|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-290 |
3.01e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 54 TEYKEKCDELQKSQRESSTLH-RQLDEvllKLEPLEKQTVKYEQMKTELENTKAELE--LNQQRCKDV----------DR 120
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRlEELRE---ELEELQEELKEAEEELEELTAELQELEekLEELRLEVSeleeeieelqKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 121 LKEKNAQIIIL---KEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDslrKYHQTSEEHESLKLENAKTLIL 197
Cdd:TIGR02168 290 LYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE---KLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 198 KGNLENELLVLKELKCQQDKEV-------GALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVR 270
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVaqlelqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260
....*....|....*....|
gi 1751363285 271 MLLEELWHCVETSNKTQEKL 290
Cdd:TIGR02168 447 EELEELQEELERLEEALEEL 466
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
28-815 |
9.27e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.84 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAE 107
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 108 LELNQQRCK-------DVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQT 180
Cdd:pfam02463 347 LEIKREAEEeeeeeleKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 181 SEEHESLKLENAKTLILKGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDS 260
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 261 EPTIDKDKVRMLLEELWHCVETSNKTQ----------EKLLLTGEETTQLKRIPSQPRLNSPSERHIFHPspgKASPETQ 330
Cdd:pfam02463 507 SGLKVLLALIKDGVGGRIISAHGRLGDlgvavenykvAISTAVIVEVSATADEVEERQKLVRALTELPLG---ARKLRLL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 331 SSILSMPKTPPRVSRPKESPQKLKKQNNVQQFNTQSRKRKVSSDVLEQVD-TLTDDSKEMTCEGLLHGDYCMDLLALKEW 409
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTElTKLKESAKAKESGLRKGVSLEEGLAEKSE 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 410 FKPLPPVLSPVhspsLELVNVNDNKPMSDTQQENESSNEKSKTLASLHEELELSDIGDKKSLLKEEegtcslLCPDTLTR 489
Cdd:pfam02463 664 VKASLSELTKE----LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD------RVQEAQDK 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 490 STVSVDNLDSEKTSESQN-VEAEDMCEVTLGCVADSLSDHAKLAPEKSVEISLVNGDTGTAGELPLKNEngEKAHLEDAK 568
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEeEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE--LRALEEELK 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 569 VTDKFTNMLENsdpcqwNESKIVDTSSSEFSECKTQEQ-PIVSVASNVKRNSMGDMNCLKSKNIENKESKISVSLEINSA 647
Cdd:pfam02463 812 EEAELLEEEQL------LIEQEEKIKEEELEELALELKeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 648 QDSSTqdvqnrLPDKAVQSEDISEDISSVTIKckksLDVRENGDLCSSKTSSDELSSKDEGIFGLMGEVSDQAWSEgRAH 727
Cdd:pfam02463 886 DELES------KEEKEKEEKKELEEESQKLNL----LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE-ENN 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 728 PKKLENLSEFEQCSTAKQMSKDEPQEFLSESKTQSNAERPLVVINSEQERSANQQESGETCKENSSESPRKTMQVNNTFN 807
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
....*...
gi 1751363285 808 QEADEMSP 815
Cdd:pfam02463 1035 KVFFYLEL 1042
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-257 |
3.96e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 32 LDEYVAALLTLKQKIvdtdHILTEYKEKCDELQKSQREsstlHRQLDEVLLKLEPLEKQTvKYEQMKTELENTKAELELN 111
Cdd:COG4913 237 LERAHEALEDAREQI----ELLEPIRELAERYAAARER----LAELEYLRAALRLWFAQR-RLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 112 QQRCKDVDRLKEKnaqiiiLKEKLEEsLRKAEDTLKGQDLENekLKNGKQLLEEDLQKMQDSLRKYHQTSeehESLKLEn 191
Cdd:COG4913 308 EAELERLEARLDA------LREELDE-LEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEALL---AALGLP- 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751363285 192 aktlilkgnLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFN---KEKRSMSSQ 257
Cdd:COG4913 375 ---------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELReleAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
52-261 |
7.65e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 52 ILTEYKEKCDELQKSQ-RESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIII 130
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 131 LKEKLEEsLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAktlilkgnleneLLVLKE 210
Cdd:COG4717 127 LLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS------------LATEEE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1751363285 211 LKcQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSE 261
Cdd:COG4717 194 LQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
40-311 |
8.98e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 40 LTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDVD 119
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 120 R------LKEKNAQIIILKEKLE-ESLRKAEDTLKGQDLENE-KLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLEN 191
Cdd:pfam02463 314 EklkeseKEKKKAEKELKKEKEEiEELEKELKELEIKREAEEeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 192 AKTLILKGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLfTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVRM 271
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1751363285 272 LLEELwHCVETSNKTQEKLLLTGEETTQLKRIPSQPRLNS 311
Cdd:pfam02463 473 LLKET-QLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
55-471 |
9.36e-08 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.01 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKSQRESSTLHRQLDEvllklepLEKQTVkYEQMKTELENTKAELELNQQRCKDVDRLKEKN----AQIII 130
Cdd:COG5022 839 EFSLKAEVLIQKFGRSLKAKKRFSL-------LKKETI-YLQSAQRVELAERQLQELKIDVKSISSLKLVNleleSEIIE 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 131 LKEKLEESLRKA-----------EDTLKGQDLENEKLKngKQLLEEDLQKMQDSLRKYHQTSEEHESLkLENAKTLILKG 199
Cdd:COG5022 911 LKKSLSSDLIENlefkteliarlKKLLNNIDLEEGPSI--EYVKLPELNKLHEVESKLKETSEEYEDL-LKKSTILVREG 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 200 NLENELLV-----LKELKCQQdkevGALINEKRRLEEMLFTTqQNLNKLQKEFNKEKRSMSSQTD-SEPTIDKDKVRMLL 273
Cdd:COG5022 988 NKANSELKnfkkeLAELSKQY----GALQESTKQLKELPVEV-AELQSASKIISSESTELSILKPlQKLKGLLLLENNQL 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 274 EELWHCVETSNKTQ---EKLLLTGEET-TQLKRIPSQP------RLNSPSERHIFHPSPGKASPETQSS-------ILSM 336
Cdd:COG5022 1063 QARYKALKLRRENSlldDKQLYQLESTeNLLKTINVKDlevtnrNLVKPANVLQFIVAQMIKLNLLQEIskflsqlVNTL 1142
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 337 PKTPPRVSRPKESPQKLKKQNNVQQ------FNTQSRKRKVSSDVL--------EQVDTLTDDSKEMTC---EGLLHGDY 399
Cdd:COG5022 1143 EPVFQKLSVLQLELDGLFWEANLEAlpspppFAALSEKRLYQSALYdeksklssSEVNDLKNELIALFSkifSGWPRGDK 1222
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751363285 400 CMDLLAlKEWfkpLPPVLSPVHSPSLELVNVNDNKPMSDTQQENESSNEKSKTLASLHEELELSDIGDKKSL 471
Cdd:COG5022 1223 LKKLIS-EGW---VPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLL 1290
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-290 |
1.16e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 32 LDEYVAALLTLKQKIVDTDHILTEYKEKCDELQK---SQRESSTLHRQLDEVL--------LKLEPLEKQTVKYEQMKTE 100
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkKESELIKLKELAEQLKeleeklkkYNLEELEKKAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 101 LENTKAELELNQQRCKDVDRLKEKnaqiiilKEKLEESLRKAEDTLKgqDLENEKLKNGKQLLEEDLQKMQdSLRKYHQt 180
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKK-------LAELEKKLDELEEELA--ELLKELEELGFESVEELEERLK-ELEPFYN- 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 181 seehESLKLENAKTlilkgNLENELLVLKELKCQQDKEVGALINEKRRLEEMlfttQQNLNKLQKEFNKEKRSMSSQTDS 260
Cdd:PRK03918 603 ----EYLELKDAEK-----ELEREEKELKKLEEELDKAFEELAETEKRLEEL----RKELEELEKKYSEEEYEELREEYL 669
|
250 260 270
....*....|....*....|....*....|
gi 1751363285 261 EPTIDKDKVRMLLEELWHCVETSNKTQEKL 290
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-276 |
4.11e-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: 55.07 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQmktELENTKAelELNQQRCKDVDRLKEKNAQIIilkEK 134
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE---ALNDLEA--RLSHSRIPEIQAELSKLEEEV---SR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 135 LEESLRKAEDTLKGQDLEN---EKLKNGKQLLEEDLQKMQDSLRKyhqtseEHESLKLENAKTLILKGNLENELLVL--- 208
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEK------EIENLNGKKEELEEELEELEAALRDLesr 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 209 ------------KELKCQQDK--EVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSqtDSEPTIDKDKVRMLLE 274
Cdd:TIGR02169 884 lgdlkkerdeleAQLRELERKieELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQ 961
|
..
gi 1751363285 275 EL 276
Cdd:TIGR02169 962 RV 963
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-252 |
8.23e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 32 LDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELN 111
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 112 QQRCKDVDRLKEKNAQIIILKEKLE-ESLRKAEDTLkgqdlenEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEH----ES 186
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTgLTPEKLEKEL-------EELEKAKEEIEEEISKITARIGELKKEIKELkkaiEE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751363285 187 LKLENAKTLILKGNLENELlvLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKR 252
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEEH--RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
39-290 |
2.05e-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: 52.33 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 39 LLTLKQKIVDTDHILTEYKEKCDELQK----SQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQR 114
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKeltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 115 CKDVDRLKEKnaQIIILKEKLEESLRKAEDTLKGQDLENEKLKNgkqLLEED--LQKMQDSLRKYhqTSEEHESLKLENA 192
Cdd:TIGR04523 403 QEKLNQQKDE--QIKKLQQEKELLEKEIERLKETIIKNNSEIKD---LTNQDsvKELIIKNLDNT--RESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 193 KTLILKGNLENellVLKELKcQQDKEVGALINEKRRLEEMLFTTQQNLNKL---QKEFNKEKRSMSSQTDS-EPTIDKDK 268
Cdd:TIGR04523 476 SINKIKQNLEQ---KQKELK-SKEKELKKLNEEKKELEEKVKDLTKKISSLkekIEKLESEKKEKESKISDlEDELNKDD 551
|
250 260
....*....|....*....|..
gi 1751363285 269 VRMLLEELWHCVETSNKTQEKL 290
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEEL 573
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-257 |
2.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 77 LDEVLLKLEPLEKQ---TVKYEQMKTELENTKAELELNqqrckdvdRLKEKNAQIIILKEKLEES---LRKAEDTLKGQD 150
Cdd:COG1196 195 LGELERQLEPLERQaekAERYRELKEELKELEAELLLL--------KLRELEAELEELEAELEELeaeLEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 151 LENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEE------HESLKLENAKTLILKgnLENELLVLKELKCQQDKEVGALIN 224
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARleqdiaRLEERRRELEERLEE--LEEELAELEEELEELEEELEELEE 344
|
170 180 190
....*....|....*....|....*....|...
gi 1751363285 225 EKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQ 257
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
28-301 |
3.59e-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: 51.56 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIVDT----DHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPL--EKQTVKYEQMKTEL 101
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLkdeqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 102 ENTKAEL-ELNQQRCKDVDRLKEKNAQIIILK----------EKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKM 170
Cdd:TIGR04523 317 KNQEKKLeEIQNQISQNNKIISQLNEQISQLKkeltnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 171 QDSLRKYHQTSEEHESlKLENAKTliLKGNLENELLVLKELKCQQDKEVGALINEKRRLEemlfTTQQNLNKLQKEFNKE 250
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDE-QIKKLQQ--EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE----LIIKNLDNTRESLETQ 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1751363285 251 KRSMSSQTDSEPTIDKDKVRmlleelwhcvETSNKTQEKLLLTgEETTQLK 301
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQK----------ELKSKEKELKKLN-EEKKELE 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-258 |
4.00e-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: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 83 KLEPLEKQ---TVKYEQMKTELENTKAEL-------------ELNQQRCKDVDRLKEKNAQIIILKEKLEES---LRKAE 143
Cdd:TIGR02168 201 QLKSLERQaekAERYKELKAELRELELALlvlrleelreeleELQEELKEAEEELEELTAELQELEEKLEELrleVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 144 DTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLILKG----NLENELLVLKELKCQQDKEV 219
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeelaELEEKLEELKEELESLEAEL 360
|
170 180 190
....*....|....*....|....*....|....*....
gi 1751363285 220 GALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQT 258
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-254 |
8.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 42 LKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRckdvdrl 121
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 122 keknaqiiilKEKLEESLRKAEDTLKGQDLENEKLKNgkqlLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLILKGNL 201
Cdd:PRK03918 254 ----------KRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751363285 202 ENELLVLKElkcqQDKEVGALINEKRRLEEMLFTTQQNLNKLQ---KEFNKEKRSM 254
Cdd:PRK03918 320 EEEINGIEE----RIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKK 371
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-252 |
1.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 30 QSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQREsstLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELE 109
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE---LREELEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 110 LNQQRCKDV-DRLKEKNAQIIILKEKLEE--SLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHES 186
Cdd:PRK03918 256 KLEEKIRELeERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751363285 187 LKLENAKTLILKGNLENELLVLKElKCQQDKEVGALINEKRRLEEMLftTQQNLNKLQKEFNK-EKR 252
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEElEKA 399
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-509 |
1.49e-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: 49.73 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 25 CTVLNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQ--KSQRESSTLHRQL---------DEVLLKLEPLEKQTVK 93
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQveKAQLEKEINDRRLelqefkilkDKKDAKIRELEARVSD 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 94 YEQMKTELENTKAEL-----ELNQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQ 168
Cdd:pfam15921 630 LELEKVKLVNAGSERlravkDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 169 KMQDSLRKYHQTSEEHESLKLENAKTLILKGN----LENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQ 244
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 245 KEF----NKEKRSMSSQTDSEPTIDKDKVrmlleELWHCVE-TSNKTQEKLLLTGEETTQLKRI--------PS-QPRLN 310
Cdd:pfam15921 790 GELevlrSQERRLKEKVANMEVALDKASL-----QFAECQDiIQRQEQESVRLKLQHTLDVKELqgpgytsnSSmKPRLL 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 311 SPSERHIFHPSpgkaSPETQSSILSMPKTPPRVSRPKESPQK------------LKKQNNVQQFNTQSRKRKVSSDVLEq 378
Cdd:pfam15921 865 QPASFTRTHSN----VPSSQSTASFLSHHSRKTNALKEDPTRdlkqllqelrsvINEEPTVQLSKAEDKGRAPSLGALD- 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 379 vDTLTDDSKEMT-CEGLLHGDYC---MDLLALKEWFKPLPPVLspvHSPSLElvnvndnKPMSD-TQQENESSNEKSKTL 453
Cdd:pfam15921 940 -DRVRDCIIESSlRSDICHSSSNslqTEGSKSSETCSREPVLL---HAGELE-------DPSSCfTFPSTASPSVKNSAS 1008
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751363285 454 ASLHEELELSDIgdkKSLLKEE-EGTcslLCPDTLTRSTVSVDNLDSEKTSESQNVE 509
Cdd:pfam15921 1009 RSFHSSPKKSPV---HSLLTSSaEGS---IGSSSQYRSAKTIHSPDSVKDSQSLPIE 1059
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-245 |
1.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 41 TLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELE-----------NTKAELE 109
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekireleerieELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 110 LNQQRCKDVDRLKEKNAQIIILKE---KLEESLRKAEDTL------------KGQDLEN--EKLKNGKQLLEEdLQKMQD 172
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLsrleeeingieeRIKELEEkeERLEELKKKLKE-LEKRLE 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751363285 173 SLRKYHQTSEEHESLK--LENAKTLIL---KGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQK 245
Cdd:PRK03918 356 ELEERHELYEEAKAKKeeLERLKKRLTgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
28-304 |
2.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIvdtDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQtvkYEQMKTELENTKAE 107
Cdd:COG4372 29 LSEQLRKALFELDKLQEEL---EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 108 LELNQQRCK----DVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEE 183
Cdd:COG4372 103 LESLQEEAEelqeELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 184 HESLKLENAKTLILKGNLENELLVLKELKcQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPT 263
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIES-LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1751363285 264 IDKDKVRMLLEELWHCVETSNKTQEKLLLTGEETTQLKRIP 304
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-251 |
3.07e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYE---QMKTELENT 104
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 105 KAELElnqqrCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGqdLENEklkngkqllEEDLQKMQDSLRKYHQTS--- 181
Cdd:PRK03918 378 KKRLT-----GLTPEKLEKELEELEKAKEEIEEEISKITARIGE--LKKE---------IKELKKAIEELKKAKGKCpvc 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751363285 182 ----EEHESLKLENAKTLILKgNLENELLVLKELKCQ---QDKEVGALINEKRRLEEMLFTTQQ--NLNKLQKEFNKEK 251
Cdd:PRK03918 442 grelTEEHRKELLEEYTAELK-RIEKELKEIEEKERKlrkELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNLEE 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-299 |
3.45e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 9 NARGIASEATSGTCQNCTVLNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQ----KSQRESSTLHRQLDEVLLKL 84
Cdd:TIGR02168 656 RPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 85 EPLEKQTVKYEQMKTELEntkaelelnqqrckdvDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLE 164
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLS----------------KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 165 EdLQKMQDSLRK-YHQTSEEHESLKLENAKTLILKGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKL 243
Cdd:TIGR02168 800 A-LREALDELRAeLTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751363285 244 QKEFNKEKRSMSSQTDSEPTIDKD---------KVRMLLEELWHCVETSNKTQEKLLLTGEETTQ 299
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEElreleskrsELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
52-270 |
4.12e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 52 ILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQmktELENTKAELELNQQrckdvdRLKEKNAQIIIL 131
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELEK------EIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 132 KEKLEESLRKAEDT---------LKGQDLeNEKLKNGkQLLEEDLQKMQDSLRKYHQTSEEHESLK--LENAKTLI--LK 198
Cdd:COG4942 103 KEELAELLRALYRLgrqpplallLSPEDF-LDAVRRL-QYLKYLAPARREQAEELRADLAELAALRaeLEAERAELeaLL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751363285 199 GNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVR 270
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-253 |
4.49e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQREsstLHRQLDEVLLKLEPLEKQTvkyEQMKTELENTKAE 107
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEEELEELEEEL---EELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 108 LELNQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQkmqdslrkyhQTSEEHESL 187
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----------ERLERLEEE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751363285 188 KLENAKTLIlkgNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRS 253
Cdd:COG1196 423 LEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
76-252 |
4.53e-05 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 45.66 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 76 QLDEVLLKLEPLEKQTVKYEQMKTELENTKAEL--ELNQQRCKDVDRLKEKNAQIIIL----KEKLE---ESLRKAEDTL 146
Cdd:pfam10368 5 KIYDHLEEAVELEKPFEEQQEPLVELEKKEQELyeEIIELGMDEFDEIKKLSDEALENveerEELLEkekESIEEAKEEF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 147 KGQDLENEKLKNGKqlLEEDLQKMQDSLRK---YHQTSEEH--ESLKLENAktliLKGNLENELLVLKELKCQQDKevga 221
Cdd:pfam10368 85 KKIKEIIEEIEDEE--LKKEAEELIDAMEEryeAYDELYDAykKALELDKE----LYEMLKDEDLTLEELQEQIEK---- 154
|
170 180 190
....*....|....*....|....*....|.
gi 1751363285 222 lINEKRrlEEMLFTTQQnLNKLQKEFNKEKR 252
Cdd:pfam10368 155 -INESY--EEVKEANEQ-FNEYTKQYNELKK 181
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-299 |
5.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKSQRESSTLHRQLdEVLLKLEplEKQTVKYEQMKTELENTKAE----LELNQQRCKDVDRLKEKNAQIII 130
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKA-EEAKKAE--EARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 131 LKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKL---ENAKTLILKGNLENELLV 207
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeEAKKAEELKKKEAEEKKK 1717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 208 LKELKcQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVRMLLEELwhcvetsNKTQ 287
Cdd:PTZ00121 1718 AEELK-KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL-------DEED 1789
|
250
....*....|..
gi 1751363285 288 EKLLLTGEETTQ 299
Cdd:PTZ00121 1790 EKRRMEVDKKIK 1801
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-253 |
8.05e-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: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 61 DELQKSQRESSTLHRQLDEVLLKLEPLEKQtvkYEQMKTELENTKAELELNQQRCKDV-DRLKEKNAQIIILKEKLEEsL 139
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALeQELAALEAELAELEKEIAE-L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 140 RKAEDTLKGQ--DLENEKLKNGKQ------LLEEDLQKMQDSLRKYHQTSEEH----ESLKLENAKTLILKGNLENELLV 207
Cdd:COG4942 96 RAELEAQKEElaELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1751363285 208 LKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRS 253
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
63-238 |
1.27e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 63 LQKSQRESSTLHRQLDEVLlklEPLEKQTVKYEQMKTELENTKAELELNQQRCK--------DVDRLKEKNAQIIILKEK 134
Cdd:pfam07888 36 LEECLQERAELLQAQEAAN---RQREKEKERYKRDREQWERQRRELESRVAELKeelrqsreKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 135 LEE-----SLRKAEDTLKGQDLENE--KLKNGKQLLEEDLQKMQDSLRKYH----QTSEEHESLKLENAKTLILKGNLEN 203
Cdd:pfam07888 113 LSEekdalLAQRAAHEARIRELEEDikTLTQRVLERETELERMKERAKKAGaqrkEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190
....*....|....*....|....*....|....*
gi 1751363285 204 ELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQ 238
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-269 |
1.39e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKSQRESSTLH--RQLDEVLLKLEPLEKqtvKYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIIILK 132
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKK---KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 133 EKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDsLRKyhqtSEEHESLKLENAKTlilkgNLENELLVLKELK 212
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-LKK----AEEENKIKAEEAKK-----EAEEDKKKAEEAK 1750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751363285 213 CQQD--KEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKV 269
Cdd:PTZ00121 1751 KDEEekKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
107-310 |
2.09e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.13 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 107 ELELNQQRCKDvdrLKEKNAQIIILKEKLEESLRKAE-----DTLKGQDLENEKLKNGKQLLEEDLQKMQ---DSLRKYH 178
Cdd:pfam09787 1 NLESAKQELAD---YKQKAARILQSKEKLIASLKEGSgveglDSSTALTLELEELRQERDLLREEIQKLRgqiQQLRTEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 179 QTSEEHESLKLENAKTLIlkGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLF----TTQQNLNKLQKEFNKEK--- 251
Cdd:pfam09787 78 QELEAQQQEEAESSREQL--QELEEQLATERSARREAEAELERLQEELRYLEEELRrskaTLQSRIKDREAEIEKLRnql 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751363285 252 --RSMSSQTDSEPtidKDKVRMLLEELWH---CVETSNKTQEKLLLTGEET-TQLKRIPS----QPRLN 310
Cdd:pfam09787 156 tsKSQSSSSQSEL---ENRLHQLTETLIQkqtMLEALSTEKNSLVLQLERMeQQIKELQGegsnGTSIN 221
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
62-302 |
2.26e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 62 ELQKSQRESSTLHRQLDEvlLKLEpLEKQTVKYEQMKTELENTKAELELNQQRckdVDRLKEKNAQIIILKEKLEESLRK 141
Cdd:COG1196 233 KLRELEAELEELEAELEE--LEAE-LEELEAELAELEAELEELRLELEELELE---LEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 142 AEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLI-LKGNLENELLVLKELKCQQDKEVG 220
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAeAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 221 ALINEKRRLEEMLfTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVRMLLEELwhcvETSNKTQEKLLLTGEETTQL 300
Cdd:COG1196 387 ELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEAL 461
|
..
gi 1751363285 301 KR 302
Cdd:COG1196 462 LE 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
54-263 |
2.61e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 54 TEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQtvkYEQMKTELENTKAELELNQQrckdvdRLKEKNAQIIILKE 133
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEE---YNELQAELEALQAEIDKLQA------EIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 134 KLEESLRKA-------------------EDTLKGQDLENEKLKNGKQLLEEdLQKMQDSLRKY-HQTSEEHESLKLENAK 193
Cdd:COG3883 87 ELGERARALyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEE-LKADKAELEAKkAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 194 TLILKGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPT 263
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-204 |
2.97e-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: 45.44 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 41 TLKQKIVDTDHILTEYKEKCDELQKSQREsstLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAEL-----ELNQQRC 115
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKKERDELEAQLRELerkieELEAQIE 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 116 KDVDRLKEKNAQIIILKEKLE--ESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQD-----------SLRKYHQTSE 182
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvnmlaiqeyeeVLKRLDELKE 993
|
170 180
....*....|....*....|..
gi 1751363285 183 EHESLKLENAKTLILKGNLENE 204
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKK 1015
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
42-190 |
3.22e-04 |
|
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: 45.27 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 42 LKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEvllKLEPLEKQTVKYEQMKTELE-NTKAELELNQQRCKDVDR 120
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEELEEKYKELSASSEELSE---EKDALLAQRAAHEARIRELEeDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 121 LKEKNAQIIIL-------KEKLEESLRKAEDTLKGQDLENEKLKNGK-------QLLEEDLQKMQDSLRKYHQTSEEHES 186
Cdd:pfam07888 155 MKERAKKAGAQrkeeeaeRKQLQAKLQQTEEELRSLSKEFQELRNSLaqrdtqvLQLQDTITTLTQKLTTAHRKEAENEA 234
|
....
gi 1751363285 187 LKLE 190
Cdd:pfam07888 235 LLEE 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
49-306 |
4.19e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 49 TDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEP-LEKQTVKYEQMKTELENTKAELELnqqrckdvdRLKEKNAQ 127
Cdd:pfam05483 153 TRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAENARLEMHF---------KLKEDHEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 128 IIILKEKLEESLRKAEDT---LKGQDLENE-KLKNGKQLLEEDLQK--------------MQDSLRKYHQTSEEHESLKL 189
Cdd:pfam05483 224 IQHLEEEYKKEINDKEKQvslLLIQITEKEnKMKDLTFLLEESRDKanqleektklqdenLKELIEKKDHLTKELEDIKM 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 190 ENAKTLILKGNLENELLVLKELKCQQDKEVGALINEKRR------------------LEEMLFTTQQNLNKLQ---KEFN 248
Cdd:pfam05483 304 SLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtefeattcsLEELLRTEQQRLEKNEdqlKIIT 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751363285 249 KEKRSMSSQTDsEPTIDKDKVRMLLEELwhcvETSNKTQEKLLltgEETTQLKRIPSQ 306
Cdd:pfam05483 384 MELQKKSSELE-EMTKFKNNKEVELEEL----KKILAEDEKLL---DEKKQFEKIAEE 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-302 |
4.89e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKSQRESstlhRQLDEVLLKLEplEKQtvKYEQMKTELENTKAELELN---QQRCKDVDRLKEKNAQiiil 131
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEA----KKAEEAKKKAE--EAK--KADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEA---- 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 132 KEKLEEsLRKAEDTLKGQDLEN-EKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTlilkgnlENELLVLKE 210
Cdd:PTZ00121 1509 KKKADE-AKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK-------AEEDKNMAL 1580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 211 LKCQQDKEVgalinEKRRLEEMLFTTQQNLNKLQKEFNKEKRsmsSQTDSEPTIDKDKVRMLLEELWHCVETSNKTQEKL 290
Cdd:PTZ00121 1581 RKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEE---AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
250
....*....|....*.
gi 1751363285 291 LLTGEETT----QLKR 302
Cdd:PTZ00121 1653 KKAEEENKikaaEEAK 1668
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
28-306 |
5.14e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKivdTDHILTEYKEKCDELQK------SQRESSTLHRQLDEVLLKLEpleKQTVKYEQMKtEL 101
Cdd:TIGR01612 1123 LDQKIDHHIKALEEIKKK---SENYIDEIKAQINDLEDvadkaiSNDDPEEIEKKIENIVTKID---KKKNIYDEIK-KL 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 102 ENTKAELELNQ---QRCKDVDRLKEKNAQIIILkEKLEESLRKAEDTLKG-----QDLENEKLKN----GKQLLEEDLQK 169
Cdd:TIGR01612 1196 LNEIAEIEKDKtslEEVKGINLSYGKNLGKLFL-EKIDEEKKKSEHMIKAmeayiEDLDEIKEKSpeieNEMGIEMDIKA 1274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 170 MQDSLRKYHQTSEEHESLKLENAKTLilkGNLENellvlKELKCQQDKEVGALINEKRRleemlfTTQQNLNKLQKEFNK 249
Cdd:TIGR01612 1275 EMETFNISHDDDKDHHIISKKHDENI---SDIRE-----KSLKIIEDFSEESDINDIKK------ELQKNLLDAQKHNSD 1340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751363285 250 EKRSMSSQTDSEPTIDKDKVRMLLEELWHC---VETSNKT-------QEKLLLTGEETTQLKRIPSQ 306
Cdd:TIGR01612 1341 INLYLNEIANIYNILKLNKIKKIIDEVKEYtkeIEENNKNikdeldkSEKLIKKIKDDINLEECKSK 1407
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
23-195 |
5.48e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 23 QNCTVLNQSLDEYVAALLTLKQKIVDTDHILTEYKEKcdeLQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELE 102
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQ---IQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 103 NTKAELELNQQRCKDVDRLKEKNAQ-IIILKEKLEESLR--KAEDTLKGQDLENEKL---KNGKQLLEEDLQKMQDSLRK 176
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQdSEIVKNSKSELARipELEKELERLREHNKHLnenIENKLLLKEEVEDLKRKLER 239
|
170
....*....|....*....
gi 1751363285 177 YHQTSEEHESLKLENAKTL 195
Cdd:pfam05557 240 EEKYREEAATLELEKEKLE 258
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-252 |
5.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 52 ILTEYKEKCDELQKsQRESSTLHRQLDEVLLKLEpLEKQTVKYEQMKTELENTKAELELNQQRCKDVD-RLKEKNAQIII 130
Cdd:COG1196 194 ILGELERQLEPLER-QAEKAERYRELKEELKELE-AELLLLKLRELEAELEELEAELEELEAELEELEaELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 131 LKEKLEE--------------SLRKAEDTLKGQDLENEKLKNgkqlLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLI 196
Cdd:COG1196 272 LRLELEEleleleeaqaeeyeLLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751363285 197 -LKGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLfttQQNLNKLQKEFNKEKR 252
Cdd:COG1196 348 eAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQ 401
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
30-341 |
5.64e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 30 QSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTE---LENTKA 106
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 107 ELELNQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHES 186
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 187 LKLENAKTLilkgnLENELLVLKELKCQQDKEVG---ALINEKRRLEEMLFTTQQNLnKLQKEFNKEKRSMSSQTDSEPT 263
Cdd:TIGR00618 382 HTLQQQKTT-----LTQKLQSLCKELDILQREQAtidTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 264 IDK---DKVRMLLEELwhcvETSNKTQEKLLLTGEETTQ-----LKRIPSQPRLNSPSERHIfhpspgkaSPETQSSILS 335
Cdd:TIGR00618 456 LEKihlQESAQSLKER----EQQLQTKEQIHLQETRKKAvvlarLLELQEEPCPLCGSCIHP--------NPARQDIDNP 523
|
....*.
gi 1751363285 336 MPKTPP 341
Cdd:TIGR00618 524 GPLTRR 529
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
27-388 |
6.29e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 27 VLNQSLDEYVAALLTLKQKIVDTDHILTeykekcDELQKSQRESSTLH-------RQLD------EVLLKLepLEKQTVK 93
Cdd:PTZ00108 939 VLEQWEEEGIEKVFKLKSTISTTNMVLF------DENGKIKKYSDALDilkefylVRLDlykkrkEYLLGK--LERELAR 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 94 YEQM-KTELENTKAELELNQQRCKD-VDRLKEKN----AQIIILKE---KLEESLRKAEDTLKGQDLENEKLKN------ 158
Cdd:PTZ00108 1011 LSNKvRFIKHVINGELVITNAKKKDlVKELKKLGyvrfKDIIKKKSekiTAEEEEGAEEDDEADDEDDEEELGAavsydy 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 159 --GKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLILKgnlenELLVLKELKCQQDKEVGALINEKRRLEEMLFTT 236
Cdd:PTZ00108 1091 llSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLE-----DLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGK 1165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 237 QQNLNKLQKEFNKEKRSMSSQTDSEPTIDKD-KVRMLLEELWHCVETS-NKTQEKLLLTGEETTQLKRIPSQPRLNSPSE 314
Cdd:PTZ00108 1166 ASKLRKPKLKKKEKKKKKSSADKSKKASVVGnSKRVDSDEKRKLDDKPdNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKS 1245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751363285 315 RHIFHPSPGKASPETQSSILSM----PKTPPRVSRPKESPQKLKKQNNVQQFNTQSRKRKVSSDVLEQVDTLTDDSKE 388
Cdd:PTZ00108 1246 KKNNSSKSSEDNDEFSSDDLSKegkpKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKK 1323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
28-180 |
6.81e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCD------ELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTEL 101
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 102 ENTKAELE--LNQQRCKDVDRLKEKNAQIiilkEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDL--QKMQDSLRKY 177
Cdd:COG4717 173 AELQEELEelLEQLSLATEEELQDLAEEL----EELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEA 248
|
...
gi 1751363285 178 HQT 180
Cdd:COG4717 249 RLL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-299 |
7.32e-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: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 77 LDEVLLKLEPLEK---QTVKYEQMKTELENTKAELELNQQRC---------KDVDRLKEKNAQIIILKEKLEESLRKAED 144
Cdd:TIGR02169 193 IDEKRQQLERLRRereKAERYQALLKEKREYEGYELLKEKEAlerqkeaieRQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 145 TLKGQDLENEKLKNGKQL--------LEEDLQKMQDSLRKYHQtseEHESLKLENAKTLILKGNLENELLVLKELKCQQD 216
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLrvkekigeLEAEIASLERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 217 KEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSqtdseptidkdkVRMLLEELWHCVETSNKTQEKLLLTGEE 296
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------YREKLEKLKREINELKRELDRLQEELQR 417
|
...
gi 1751363285 297 TTQ 299
Cdd:TIGR02169 418 LSE 420
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
23-258 |
8.05e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 23 QNCTVLNQSLDEYVAALLTLKQKIVDTDHilteYKEKCDELQKSQRESSTLH-RQLDEVLLKLE-PLEKQTVKYEQMKTE 100
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQD----LTEKLSEAEDMLACEQHALlRKLQPEQDLQDvRLHLQQCSQELALKL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 101 LENTKAELELNQQRCKD----VDRLKEKNAQIIILKEKLEESLRKAEDTLKgqdlenEKLKNGKQLLEEDLQKMQDSLRK 176
Cdd:TIGR00618 646 TALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWK------EMLAQCQTLLRELETHIEEYDRE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 177 YHQTSEEHESLKLENAKTLILKGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSS 256
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
..
gi 1751363285 257 QT 258
Cdd:TIGR00618 800 LL 801
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
81-205 |
9.85e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 81 LLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCK---DVDR-LKEKNAQIiilkEKLEESLRKAEDTLKGQDLENEKL 156
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKlrnEFEKeLRERRNEL----QKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 157 KNGKQLLEEDLQKMQDSLRKYHQTSEEHES---LKLEN--------AKTLILKgNLENEL 205
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEeqlQELERisgltaeeAKEILLE-KVEEEA 167
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
80-257 |
1.69e-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: 42.44 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 80 VLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDV--------DRLKEKNAQIIILKEKL---EESLRKAEDTLKG 148
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALkkeekallKQLAALERRIAALARRIralEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 149 QDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLIlkgnleNELLVLKELKCQQDKEVGALINEKRR 228
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAV------RRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190
....*....|....*....|....*....|..
gi 1751363285 229 LEEM---LFTTQQNLNKLQKEFNKEKRSMSSQ 257
Cdd:COG4942 162 LAALraeLEAERAELEALLAELEEERAALEAL 193
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
31-271 |
2.15e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 31 SLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQ-------------- 96
Cdd:PTZ00440 485 SKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQsietlikdeklkrs 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 97 MKTELENTKAELELNQQRCKDVDRLKEKNAQIIILKEKL-EESLRKAEDTLKGQDLENEKLK-NGKQLLEEDLQKMQDSL 174
Cdd:PTZ00440 565 MKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELiNEALFNKEKFINEKNDLQEKVKyILNKFYKGDLQELLDEL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 175 RKYHqtsEEHESLKLENAKT---LILKGNLENELLVLKELKCQQ--------DKEVGALINEKRRLEEMLFTT-----QQ 238
Cdd:PTZ00440 645 SHFL---DDHKYLYHEAKSKedlQTLLNTSKNEYEKLEFMKSDNidniiknlKKELQNLLSLKENIIKKQLNNieqdiSN 721
|
250 260 270
....*....|....*....|....*....|...
gi 1751363285 239 NLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVRM 271
Cdd:PTZ00440 722 SLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQI 754
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
73-281 |
2.24e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.28 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 73 LHRQLDEVLLKLEPLEkQTVKYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKG-QDL 151
Cdd:cd00176 5 FLRDADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQErLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 152 ENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKtlilkgnlenELLVLKELKCQQDKEVGALINEKRRLEE 231
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEK----------EAALASEDLGKDLESVEELLKKHKELEE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751363285 232 MLFTTQQNLNKLQKEFnkEKRSMSSQTDSEPTIDK--DKVRMLLEELWHCVE 281
Cdd:cd00176 154 ELEAHEPRLKSLNELA--EELLEEGHPDADEEIEEklEELNERWEELLELAE 203
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
82-252 |
2.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 82 LKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDVDRLKEKNaqiiilKEKLEESLRKAedtlkgqdleNEKLKNGKQ 161
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK------EKELEEVLREI----------NEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 162 LLEEdLQKMQDSLRKYHQTSEEHESLKLENAKTLILKGNLENELLVLKELKCQQDKEVGALINEKRRLEEM--LFTTQQN 239
Cdd:PRK03918 219 LREE-LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIK 297
|
170
....*....|...
gi 1751363285 240 LNKLQKEFNKEKR 252
Cdd:PRK03918 298 LSEFYEEYLDELR 310
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
85-303 |
2.35e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 85 EPLEKQTVKYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIIILKEK---LEESLRKAEDTLKGQDLENEKLKNGKQ 161
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERredLEELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 162 LLEEDLQKMQDSLRKYHQTSEEH-ESLKLENAKTLILKGNLEN-----ELLVLKElkcQQDKEVGALiNEKRRleemlft 235
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEArEEVAELNSKLAELKERIESlerirTLLAAIA---DAEDEIERL-REKRE------- 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751363285 236 TQQNLNKLQKEFNKEKRSMSSQTDSEptIDKDKVRMLLEELWHCVETSNKTQEKL-LLTGEETTQLKRI 303
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAE--FDEARIEEAREDKERAEEYLEQVEEKLdELREERDDLQAEI 683
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
52-276 |
3.13e-03 |
|
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: 42.02 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 52 ILTEYKEKCDELQKSQR-ESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIii 130
Cdd:pfam05483 350 VVTEFEATTCSLEELLRtEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 131 lkEKLEESLRKAEDTLKGQdleneklkngKQLLEEDLQKMQDSLRKYhQTSEEHESLKLENAKTlilkgNLENELLVLKE 210
Cdd:pfam05483 428 --EKIAEELKGKEQELIFL----------LQAREKEIHDLEIQLTAI-KTSEEHYLKEVEDLKT-----ELEKEKLKNIE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751363285 211 LKCQQDK---EVGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIdKDKVRMLLEEL 276
Cdd:pfam05483 490 LTAHCDKlllENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVREEF 557
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
58-261 |
3.35e-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: 42.03 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 58 EKCDELQKSQRESSTLH---RQLDEVLLKLEPLEKQ-TVKYEQMKTELENTKAELE---------LNQQRCKDVDRLK-- 122
Cdd:pfam17380 375 SRMRELERLQMERQQKNervRQELEAARKVKILEEErQRKIQQQKVEMEQIRAEQEearqrevrrLEEERAREMERVRle 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 123 --EKNAQIIILKEKLEESLRKA----EDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEheslkLENAKTLI 196
Cdd:pfam17380 455 eqERQQQVERLRQQEEERKRKKleleKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKE-----MEERQKAI 529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751363285 197 LKGnlENELLVLKELKCQQDKEvgalinEKRRLEEMLFTTQQNLNKLQKeFNKEKRSMSSQTDSE 261
Cdd:pfam17380 530 YEE--ERRREAEEERRKQQEME------ERRRIQEQMRKATEERSRLEA-MEREREMMRQIVESE 585
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
61-171 |
3.40e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.92 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 61 DELQKSQRESSTLHRQLDEVLLKLEPLEKQTvkyEQMKTELENTKAELELNQQRCKDVD-RLKEKNAQIIILKEKLE--- 136
Cdd:pfam08614 64 EELAELYRSRGELAQRLVDLNEELQELEKKL---REDERRLAALEAERAQLEEKLKDREeELREKRKLNQDLQDELValq 140
|
90 100 110
....*....|....*....|....*....|....*
gi 1751363285 137 ESLRKAEDTLKgqDLENEklknGKQLLEEDLQKMQ 171
Cdd:pfam08614 141 LQLNMAEEKLR--KLEKE----NRELVERWMKRKG 169
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
53-232 |
3.50e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 53 LTEYKEKCDELQKSQRESstlhrqLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDvdRLKEKNAQIIILK 132
Cdd:PRK02224 514 LEERREDLEELIAERRET------IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE--EVAELNSKLAELK 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 133 EKLEeSLRKAEDTL-----KGQDLE--NEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLE-------NAKTLIlk 198
Cdd:PRK02224 586 ERIE-SLERIRTLLaaiadAEDEIErlREKREALAELNDERRERLAEKRERKRELEAEFDEARIEearedkeRAEEYL-- 662
|
170 180 190
....*....|....*....|....*....|....
gi 1751363285 199 GNLENELLVLKELKCQQDKEVGALINEKRRLEEM 232
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
108-250 |
4.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 108 LELnQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDLQKMQDSLRKY------HQTS 181
Cdd:COG1579 10 LDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnVRNN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751363285 182 EEHESL--KLENAKTLIlkGNLENELLVLKElkcqqdkEVGALINEKRRLEEMLFTTQQNLNKLQKEFNKE 250
Cdd:COG1579 89 KEYEALqkEIESLKRRI--SDLEDEILELME-------RIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
28-299 |
5.24e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 28 LNQSLDEYVAALLTLKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQLDEvLLKLEPLEKQTVKYEQMKTELENTK-- 105
Cdd:COG5022 976 LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE-LQSASKIISSESTELSILKPLQKLKgl 1054
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 106 AELELNQQRCKDVDRLKEKNAQIIIlkEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEED-LQKMQDSLRKYHQTSEEH 184
Cdd:COG5022 1055 LLLENNQLQARYKALKLRRENSLLD--DKQLYQLESTENLLKTINVKDLEVTNRNLVKPANvLQFIVAQMIKLNLLQEIS 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 185 ESLKLENAKTLILKGNLENELLVLKELKCQQD------KEVGALINEKRRLEEMLFTtqqNLNKLQKEFNKEKRS-MSSQ 257
Cdd:COG5022 1133 KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANlealpsPPPFAALSEKRLYQSALYD---EKSKLSSSEVNDLKNeLIAL 1209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1751363285 258 TDSEPTID--KDKVRMLLEELWHCVETSNKTQEKLLLTGEETTQ 299
Cdd:COG5022 1210 FSKIFSGWprGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTP 1253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
55-140 |
5.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKS-----QRESsTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQrcKDVDRL-------K 122
Cdd:PRK12704 76 ELRERRNELQKLekrllQKEE-NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE--EQLQELerisgltA 152
|
90
....*....|....*...
gi 1751363285 123 EKNAQIIIlkEKLEESLR 140
Cdd:PRK12704 153 EEAKEILL--EKVEEEAR 168
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
74-275 |
5.81e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 74 HRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDL-- 151
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLkl 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 152 --ENEKLKNGKQLLEEDLQKMQDSLRKYHQTSEEHESLKLENAKTLilKGNLENELLVLKELKCQQDKEVGALINEKRRL 229
Cdd:pfam02463 235 neERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE--KKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1751363285 230 EEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTIDKDKVRMLLEE 275
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE 358
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
61-388 |
6.04e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 61 DELQKSQRESSTLHRQLDEvlLKLEPLEKQTVKYEQMKTELENTKAE---------LELNQQRCKDVDRL---------K 122
Cdd:PTZ00108 1024 GELVITNAKKKDLVKELKK--LGYVRFKDIIKKKSEKITAEEEEGAEeddeaddedDEEELGAAVSYDYLlsmpiwsltK 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 123 EKnaqiiilKEKLEESLRKAEDtlkgqdlENEKLKNG--KQLLEEDLQKMQDSLRKYHQT--SEEHESLKLENAKTLILK 198
Cdd:PTZ00108 1102 EK-------VEKLNAELEKKEK-------ELEKLKNTtpKDMWLEDLDKFEEALEEQEEVeeKEIAKEQRLKSKTKGKAS 1167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 199 GNLENELLVLKELKCQQDKE-------------VGALINEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSSQTDSEPTI- 264
Cdd:PTZ00108 1168 KLRKPKLKKKEKKKKKSSADkskkasvvgnskrVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKk 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 265 --DKDKVRMLLEELWHCVETSNKTQEKL---LLTGEETTQLKRIPSQPRLNSPSERHIfhPSPGKASPETQSSILSMPKT 339
Cdd:PTZ00108 1248 nnSSKSSEDNDEFSSDDLSKEGKPKNAPkrvSAVQYSPPPPSKRPDGESNGGSKPSSP--TKKKVKKRLEGSLAALKKKK 1325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1751363285 340 PPR--VSRPKESPQKLKKQNNVQQFNTQSR--KRKVSSDVLEQVDTLTDDSKE 388
Cdd:PTZ00108 1326 KSEkkTARKKKSKTRVKQASASQSSRLLRRprKKKSDSSSEDDDDSEVDDSED 1378
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
83-315 |
6.20e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 83 KLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDVdrLKEKNAQIIILKEKLEESlrkaedtlKGQDLEnEKLKNGKQL 162
Cdd:PTZ00440 982 HLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDL--IKKQHDDIIELIDKLIKE--------KGKEIE-EKVDQYISL 1050
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 163 LEEDLQKMQ-----DSLRKYHQTSEEHESLKLENAKTLILkGNLENELLVLKELKCQQDKEVGALINEKRRLEEMLFTTQ 237
Cdd:PTZ00440 1051 LEKMKTKLSsfhfnIDIKKYKNPKIKEEIKLLEEKVEALL-KKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKK 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 238 QNLNKLQKEFNKEKRSMSSQTDSEPTI-DKDKVRMLLEELW--HCVETSNKTQEKLLLTGEETTQLKRIPSQPRLNSPSE 314
Cdd:PTZ00440 1130 KSLEKIYKQMEKTLKELENMNLEDITLnEVNEIEIEYERILidHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKE 1209
|
.
gi 1751363285 315 R 315
Cdd:PTZ00440 1210 R 1210
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
42-369 |
6.95e-03 |
|
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: 40.86 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 42 LKQKIVDTDHILTEYKEKCDELQKSQRESSTLHRQL-----------DEVLLKLEPLEKQTVKYEQMKTELENTKAELEl 110
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatkticqltEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 111 nQQRCKDVDRLKEKNAQIIILKEKLEESLRKAEDTLKGQDLENEKLKNGKQLLEEDlQKMQDSLRKYHQTSEEHESLKLE 190
Cdd:pfam05483 363 -ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED-EKLLDEKKQFEKIAEELKGKEQE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 191 NAKTLILK----GNLENELLVLKELKCQQDKEVGALIN--EKRRLEEMLFTTQQNLNKLQ-KEFNKEKRSMS----SQTD 259
Cdd:pfam05483 441 LIFLLQARekeiHDLEIQLTAIKTSEEHYLKEVEDLKTelEKEKLKNIELTAHCDKLLLEnKELTQEASDMTlelkKHQE 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 260 SEPTIDKDKVRMlLEELWHCVETSNKTQEKLLLTGEETTQlKRIPSQPRLNSpSERHIFHPSPGKASPETQSSILSMPKT 339
Cdd:pfam05483 521 DIINCKKQEERM-LKQIENLEEKEMNLRDELESVREEFIQ-KGDEVKCKLDK-SEENARSIEYEVLKKEKQMKILENKCN 597
|
330 340 350
....*....|....*....|....*....|
gi 1751363285 340 PPRvsrpKESPQKLKKQNNVQQFNTQSRKR 369
Cdd:pfam05483 598 NLK----KQIENKNKNIEELHQENKALKKK 623
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-303 |
7.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 55 EYKEKCDELQKSQRESstlhRQLDEVLLKLEPLEKQTvkYEQMKTELENTKAELELNQQRCKDVDRLKEKNAQIIILKEK 134
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEA----KKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 135 LEESLRKAEDTLKGQDLEN--EKLKNGKQLLEEDLQKMqdSLRKYHQTSEEHESLKLENAKTLILKGNLENELLVLKELK 212
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKNM--ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 213 CQQDKEVGALINEKRRLEEMLFTTQQNLNKLQK-----EFNKEKRSMSSQTDSEptiDKDKVrmllEELWHCVETSNKTQ 287
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeEENKIKAAEEAKKAEE---DKKKA----EEAKKAEEDEKKAA 1691
|
250
....*....|....*.
gi 1751363285 288 EKLLLTGEETTQLKRI 303
Cdd:PTZ00121 1692 EALKKEAEEAKKAEEL 1707
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
62-176 |
7.08e-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: 39.50 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 62 ELQKSQRESSTLHRQLDEVLLKLEPLEKQTVKYEQMKTELENTKAELELNQQRCKDV----DRLKEKNAQiiiLKEKLEE 137
Cdd:pfam13851 48 LMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLEKELKDLkwehEVLEQRFEK---VERERDE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1751363285 138 SLRKAEDTLkgQDL-ENEKLKNgkQLLEEDLQKMQDSLRK 176
Cdd:pfam13851 125 LYDKFEAAI--QDVqQKTGLKN--LLLEKKLQALGETLEK 160
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
48-256 |
7.30e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 48 DTDHI--LTEYKEKCDELQKSQRESstlhRQLDEVLLKLEP----LEKQTVKYEQMKTELENTKAELELNQQRC------ 115
Cdd:COG3096 888 DETLAdrLEELREELDAAQEAQAFI----QQHGKALAQLEPlvavLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalsev 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 116 ---------KDVDRLKEKNAQiiiLKEKLEESLRKAEDTLKGQDlenEKLKNGKQLLEEDLQKMQdSLRKYHQtseehes 186
Cdd:COG3096 964 vqrrphfsyEDAVGLLGENSD---LNEKLRARLEQAEEARREAR---EQLRQAQAQYSQYNQVLA-SLKSSRD------- 1029
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363285 187 lklenAKTLILKgNLENELLVLkELKCQQDKEVGALInEKRRLEEMLFTTQQNLNKLQKEFNKEKRSMSS 256
Cdd:COG3096 1030 -----AKQQTLQ-ELEQELEEL-GVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| |
