|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-118 |
1.20e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 87.32 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 2 NPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYG 81
Cdd:COG0666 147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907077947 82 ALTGDKLILQLLHESARRSSPPSASLEEDSGEASSQN 118
Cdd:COG0666 227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-93 |
1.55e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 84.24 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 2 NPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYG 81
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
90
....*....|..
gi 1907077947 82 ALTGDKLILQLL 93
Cdd:COG0666 194 AENGHLEIVKLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-93 |
1.52e-15 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 78.07 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 2 NPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYG 81
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
90
....*....|..
gi 1907077947 82 ALTGDKLILQLL 93
Cdd:COG0666 161 AANGNLEIVKLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1-71 |
1.24e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.24e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907077947 1 MNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAtnDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITD 71
Cdd:pfam12796 23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-99 |
2.11e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.91 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 2 NPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYG 81
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
|
90
....*....|....*...
gi 1907077947 82 ALTGDKLILQLLHESARR 99
Cdd:COG0666 260 AAAGAALIVKLLLLALLL 277
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
12-93 |
1.32e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 12 LIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDalGQDATHYGALTGDKLILQ 91
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
..
gi 1907077947 92 LL 93
Cdd:pfam12796 79 LL 80
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
640-874 |
3.35e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 640 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEH 719
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE---LAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALD 799
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907077947 800 KAKEKDKKITDLSKEvftlkEALKVQQSTPASSKEEEALRGQVTALQQQIQEEAREHGAVVALYRTHLLYAIQGQ 874
Cdd:COG1196 411 ALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-851 |
6.56e-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: 63.15 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 151 EEIVRLRQERGRLLQKIRGLEQHKE--RRRKEPLEAEASSVHS----LERQVQELQQMLAEKQEEKESLGREVESLQSRL 224
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQilRERLANLERQLEELEAqleeLESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 225 SLLENERENTSydvATLQDEEGEMPDFPGADALMPK------NQSPSAEEIVASLQEQVAQLTRQNQELLEKVQiLEEFE 298
Cdd:TIGR02168 361 EELEAELEELE---SRLEELEEQLETLRSKVAQLELqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLE-EAELK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 299 KDEAQMAEESQAEVVPLVLYESLRAELEQLRRQYTEAMhsqqqqqegEPPRAQEGEETAYQEIKDKGITIQNgpsvpdlN 378
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAE---------QALDAAERELAQLQARLDSLERLQE-------N 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 379 GTTYAETKANGME--LQAGGSKGVwnteagVSEAAPIEPE-AAGSEATGKDRLAAKEMDTSATMAEALN----------- 444
Cdd:TIGR02168 501 LEGFSEGVKALLKnqSGLSGILGV------LSELISVDEGyEAAIEAALGGRLQAVVVENLNAAKKAIAflkqnelgrvt 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 445 VKALGDNAESEPVAAEDTGGKENPGMK---------ADEVDVLAQAGLTGTVIRNMEAIGVRDtgIQATGLEAKAVKTTG 515
Cdd:TIGR02168 575 FLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfDPKLRKALSYLLGGVLVVDDLDNALEL--AKKLRPGYRIVTLDG 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 516 VQATVAEVIGVKVTGVQTTAIE-AIGVKDTTQVATGAQADCWQAT-EADCTGAQDTAMEPTGAQATVTETTEAETSGTED 593
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILErRREIEELEEKIEELEEKIAELEkALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 594 PCAAILhpgAAAAALQAELETRIRGLEEALRRREREAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERAR 673
Cdd:TIGR02168 733 KDLARL---EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 674 TEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQ 753
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 754 REALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEK-DKKITDLSKEVFTLKEAlkVQQSTPASS 832
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEE--AEALENKIE 964
|
730
....*....|....*....
gi 1907077947 833 KEEEALRGQVTALQQQIQE 851
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
640-897 |
1.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 640 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEH 719
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE---LEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALD 799
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 800 KAKEKDKKITDLSKEVFTLKEALKvqqstpasSKEEEALRGQVTALQQQIQEEAREHGAVVALYRTHLLYAIQGQMDEDV 879
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250
....*....|....*...
gi 1907077947 880 QCILSQILQMQRLQAQGR 897
Cdd:COG1196 504 EGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
615-879 |
3.43e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 615 RIRGLEEALRRREREAAAeleaargRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELS 694
Cdd:COG1196 299 RLEQDIARLEERRRELEE-------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 695 STVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAE 774
Cdd:COG1196 372 AELAEAEEELEELAEE---LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 775 QQLRGLRTEAERARQAQSRAQEALDKAKEKDKKItDLSKEVFTLKEALKVQQSTPASSKEEEALRGQVTALQQQIQEEAR 854
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
250 260
....*....|....*....|....*
gi 1907077947 855 EHGAVVALYRTHLLYAIQGQMDEDV 879
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIV 552
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
10-61 |
8.97e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 8.97e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907077947 10 TPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLL 61
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
614-870 |
6.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 614 TRIRGLEEALRRRE----------REAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQAL 683
Cdd:COG1196 253 AELEELEAELAELEaeleelrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 684 AASEARVAELSSTVDAAREELErmrgasvpadEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSER 763
Cdd:COG1196 333 EELEEELEELEEELEEAEEELE----------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 764 HAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQStpASSKEEEALRGQVT 843
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--ELLEEAALLEAALA 480
|
250 260
....*....|....*....|....*..
gi 1907077947 844 ALQQQIQEEAREHGAVVALYRTHLLYA 870
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-861 |
9.62e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 152 EIVRLRQERGRLLQKIRGLeQHKERRRKEPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENER 231
Cdd:TIGR02168 233 RLEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 232 ENTSYDVATLQ---DEEGEMPDFPGADALMPKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEE-FEKDEAQMAEE 307
Cdd:TIGR02168 312 ANLERQLEELEaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 308 SQAEvvplvlyESLRAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKdkgitiqngpsvpdlngTTYAETKA 387
Cdd:TIGR02168 392 ELQI-------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-----------------AELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 388 NGMELQAGGSKGVWNTE---AGVSEAAPIEPEAAGSEATGKDRLAAKEMDTSATMAEALNVKALGDNAE----SEPVAAE 460
Cdd:TIGR02168 448 ELEELQEELERLEEALEelrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 461 dtggkenpGMKADE-----VDVLAQAGLTGTVIRNMEAIGV------RDTGIQATGLEAKAVKTTGVQATVAEVIgVKVT 529
Cdd:TIGR02168 528 --------LISVDEgyeaaIEAALGGRLQAVVVENLNAAKKaiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL-KNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 530 GVQTTAIEAIGVKDTTQVATGAQADcwqateadctgaqDTAMEPTGAQATVTETTEAETSGTEDPCAAILHPGAaaaalq 609
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYLLG-------------GVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG------ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 610 aeletRIRGLEEALRRREREAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEAR 689
Cdd:TIGR02168 660 -----VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 690 VAELSSTVDAAREELERMRGASVPAD-----------EHEHALSALRDHVTRLQAQLADLARRHEK-------------- 744
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEaeieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdelraeltl 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 745 TSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKV 824
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
730 740 750
....*....|....*....|....*....|....*..
gi 1907077947 825 QQSTpaSSKEEEALRGQVTALQQQIQEEAREHGAVVA 861
Cdd:TIGR02168 895 ELEE--LSEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
639-892 |
1.32e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 639 GRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRG----ASVPA 714
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 715 DEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEA----ERARQA 790
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 791 QSRAQEALDKAKEKDKKITDLSKEVFTLKEalkvqqstpasskEEEALRGQVTALQQQIQEEAREHGAVVALYRT----- 865
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSE-------------DIESLAAEIEELEELIEELESELEALLNERASleeal 889
|
250 260
....*....|....*....|....*..
gi 1907077947 866 HLLYAIQGQMDEDVQCILSQILQMQRL 892
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRE 916
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
642-803 |
1.67e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 642 AEAEEAARGRSRELEALRELLA--TATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGA--SVPADEH 717
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 718 EH----------ALSALRDHVTRLQAQLADLARRHEkTSAEVFQVQREalfmkserhAAEAQLATAEQQLRGLRTEAERA 787
Cdd:COG4913 341 EQlereierlerELEERERRRARLEALLAALGLPLP-ASAEEFAALRA---------EAAALLEALEEELEALEEALAEA 410
|
170
....*....|....*.
gi 1907077947 788 RQAQSRAQEALDKAKE 803
Cdd:COG4913 411 EAALRDLRRELRELEA 426
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-95 |
1.69e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.80 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 1 MNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHY 80
Cdd:COG0666 47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126
|
90
....*....|....*
gi 1907077947 81 GALTGDKLILQLLHE 95
Cdd:COG0666 127 AAYNGNLEIVKLLLE 141
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
625-855 |
3.04e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 625 RREREAAAEleaargRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREEL 704
Cdd:COG1196 224 ELEAELLLL------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 705 ERMRGASVPADEHEHALSALRDhvtRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQlrgLRTEA 784
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAE 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907077947 785 ERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQstpassKEEEALRGQVTALQQQIQEEARE 855
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL------ERLERLEEELEELEEALAELEEE 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-780 |
3.76e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 152 EIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENER 231
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 232 ENTSYDVATLQDEEgempdfpgadalmpknqspsaEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQAE 311
Cdd:COG1196 312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 312 VvplvlyESLRAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKDkgitiqngpsvpdlngttyAETKANGME 391
Cdd:COG1196 371 E------AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL-------------------ERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 392 LQAggskgvwnTEAGVSEAAPIEPEAAGSEATGKDRLAAKEMDTSATMAEALNVKALGDNAESEPVAAEDTggkenpgmK 471
Cdd:COG1196 426 LEE--------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--------A 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 472 ADEVDVLAqagltgtvirnmEAIGVRDTGIQATGLEAKAVKTTGVQATVAEVIGV-----KVTGVQTTAIEAIGVKDTTQ 546
Cdd:COG1196 490 AARLLLLL------------EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaayeAALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 547 VATGAQADCWQATEADCTGAQDTAMEPTGAQATVTETTEAETSGTEDPCAAIlhpgaaaaaLQAELETRIRGLEEALRRR 626
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR---------EADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 627 EREAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELER 706
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907077947 707 MRGASVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFmksERHAAEAQLATAEQQLRGL 780
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP---DLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
640-858 |
6.71e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 640 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHEH 719
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 ALSALRdhvtrlQAQLADLARRHEKTSAEVFQVQREALFMKSERhaaeAQLATAEQQLRGLRTEAERARQAQSRAQEALD 799
Cdd:COG4942 122 LALLLS------PEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 800 KAK-EKDKKITDLSKEVFTLKEALKVQQstpassKEEEALRGQVTALQQQIQEEAREHGA 858
Cdd:COG4942 192 ALKaERQKLLARLEKELAELAAELAELQ------QEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
653-861 |
8.70e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 653 RELEALRELLATATATGERARTEAAELRQALAA---------SEARVAELSSTVDAAREELERMRGASvpadehehalsa 723
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASS------------ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 724 lrDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGL--RTEAERARQAQSRAQEALDKA 801
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 802 KEKDKKiTDLSKEVFTLKEALkvqqstpasSKEEEALRGQVTALQQQIQEEAREHGAVVA 861
Cdd:COG4913 763 VERELR-ENLEERIDALRARL---------NRAEEELERAMRAFNREWPAETADLDADLE 812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
692-855 |
9.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 692 ELSSTVDAARE---ELERMRGASVPADEHEHALSALRDHVTRLQAQLADLAR-RHEKTSAEVFQVQREALFMKSERHAAE 767
Cdd:COG4913 222 DTFEAADALVEhfdDLERAHEALEDAREQIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 768 AQLATAEQQLRGLRTEAERARQAQSRAQEALDKA------------KEKDKKITDLSKEVFTLKEALK-VQQSTPASSKE 834
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlereiERLERELEERERRRARLEALLAaLGLPLPASAEE 381
|
170 180
....*....|....*....|.
gi 1907077947 835 EEALRGQVTALQQQIQEEARE 855
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA 402
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
16-137 |
1.78e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 16 AQMCHTDLC-----------RLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALT 84
Cdd:PTZ00322 79 AHMLTVELCqlaasgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 85 GDKLILQLL-------HESARRSSPPSASLEEDSGEASsqnSVSSHekqgAPKKRKAPQP 137
Cdd:PTZ00322 159 GFREVVQLLsrhsqchFELGANAKPDSFTGKPPSLEDS---PISSH----HPDFSAVPQP 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
640-850 |
6.60e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 640 RFAEAEEAARGRSR---ELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADE 716
Cdd:PRK02224 500 RAEDLVEAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 717 HEHALSALRDHVTRLQAQLADLA-------RRHEKTS--AEVFQVQREALFMKSERHaaeAQLATA--EQQLRGLRTEAE 785
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIAdaedeieRLREKREalAELNDERRERLAEKRERK---RELEAEfdEARIEEAREDKE 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907077947 786 RARQAQSRAQEALDkakEKDKKITDLSKEVFTLKEALkvqqstpassKEEEALRGQVTALQQQIQ 850
Cdd:PRK02224 657 RAEEYLEQVEEKLD---ELREERDDLQAEIGAVENEL----------EELEELRERREALENRVE 708
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
678-855 |
1.35e-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: 49.28 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 678 ELRQALAASEARVAELSstVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREAL 757
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEE---LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 758 FMKSERHAAEAQLATAEQQLRGLRTEAERA----RQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKvqqstpASSK 833
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELeaqlEELESKLDELAEELAELEEKLEELKEELESLEAELE------ELEA 365
|
170 180
....*....|....*....|..
gi 1907077947 834 EEEALRGQVTALQQQIQEEARE 855
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSK 387
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
643-851 |
1.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 643 EAEEAARGR-SRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAR--EELERMRGASVPADEHEH 719
Cdd:PTZ00121 1165 KAEEARKAEdAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKK 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 ALSALRDHVTRL--QAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQA---QSRA 794
Cdd:PTZ00121 1245 AEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKA 1324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907077947 795 QEALDKAKEKDKKITDLSK--------EVFTLKEALKVQQSTPASSKEEEALRGQVTALQQQIQE 851
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKaaeaakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
670-891 |
1.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 670 ERART--EAAELrqALAASEARVAELSSTVDAAREEL----ERMRGASVPADEHEHALSALR---DHVTRLQAQladlar 740
Cdd:PRK04863 424 ERAKQlcGLPDL--TADNAEDWLEEFQAKEQEATEELlsleQKLSVAQAAHSQFEQAYQLVRkiaGEVSRSEAW------ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 741 rhektsaevfQVQREALfmksERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKE 820
Cdd:PRK04863 496 ----------DVARELL----RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 821 ALKVQQSTPASSKEE-----EALRGQVTALQQQIQE-EARE---HGAVVALYRthlLYAIQGQMDEDVQCILSQILQMQR 891
Cdd:PRK04863 562 ELEARLESLSESVSEarerrMALRQQLEQLQARIQRlAARApawLAAQDALAR---LREQSGEEFEDSQDVTEYMQQLLE 638
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-335 |
1.88e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 147 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 226
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 227 LENERENTSYDVATLQDEEGEmpdfpgadalmpknqspSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAE 306
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEA-----------------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180
....*....|....*....|....*....
gi 1907077947 307 ESQAEVVPLVLYESLRAELEQLRRQYTEA 335
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
643-837 |
3.81e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 643 EAEEAARGRSRELEALRELLATATATGERARTEAAELRQA---------LAASEARVAELSSTVDAAREELERMRgasvP 713
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkkaeekKKADEAKKAEEKKKADEAKKKAEEAK----K 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 714 ADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARqaqsR 793
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK----K 1392
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907077947 794 AQEALDKAKEKDKKITDLSKEVFTLKEALKVQQSTPASSKEEEA 837
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
639-859 |
4.79e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 639 GRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEAR-------------------VAELSSTVDA 699
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelskleeeVSRIEARLRE 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 700 AREELER-----------MRGASVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEA 768
Cdd:TIGR02169 817 IEQKLNRltlekeylekeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 769 QLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEvftlkealkvqqstPASSKEEEALRGQVTALQQQ 848
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--------------DEEIPEEELSLEDVQAELQR 962
|
250
....*....|.
gi 1907077947 849 IQEEAREHGAV 859
Cdd:TIGR02169 963 VEEEIRALEPV 973
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
41-94 |
5.34e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 5.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907077947 41 GRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLH 94
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
93-855 |
5.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 93 LHESARRSSPPSASLEEDSGEA--SSQNSVSSHEKQGAPKKRKAPQP---PASTPVPDDRDAYE----EIVRLRQERGRL 163
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAkkKAEDARKAEEARKAEDARKAEEArkaEDAKRVEIARKAEDarkaEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 164 LQKIRGLEQHKE---RRRKEPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENERENTSYDvat 240
Cdd:PTZ00121 1179 EAARKAEEVRKAeelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR--- 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 241 lQDEEGEMPDFPGADALMPKNQSPSAEEIVASLQEQVAQLTRQNQEllekVQILEEFEK--DEAQMAEESQAEVvplvly 318
Cdd:PTZ00121 1256 -KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE----KKKADEAKKkaEEAKKADEAKKKA------ 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 319 ESLRAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKDKgitiqngpsvpdlNGTTYAETKANGMELQAGGSK 398
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE-------------KKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 399 GVWNTEAGVSEAAPIEPEAAGSEATGKDRLAAKEMDTSATMAEALNVKA-LGDNAESEPVAAEDTGGKENPGMKADEVDv 477
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKAEEAKKKAEEAK- 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 478 laqagltgtvirnmeaigvrdtgiqatglEAKAVKTTGVQATVAEVIGVKVTGVQTTAIEAIGVKDTTQVATGAQadcwQ 557
Cdd:PTZ00121 1471 -----------------------------KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK----K 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 558 ATEADCTGAQDTAMEPTGAQATVTETteaetsgtedpcaailhpgAAAAALQAELETRIRGLEEALRRREREAAAELEAA 637
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAE-------------------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 638 RGRFAE-AEEAARGRSRELEALREllatatatgERARTEAAELRQalaASEARVAelSSTVDAAREELERMRGASVPADE 716
Cdd:PTZ00121 1579 ALRKAEeAKKAEEARIEEVMKLYE---------EEKKMKAEEAKK---AEEAKIK--AEELKKAEEEKKKVEQLKKKEAE 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 717 HEHALSALRDHVTRLQAQLADLARRHE--KTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTE----AERARQA 790
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKA 1724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907077947 791 QS----RAQEALDKAKEKDKKITDLSKEVftlKEALKVQQSTPASSKEEEALRGQVTALqqqIQEEARE 855
Cdd:PTZ00121 1725 EEenkiKAEEAKKEAEEDKKKAEEAKKDE---EEKKKIAHLKKEEEKKAEEIRKEKEAV---IEEELDE 1787
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
83-364 |
6.75e-05 |
|
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: 46.66 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 83 LTGDKLILQLLHESARRSSPpSASLEEDSGEASSQNSVSSHEKQGA---PKKRKAPQPPASTPVPDDRDA--YEEIVRLR 157
Cdd:pfam17380 265 MTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKArevERRRKLEEAEKARQAEMDRQAaiYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 158 QERGRLLQKIRGLEQHKE--RRRKEPLEAEASSVHSLERqvqelqqMLAEKQEEKESLGREVESLQsRLSLLENERENTs 235
Cdd:pfam17380 344 MERERELERIRQEERKREleRIRQEEIAMEISRMRELER-------LQMERQQKNERVRQELEAAR-KVKILEEERQRK- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 236 ydvatLQDEEGEMPDfpgadalMPKNQSPSAEEIVASLQEQVA-QLTRQNQELLEKVQILE----------------EFE 298
Cdd:pfam17380 415 -----IQQQKVEMEQ-------IRAEQEEARQREVRRLEEERArEMERVRLEEQERQQQVErlrqqeeerkrkklelEKE 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907077947 299 KDEAQMAEESQAEVVPLVLYESLRAELEQLRRQY---TEAMHSQQQQQEGEPPRAQEGEETAYQEIKDK 364
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlleKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-823 |
6.98e-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: 46.97 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 640 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEH 719
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE---LRELES 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREAlfmkSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQ---- 795
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL----SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikel 984
|
170 180 190
....*....|....*....|....*....|...
gi 1907077947 796 -----EALDKAKEKDKKITDLSKEVFTLKEALK 823
Cdd:TIGR02168 985 gpvnlAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
642-828 |
8.92e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 642 AEAEEAargrsreLEALRE--LLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHEh 719
Cdd:COG3206 192 EEAEAA-------LEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQRealfmksERHAAEAQLATAEQQ-LRGLRTEAERARQAQSRAQEAL 798
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQL 336
|
170 180 190
....*....|....*....|....*....|
gi 1907077947 799 DKAKEKDKKITDLSKEVFTLKEALKVQQST 828
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
5-105 |
9.76e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.40 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 5 DRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALT 84
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
|
90 100
....*....|....*....|.
gi 1907077947 85 GDKLILQLLHESARRSSPPSA 105
Cdd:PLN03192 602 KHHKIFRILYHFASISDPHAA 622
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-331 |
1.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 141 TPVPDDRDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEP-LEAEASSVHSLERQVQELQQMLAEKQEEKESL------ 213
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELeaqirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 214 --GREVESLQSRLSLLENERENTSYDVATLQDeegempdfpGADALmpKNQSPSAEEIVASLQEQVAQLTRQNQELLEKV 291
Cdd:COG4913 335 ngGDRLEQLEREIERLERELEERERRRARLEA---------LLAAL--GLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907077947 292 QiLEEFEKDEAQMAEESQaevvplvlYESLRAELEQLRRQ 331
Cdd:COG4913 404 E-EALAEAEAALRDLRRE--------LRELEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
721-880 |
1.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 721 LSALRDHVTRLQAQLADLARRHE--KTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEAL 798
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 799 DKAKEKDKKITDLSKEVFTLKEALKvqqstpASSKEEEALRGQVTALQQQIQEEAREHGAvvALYRTHLLYAIQGQMDED 878
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELE------QAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDAVERELREN 770
|
..
gi 1907077947 879 VQ 880
Cdd:COG4913 771 LE 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-331 |
1.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 151 EEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEASSVHSLERQvQELQQMLAEKQEEKESLGREVESLQSRLSLLENE 230
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 231 RENTSYDVATLQDEEgempdfpgadalmpKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQA 310
Cdd:COG1196 346 LEEAEEELEEAEAEL--------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180
....*....|....*....|.
gi 1907077947 311 EvvpLVLYESLRAELEQLRRQ 331
Cdd:COG1196 412 L---LERLERLEEELEELEEA 429
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
45-98 |
1.31e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.64 E-value: 1.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907077947 45 LMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLHESAR 98
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
147-334 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 147 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAE-----------------ASSVHSLERQVQELQQMLAEKQEE 209
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkekreyegyelLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 210 KESLGREVESLQSRLSLLENERENTSYDVATLQDEEgempdfpgadALMPKNQSPSAEEIVASLQEQVAQLTRQNQELLE 289
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE----------QLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907077947 290 KVQILE-EFEKDEAQMA------EESQAEVVPLV-LYESLRAELEQLRRQYTE 334
Cdd:TIGR02169 323 RLAKLEaEIDKLLAEIEelereiEEERKRRDKLTeEYAELKEELEDLRAELEE 375
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-360 |
1.83e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 151 EEIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENE 230
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 231 RENTSYDVATLQDEEGEMpdfpgadalmpknqspsAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQA 310
Cdd:COG1196 367 LLEAEAELAEAEEELEEL-----------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907077947 311 EVVPLVLYESLRAELEQLRRQYTEAmhsQQQQQEGEPPRAQEGEETAYQE 360
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAEL---EEEEEALLELLAELLEEAALLE 476
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
709-822 |
2.26e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 709 GASVPADEHEHALSALRDHVTRLQAQLADLARrhektsaEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAErar 788
Cdd:PRK11448 132 GPFVPPEDPENLLHALQQEVLTLKQQLELQAR-------EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE--- 201
|
90 100 110
....*....|....*....|....*....|....
gi 1907077947 789 QAQSRAQEALDKAKEKDKKITDLSKEVFTLKEAL 822
Cdd:PRK11448 202 QLQEKAAETSQERKQKRKEITDQAAKRLELSEEE 235
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1-93 |
2.98e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.18 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 1 MNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHY 80
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
90
....*....|...
gi 1907077947 81 GALTGDKLILQLL 93
Cdd:PHA02874 197 AAEYGDYACIKLL 209
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
191-305 |
3.08e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 191 SLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENERENtsydVATLQDE-EGEMPDFPGADALMP------KNQS 263
Cdd:PRK09039 57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSR----LQALLAElAGAGAAAEGRAGELAqeldseKQVS 132
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907077947 264 PSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKD-EAQMA 305
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDREsQAKIA 175
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
27-75 |
3.29e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907077947 27 LLQQG-AATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQ 75
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL 50
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
2-61 |
3.36e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 3.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 2 NPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLL 61
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
670-825 |
3.76e-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: 44.12 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 670 ERARTEAAELRQALAASEARVAELSSTVDAAREELERMRgasvpadehehalSALRDHVTRLQAQLADLARRHEKTSAEV 749
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------------RELESRVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907077947 750 FQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQ 825
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
642-851 |
5.07e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 642 AEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHEHAL 721
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 722 SALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKA 801
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907077947 802 KEKDKKITDLSKEVFTLKEALKVQQSTPASSKEE------------EALRGQVTALQQQIQE 851
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEealeelpeppdlEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
688-855 |
5.25e-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: 43.90 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 688 ARVAELSSTVDAAREELERMRgasVPADEHEHALSALRDHVTRLQAQLADLAR----RHEKTSAEVFQVQREALFMKSER 763
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVE---ENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 764 HAAEAQLATAEQQLRGLRTEAERARQaqsRAQEALDKAKEKDKKITDLSKEvftlkEALKVQQSTPASSKEEEALRGQVT 843
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEK---RLEEIEQLLEELNKKIKDLGEE-----EQLRVKEKIGELEAEIASLERSIA 311
|
170
....*....|..
gi 1907077947 844 ALQQQIQEEARE 855
Cdd:TIGR02169 312 EKERELEDAEER 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1-69 |
7.59e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.06 E-value: 7.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 1 MNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALM-LACEGGSPETVEVLLQGGAQLSI 69
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
2-79 |
8.71e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 42.70 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 2 NPRDRSGATPLIiaAQMCHT---DLCRLLLQQGAATNDQDLQGRTALMLACEGGS--PETVEVLLQGGAQLSITDALGQD 76
Cdd:PHA03095 77 NAPERCGFTPLH--LYLYNAttlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMT 154
|
...
gi 1907077947 77 ATH 79
Cdd:PHA03095 155 PLA 157
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
652-783 |
8.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 652 SRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEhehalsalrdhvTRL 731
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR------------ALL 751
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907077947 732 QAQLADLARRhektsaEVFQVQREALfmKSERHAAEAQLATAEQQLRGLRTE 783
Cdd:COG4913 752 EERFAAALGD------AVERELRENL--EERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-338 |
1.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 148 DAYEEIVRLRQERGRLLQKIRGLEQHKE--RRRKEPLEAEASSVHSLERQ------VQELQQMLAEKQEEKESLGR---E 216
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDAssdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 217 VESLQSRLSLLENERENTSYDVATLQDEEGEMpdfpgadalmpKNQSPSAEEIVASLQEQVAQLTRQNQ----ELLEKVQ 292
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRL-----------EKELEQAEEELDELQDRLEAAEDLARlelrALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907077947 293 ILEEFEKDEAQMAEESQAEVvplvlyESLRAELEQLRRQYTEAMHS 338
Cdd:COG4913 756 AAALGDAVERELRENLEERI------DALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-867 |
1.01e-03 |
|
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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 188 SVHSLERQVQELQQMLAEKQEEKE----SLGREVESLQSRLSLLENERENTSYDVATLQDE----EGEMPDFPGADALMp 259
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRElelaLLVLRLEELREELEELQEELKEAEEELEELTAElqelEEKLEELRLEVSEL- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 260 KNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILE-EFEKDEAQMAEESQAEVVPLVLYESLRAELEQLRRQYT--EAM 336
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEslEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 337 HSQQQQQEGEPPRAQEGEETAYQEIKDKGITIQNgpSVPDLNGT-TYAETKANgmELQAGGSKGVWNTEAGVSEAAPIEP 415
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLEL--QIASLNNEiERLEARLE--RLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 416 EAAGSEATGKDRLAAKEMDTSATMAEAL-NVKALGDNAESEPVAAEDTGGKENPGMKADEVDVLAQAGLTGTVIRNMeai 494
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALeELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL--- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 495 gvrdtgiqatgleAKAVKTTGVQATVAEVIgvKVTGVQTTAIEAIGVKDTTQVATGAQADCWQATEADCTGAQDTAMept 574
Cdd:TIGR02168 513 -------------KNQSGLSGILGVLSELI--SVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVT--- 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 575 gaqatvtetteaetsgtedPCAAILHPGAAAAALQAELETRIRGLEEALRRREREAAAELEAARGRF-----AEAEEAAR 649
Cdd:TIGR02168 575 -------------------FLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvVDDLDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 650 GRSRELEAlRELLATAT---------ATGERARTEA---------AELRQALAASEARVAELSSTVDAAREELERMRGAS 711
Cdd:TIGR02168 636 ELAKKLRP-GYRIVTLDgdlvrpggvITGGSAKTNSsilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 712 VPADEHEHALSALrdhVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLrgLRTEAERArQAQ 791
Cdd:TIGR02168 715 EQLRKELEELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL--AEAEAEIE-ELE 788
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907077947 792 SRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQSTPASSKEE-EALRGQVTALQQQIqEEAREHGAVVALYRTHL 867
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiAATERRLEDLEEQI-EELSEDIESLAAEIEEL 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
646-806 |
1.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 646 EAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELS---------STVDAAREELERMRGASVPADE 716
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 717 HEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERH-AAEAQLATAEQQLRGLRTEAERARQAQSRAQ 795
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|.
gi 1907077947 796 EALDKAKEKDK 806
Cdd:COG4717 234 NELEAAALEER 244
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
40-71 |
1.18e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 1.18e-03
10 20 30
....*....|....*....|....*....|...
gi 1907077947 40 QGRTALMLAC-EGGSPETVEVLLQGGAQLSITD 71
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
645-802 |
1.25e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 645 EEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELErmrGASVPADEHEHALSAL 724
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE---KLKREINELKRELDRL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 725 RDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAE-------AQLATAEQQLRGLRTEAERARQAQSRAQEA 797
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
....*
gi 1907077947 798 LDKAK 802
Cdd:TIGR02169 492 LAEAE 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-336 |
1.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 147 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRkepLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 226
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELEYLRAALR---LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 227 LENERENTSYD-VATLQDEegempdfpgadalmpknqspsaeeiVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMA 305
Cdd:COG4913 328 LEAQIRGNGGDrLEQLERE-------------------------IERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190
....*....|....*....|....*....|.
gi 1907077947 306 EESQAEVVPLVlyESLRAELEQLRRQYTEAM 336
Cdd:COG4913 383 AALRAEAAALL--EALEEELEALEEALAEAE 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-297 |
1.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 147 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKE----PLEAEassVHSLERQ----------VQELQQMLAEKQEEKES 212
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvaSAERE---IAELEAElerldassddLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 213 LGREVESLQSRLSLLENERENTSYDVATLQDEEGEMPD------FPGADALMPK-NQSPSAEEIVASLQEQVAQLTRQNQ 285
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelRALLEERFAAaLGDAVERELRENLEERIDALRARLN 783
|
170
....*....|...
gi 1907077947 286 ELLEK-VQILEEF 297
Cdd:COG4913 784 RAEEElERAMRAF 796
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
640-804 |
1.46e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 640 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpadeheh 719
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 720 alsalrDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALD 799
Cdd:COG1579 89 ------KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*
gi 1907077947 800 KAKEK 804
Cdd:COG1579 163 AEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
147-300 |
1.49e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 147 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEASSVHsLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 226
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 227 LENERENTSYDVATLQDEEGEMPDFPGADALMPK-------------------NQSPSAEEIVA----SLQEQVAQLTRQ 283
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqrveeeiralepvnMLAIQEYEEVLkrldELKEKRAKLEEE 1001
|
170
....*....|....*..
gi 1907077947 284 NQELLEKVQILEEFEKD 300
Cdd:TIGR02169 1002 RKAILERIEEYEKKKRE 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
631-757 |
1.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 631 AAELEAARGRFAEAEEAARGRS-RELEALRELLATATATGERARTEAAELRQALA-------ASEARVAELSSTVDAARE 702
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLE 394
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907077947 703 ELERMRGA-SVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVqREAL 757
Cdd:COG4913 395 ALEEELEAlEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDAL 449
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
715-851 |
1.72e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 715 DEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTE----------- 783
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeie 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 784 --AERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQStpASSKEEEALRGQVTALQQQIQE 851
Cdd:COG1579 100 slKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA--ELDEELAELEAELEELEAEREE 167
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-335 |
1.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 146 DRDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEA---------SSVHSLERQVQELQQMLAEKQEEKESLGRE 216
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleeheerrEELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 217 VESLQSRLSLLENERENT---------SYDVATLQDEEGEMPDFPGADALMPKNQSPSA-EEIVASLQEQVAQLTRQNQE 286
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddaDAEAVEARREELEDRDEELRDRLEECRVAAQAhNEEAESLREDADDLEERAEE 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907077947 287 LLEKVQILEEFEKDEAQMAEESQAEVvplvlyESLRAELEQLRRQYTEA 335
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEI------EELEEEIEELRERFGDA 403
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
658-826 |
2.08e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 658 LRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELErmrgasvpadehehALSALRDhvtRLQAQLAD 737
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS--------------AAEAERS---RLQALLAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 738 LARRheKTSAEvfqvQREALfMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDK----KITDLSK 813
Cdd:PRK09039 107 LAGA--GAAAE----GRAGE-LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDResqaKIADLGR 179
|
170
....*....|....*
gi 1907077947 814 EvftLKEAL--KVQQ 826
Cdd:PRK09039 180 R---LNVALaqRVQE 191
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
8-38 |
2.15e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|..
gi 1907077947 8 GATPLIIAAQMC-HTDLCRLLLQQGAATNDQD 38
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
646-878 |
2.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 646 EAARGRSRELEALRELLATAtatgERARTEAAELRQALAASEA-----RVAELSSTVDAAREELERMRGASVPADEHEHA 720
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKA----EEDKKKADELKKAAAAKKKadeakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 721 LSALRDHVTRLQAQLADLARR--HEKTSAEVFQVQREALFMKSE--RHAAEAQLATAEQQLRGLRTEAERARQAQ-SRAQ 795
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKADEAKKAEEAKKADEAKKAEeAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 796 EALDKAKEKdKKITDLSK--EVFTLKEALKVQQSTPASSKEEEALRGQVTALQQqiqEEAREHGAVVALYRTHLLYAIQG 873
Cdd:PTZ00121 1537 DEAKKAEEK-KKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEA 1612
|
....*
gi 1907077947 874 QMDED 878
Cdd:PTZ00121 1613 KKAEE 1617
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
615-801 |
2.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 615 RIRgleealrrREREAAAELEAARGRFAEAEEAARGRSRELEALREL----LATATATGERARTEAAelRQALAASEARV 690
Cdd:COG4913 618 ELA--------ELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeIDVASAEREIAELEAE--LERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 691 AELSSTVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALfmkSERHAAEAQL 770
Cdd:COG4913 688 AALEEQLEELEAELEELEEE---LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---EERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|.
gi 1907077947 771 ATAEQQLRGLRTEAERARQAQSRAQEALDKA 801
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
2-77 |
2.79e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 40.71 E-value: 2.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907077947 2 NPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDA 77
Cdd:COG0666 213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
147-233 |
2.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 147 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 226
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
....*..
gi 1907077947 227 LENEREN 233
Cdd:COG4717 232 LENELEA 238
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
183-331 |
3.14e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.32 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 183 EAEASSVHSLERQVQELQQMLAEKQEEKESLG----REVESLQSRLSLLENERENTSydvATLQDEE--------GEMPD 250
Cdd:pfam15397 77 EKEESKLNKLEQQLEQLNAKIQKTQEELNFLStykdKEYPVKAVQIANLVRQLQQLK---DSQQDELdeleemrrMVLES 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 251 FpgADALMPKNQ---SPSAEEIVASLQEQVAQLTRQNQELLEKvqiLEEFEKDEAQMAEESQAevvplvlyesLRAELEQ 327
Cdd:pfam15397 154 L--SRKIQKKKEkilSSLAEKTLSPYQESLLQKTRDNQVMLKE---IEQFREFIDELEEEIPK----------LKAEVQQ 218
|
....
gi 1907077947 328 LRRQ 331
Cdd:pfam15397 219 LQAQ 222
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
41-69 |
3.40e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.70 E-value: 3.40e-03
10 20
....*....|....*....|....*....
gi 1907077947 41 GRTALMLACEGGSPETVEVLLQGGAQLSI 69
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-93 |
4.30e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.42 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 1 MNPRDRSGATPLIIAAQMCHTDL--CRLLLQQGA----------------ATNDQDLQGRTALMLACEGGSPETVEVLLQ 62
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213
|
90 100 110
....*....|....*....|....*....|.
gi 1907077947 63 GGAQLSITDALGQDATHYGALTGDKLILQLL 93
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
709-863 |
4.57e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 709 GASVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERAR 788
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 789 QAQSRAQEALDKAKEKDKKITDLSKEVF---------TLKEALKVQQSTPASSKEEEALRGQVTALQQQIQEEAREHGAV 859
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
....
gi 1907077947 860 VALY 863
Cdd:COG4942 177 EALL 180
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
646-797 |
4.88e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 646 EAARGRSRELEALRELLATATATGERARTEA------AELRQALAASEARVAELSST-------VDAAREELERMRGASv 712
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQL- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 713 pADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVfqvqrealfmkserhaaeAQLATAEQQLRGLRTEAERAR---- 788
Cdd:COG3206 308 -QQEAQRILASLEAELEALQAREASLQAQLAQLEARL------------------AELPELEAELRRLEREVEVARelye 368
|
....*....
gi 1907077947 789 QAQSRAQEA 797
Cdd:COG3206 369 SLLQRLEEA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
642-804 |
5.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 642 AEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRgASVPADEHEHAL 721
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-EALDEEELEEEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 722 SALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKserhaAEAQLATAEQQLRglrtEAERARQAQSRAQEALDKA 801
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAE-----LLQELEELKAELR----ELAEEWAALKLALELLEEA 505
|
...
gi 1907077947 802 KEK 804
Cdd:COG4717 506 REE 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-232 |
6.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 145 DDRDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLE-AEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSR 223
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
....*....
gi 1907077947 224 LSLLENERE 232
Cdd:COG4717 462 LEQLEEDGE 470
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
40-65 |
6.31e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 34.87 E-value: 6.31e-03
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
157-385 |
6.33e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 157 RQERGRLLQKIRGLEQHKER-----RRKEPLEAEASSVHSLERQVQELQQMLAE-KQEEKESLGREVESLQSRLSLLEN- 229
Cdd:COG5022 857 AKKRFSLLKKETIYLQSAQRvelaeRQLQELKIDVKSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKKl 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 230 ----------ERENTSYD-VATLQDEEGEMpdfpgadalmpKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFE 298
Cdd:COG5022 937 lnnidleegpSIEYVKLPeLNKLHEVESKL-----------KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 299 KD-EAQMAEESQAEVVPLVLyeslrAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKDKGITIQNGPSVPDL 377
Cdd:COG5022 1006 KQyGALQESTKQLKELPVEV-----AELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDD 1080
|
....*...
gi 1907077947 378 NGTTYAET 385
Cdd:COG5022 1081 KQLYQLES 1088
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
6-96 |
8.10e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 39.59 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077947 6 RSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTG 85
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
90
....*....|.
gi 1907077947 86 DKLILQLLHES 96
Cdd:PHA02875 180 DIAICKMLLDS 190
|
|
| |
