQRIETLERYLADLPTLEDHQKQTEQLKDAELKNTELQGRVAELETMLEDtqaaCREKEVQLESLRQREAQ 543
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE 181
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
383-543 |
1.15e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 383 RLQELQRE-NTFLRAQFAQKT-------------EALSKEKMELEKKlsaseveIQLIRESLKVTLQKHSEEGKKQEERV 448
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANRqrekekerykrdrEQWERQRRELESR-------VAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 449 KGRDKhinnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQ-TEQLKDAELKNTELQGRvael 516
Cdd:pfam07888 108 ASSEE----LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKaGAQRKEEEAERKQLQAK---- 179
|
170 180
....*....|....*....|....*..
gi 1958777543 517 etmLEDTQAACREKEVQLESLRQREAQ 543
Cdd:pfam07888 180 ---LQQTEEELRSLSKEFQELRNSLAQ 203
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
320-542 |
1.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 320 TLEPAQwiSILNSNEHLLKEKELL---IDKQRKHISQLEQKvRES---ELQVHSAllgrpapfgdvcllRLQELQRENTF 393
Cdd:PRK02224 235 TRDEAD--EVLEEHEERREELETLeaeIEDLRETIAETERE-REElaeEVRDLRE--------------RLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 394 LRAQFA---QKTEALSKEKMELEKKLSASEVEIQLIReslkVTLQKHSEEGKKQEERVKGRDkhinnlkkkcqkesEQNR 470
Cdd:PRK02224 298 LLAEAGlddADAEAVEARREELEDRDEELRDRLEECR----VAAQAHNEEAESLREDADDLE--------------ERAE 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777543 471 EKQQRIETLERYLADlpTLEDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQREA 542
Cdd:PRK02224 360 ELREEAAELESELEE--AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
391-501 |
2.60e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 391 NTFLRaQFAQKTEALSKEKMELEKKLSASEVEIQLIR---ESLKVTLQKHSEEGKKQEERVKGRDK----HINNLKKKCQ 463
Cdd:pfam02841 175 EEVLQ-EFLQSKEAVEEAILQTDQALTAKEKAIEAERakaEAAEAEQELLREKQKEEEQMMEAQERsyqeHVKQLIEKME 253
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958777543 464 KESEQNREKQQRI--ETLERYLADLptLEDHQKQTEQLKD 501
Cdd:pfam02841 254 AEREQLLAEQERMleHKLQEQEELL--KEGFKTEAESLQK 291
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
327-543 |
2.91e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 327 ISILNSNEHLLKEkELLIDKQRKH-----ISQLEQKVRESELQVHsallgrpapfgdvclLRLQELQRENTFLRAQFAqK 401
Cdd:TIGR04523 98 INKLNSDLSKINS-EIKNDKEQKNkleveLNKLEKQKKENKKNID---------------KFLTEIKKKEKELEKLNN-K 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 402 TEALSKEKMELEKKLSASEVEIQLIRESLKVTLQKHSEEG------KKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 475
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777543 476 IETLERyladlpTLEDHQKQTEQLKDAELKN-TELQGRVAELET---MLEDTQAACREKEVQLESLRQREAQ 543
Cdd:TIGR04523 241 INEKTT------EISNTQTQLNQLKDEQNKIkKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQ 306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
463-543 |
5.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 463 QKESEQNREK-QQRIETLERYLADlpTLEDHQKQTEQLKDAELKNTELQGRVAELETMLEDTQAACREKEVQLESLRQRE 541
Cdd:COG4942 22 AAEAEAELEQlQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
..
gi 1958777543 542 AQ 543
Cdd:COG4942 100 EA 101
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
334-543 |
6.05e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 334 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGdvcllrlqeLQRENTFLRAQFAQKtealskeKMEL 412
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA---------MERERELERIRQEER-------KREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 413 EK-KLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLED 491
Cdd:pfam17380 363 ERiRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-------KVKILEEERQRKIQQQKVE-----------MEQ 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958777543 492 HQKQTEQLKDAELKNTElQGRVAELETMLEDTQaacrEKEVQLESLRQREAQ 543
Cdd:pfam17380 425 IRAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEE 471
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
338-544 |
6.07e-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: 39.64 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 338 KEKELLIDKQRKHISQLEQKVreSELQVHSALLGrpapfgdvcllrlqelqrENTFLRAQFAQKTEALSKEKMELEKKLS 417
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKT--NELKSEKLQIG------------------TNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 418 ASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKHINNLKKKCQK------------ESEQNREKQQRIETLERYLAD 485
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdienkiQDGKDDYLKQKETELNTVNAQ 985
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777543 486 LPTLEDHQKQTEqlKDAELKNTELQGRVAElETMLEDtQAACREKEVQLESLRQREAQF 544
Cdd:TIGR00606 986 LEECEKHQEKIN--EDMRLMRQDIDTQKIQ-ERWLQD-NLTLRKRENELKEVEEELKQH 1040
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
399-540 |
6.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 399 AQKTEALSKEKMELEKKLSASEVEIQLIRESLKvtlqkhseegkKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIET 478
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQ-----------KLEKRLL---QKEENLDRK----LELLEKREEELEK 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958777543 479 LEryladlptledhQKQTEQLKDAELKNTELQGRVAELETMLEDTQAACRE--KEVQLESLRQR 540
Cdd:PRK12704 115 KE------------KELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-544 |
6.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 383 RLQELQREntflRAQFAQKTEALsKEKMELEKKLSASEVEIQLIRESLKvTLQKHSEEgkkQEERVKGRDKHINNLKKKC 462
Cdd:PRK02224 476 RVEELEAE----LEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERRE-DLEELIAE---RRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 463 QKESEQNREKQQRIETLEryladlptlEDHQKQTEQLKDAELKNTELQGRVAELETmLEDTQAACREKEVQLESLRQREA 542
Cdd:PRK02224 547 AELEAEAEEKREAAAEAE---------EEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKRE 616
|
..
gi 1958777543 543 QF 544
Cdd:PRK02224 617 AL 618
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
382-541 |
6.98e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.16 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 382 LRLQELQRENtflRAQFAQKTeaLSKEKMELEKKLSAS-EVEIQLIRESLKVTLQKHSEEGKKQEERVKgrdkhinnlKK 460
Cdd:pfam15709 345 MRRLEVERKR---REQEEQRR--LQQEQLERAEKMREElELEQQRRFEEIRLRKQRLEEERQRQEEEER---------KQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 461 KCQKESEQNREKQQRiETLERYLADLptleDHQKQTEQLKDAElkntELQGRVAELETMLEDTQAACRE--KEVQLESLR 538
Cdd:pfam15709 411 RLQLQAAQERARQQQ-EEFRRKLQEL----QRKKQQEEAERAE----AEKQRQKELEMQLAEEQKRLMEmaEEERLEYQR 481
|
...
gi 1958777543 539 QRE 541
Cdd:pfam15709 482 QKQ 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
332-500 |
8.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 332 SNEHLLKEKELLIDKQRKHISQLEQkvRESELQVHSALLGRpapfgdvcLLRLQELQRENTFLRAQFAQKTEALS--KEK 409
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEK--------LLQLLPLYQELEALEAELAELPERLEelEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 410 M----ELEKKLSASEVEIQLIRESLKVTLQKHSEEGKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLAD 485
Cdd:COG4717 155 LeelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|....*
gi 1958777543 486 LPTLEDHQKQTEQLK 500
Cdd:COG4717 235 ELEAAALEERLKEAR 249
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
278-499 |
8.45e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.34 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 278 EQSCELSTCRqqlELIRLQMEQMQlQNGAICHHpaaftpslptLEPAQWISILNsnehllKEKELLIDKQRKHISQL--- 354
Cdd:pfam17380 369 EIAMEISRMR---ELERLQMERQQ-KNERVRQE----------LEAARKVKILE------EERQRKIQQQKVEMEQIrae 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 355 EQKVRESELQVHSALLGRpapfgDVCLLRLQELQRENTF--LRAQFA-QKTEALSKEKMELEKKLsASEVEIQLIRESLK 431
Cdd:pfam17380 429 QEEARQREVRRLEEERAR-----EMERVRLEEQERQQQVerLRQQEEeRKRKKLELEKEKRDRKR-AEEQRRKILEKELE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 432 VTLQKHSEEGKKQ-------EERVKG----RDKHINNLKKKCQKESEQNREKQQ----------RIETLERYLADLPTLE 490
Cdd:pfam17380 503 ERKQAMIEEERKRkllekemEERQKAiyeeERRREAEEERRKQQEMEERRRIQEqmrkateersRLEAMEREREMMRQIV 582
|
....*....
gi 1958777543 491 DHQKQTEQL 499
Cdd:pfam17380 583 ESEKARAEY 591
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
327-500 |
9.32e-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: 38.46 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 327 ISILNSNEHLLKEKELLIDKQRKHISQLEQKVREselqvhsallgrpapfgdvcllRLQELQRENTFLRaqfAQKTEALS 406
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRD----------------------RKDALEEELRQLK---QLEDELED 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 407 KEKMELEKklsaseveiqlIRESLKVTLQKHSEEGKKQEERVKGRDKH---INNLKKKCQKESEQNREKQQRIETLERY- 482
Cdd:smart00787 201 CDPTELDR-----------AKEKLKKLLQEIMIKVKKLEELEEELQELeskIEDLTNKKSELNTEIAEAEKKLEQCRGFt 269
|
170
....*....|....*...
gi 1958777543 483 LADLPTLEDHQKQTEQLK 500
Cdd:smart00787 270 FKEIEKLKEQLKLLQSLT 287
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
403-540 |
9.81e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 38.70 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777543 403 EALSKEKMELEKKLSAsevEIQLIRESLKVTlQKHSEEGKKQEERVKGRDKHINNLKKKCQKESEQNREKQ--QRIETLE 480
Cdd:pfam02029 149 VRQAEEEGEEEEDKSE---EAEEVPTENFAK-EEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEvtKLKVTTK 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777543 481 RYLADLPTLEDHQKQTEQLKDAELKNTELQGRVAELETM-LEDTQAACREKEVQLESLRQR 540
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKK 285
|
|
| |
