|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-167 |
1.29e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 110.81 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALML 96
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968514 97 ACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLHESARRSSPPSASLEEDSGEASSQN 167
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-142 |
1.23e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.34 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALML 96
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568968514 97 ACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLL 142
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-148 |
6.25e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 100.03 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALML 96
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568968514 97 ACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLHESARR 148
Cdd:COG0666 226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
28-120 |
5.96e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 28 LHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAtnDQDLQGRTALMLACEGGSPETVE 107
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 568968514 108 VLLQGGAQLSITD 120
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-142 |
7.08e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 85.39 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALML 96
Cdd:COG0666 47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568968514 97 ACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLL 142
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
12-87 |
1.05e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 1.05e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968514 12 EASCVVDIEDSSGWTALHHAAAGGCLSCSKLLCSfkaHMNPRDR-SGATPLIIAAQMCHTDLCRLLLQQGAATNDQD 87
Cdd:pfam12796 18 ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKdNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
61-142 |
1.69e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 61 LIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDalGQDATHYGALTGDKLILQ 140
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
..
gi 568968514 141 LL 142
Cdd:pfam12796 79 LL 80
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-126 |
1.40e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.52 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALML 96
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
|
90 100 110
....*....|....*....|....*....|
gi 568968514 97 ACEGGSPETVEVLLQGGAQLSITDALGQDA 126
Cdd:COG0666 259 AAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-900 |
1.18e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 200 EEIVRLRQERGRLLQKIRGLEQHKE--RRRKEPLEAEASSVHS----LERQVQELQQMLAEKQEEKESLGREVESLQSRL 273
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQilRERLANLERQLEELEAqleeLESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 274 SLLENERENTSydvATLQDEEGEMPDFPGADALMPK------NQSPSAEEIVASLQEQVAQLTRQNQELLEKVQiLEEFE 347
Cdd:TIGR02168 361 EELEAELEELE---SRLEELEEQLETLRSKVAQLELqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLE-EAELK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 348 KDEAQMAEESQAEVVPLVLYESLRAELEQLRRQYTEAMhsqqqqqegEPPRAQEGEETAYQEIKDKGITIQNgpsvpdlN 427
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAE---------QALDAAERELAQLQARLDSLERLQE-------N 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 428 GTTYAETKANGME--LQAGGSKGVwnteagVSEAAPIEPE-AAGSEATGKDRLAAKEMDTSATMAEALN----------- 493
Cdd:TIGR02168 501 LEGFSEGVKALLKnqSGLSGILGV------LSELISVDEGyEAAIEAALGGRLQAVVVENLNAAKKAIAflkqnelgrvt 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 494 VKALGDNAESEPVAAEDTGGKENPGMK---------ADEVDVLAQAGLTGTVIRNMEAIGVRDtgIQATGLEAKAVKTTG 564
Cdd:TIGR02168 575 FLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfDPKLRKALSYLLGGVLVVDDLDNALEL--AKKLRPGYRIVTLDG 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 565 VQATVAEVIGVKVTGVQTTAIE-AIGVKDTTQVATGAQADCWQAT-EADCTGAQDTAMEPTGAQATVTETTEAETSGTED 642
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILErRREIEELEEKIEELEEKIAELEkALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 643 PCAAILhpgAAAAALQAELETRIRGLEEALRRREREAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERAR 722
Cdd:TIGR02168 733 KDLARL---EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 723 TEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQ 802
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 803 REALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEK-DKKITDLSKEVFTLKEAlkVQQSTPASS 881
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEE--AEALENKIE 964
|
730
....*....|....*....
gi 568968514 882 KEEEALRGQVTALQQQIQE 900
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
689-923 |
1.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEH 768
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE---LAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALD 848
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968514 849 KAKEKDKKITDLSKEvftlkEALKVQQSTPASSKEEEALRGQVTALQQQIQEEAREHGAVVALYRTHLLYAIQGQ 923
Cdd:COG1196 411 ALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
689-946 |
4.78e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEH 768
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE---LEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALD 848
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 849 KAKEKDKKITDLSKEVFTLKEALKvqqstpasSKEEEALRGQVTALQQQIQEEAREHGAVVALYRTHLLYAIQGQMDEDV 928
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250
....*....|....*...
gi 568968514 929 QCILSQILQMQRLQAQGR 946
Cdd:COG1196 504 EGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
664-928 |
1.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 664 RIRGLEEALRRREREAAAeleaargRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELS 743
Cdd:COG1196 299 RLEQDIARLEERRRELEE-------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 744 STVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAE 823
Cdd:COG1196 372 AELAEAEEELEELAEE---LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 824 QQLRGLRTEAERARQAQSRAQEALDKAKEKDKKItDLSKEVFTLKEALKVQQSTPASSKEEEALRGQVTALQQQIQEEAR 903
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
250 260
....*....|....*....|....*
gi 568968514 904 EHGAVVALYRTHLLYAIQGQMDEDV 928
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIV 552
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1-118 |
4.44e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.62 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 1 MKTLRARFKKTeascvvDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQG 80
Cdd:PHA02875 118 MKLLIARGADP------DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
90 100 110
....*....|....*....|....*....|....*....
gi 568968514 81 AATNDQDLQGRTALM-LACEGGSPETVEVLLQGGAQLSI 118
Cdd:PHA02875 192 ANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
59-110 |
9.47e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 9.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568968514 59 TPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLL 110
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-144 |
1.32e-08 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 57.27 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 16 VVDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALM 95
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568968514 96 LACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLHE 144
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE 141
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-910 |
1.80e-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: 58.53 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 201 EIVRLRQERGRLLQKIRGLeQHKERRRKEPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENER 280
Cdd:TIGR02168 233 RLEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 281 EN--TSYDVATLQDEEGE-MPDFPGADALMPKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEE-FEKDEAQMAEE 356
Cdd:TIGR02168 312 ANleRQLEELEAQLEELEsKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 357 SQAEvvplvlyESLRAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKdkgitiqngpsvpdlngTTYAETKA 436
Cdd:TIGR02168 392 ELQI-------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-----------------AELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 437 NGMELQAGGSKGVWNTE---AGVSEAAPIEPEAAGSEATGKDRLAAKEMDTSATMAEALNVKALGDNAE----SEPVAAE 509
Cdd:TIGR02168 448 ELEELQEELERLEEALEelrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 510 dtggkenpGMKADE-----VDVLAQAGLTGTVIRNMEAIGV------RDTGIQATGLEAKAVKTTGVQATVAEVIgVKVT 578
Cdd:TIGR02168 528 --------LISVDEgyeaaIEAALGGRLQAVVVENLNAAKKaiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL-KNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 579 GVQTTAIEAIGVKDTTQVATGAqadcWQATeadctgaqdTAMEPTGAQATVTETTEAETSGTEDPCAAILHPGAaaaalq 658
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSY----LLGG---------VLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG------ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 659 aeletRIRGLEEALRRREREAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEAR 738
Cdd:TIGR02168 660 -----VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 739 VAELSSTVDAAREELERMRGASVPAD-----------EHEHALSALRDHVTRLQAQLADLARRHEK-------------- 793
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEaeieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdelraeltl 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 794 TSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKV 873
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
730 740 750
....*....|....*....|....*....|....*..
gi 568968514 874 QQSTpaSSKEEEALRGQVTALQQQIQEEAREHGAVVA 910
Cdd:TIGR02168 895 ELEE--LSEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
24-77 |
2.52e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 2.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568968514 24 GWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLL 77
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
663-919 |
3.42e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 663 TRIRGLEEALRRRE----------REAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQAL 732
Cdd:COG1196 253 AELEELEAELAELEaeleelrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 733 AASEARVAELSSTVDAAREELErmrgasvpadEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSER 812
Cdd:COG1196 333 EELEEELEELEEELEEAEEELE----------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 813 HAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQStpASSKEEEALRGQVT 892
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--ELLEEAALLEAALA 480
|
250 260
....*....|....*....|....*..
gi 568968514 893 ALQQQIQEEAREHGAVVALYRTHLLYA 919
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
688-916 |
5.51e-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: 56.99 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 688 GRFAEAEEAARGRSRELEalrellatatatgerarteaaELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHE 767
Cdd:TIGR02168 663 GGSAKTNSSILERRREIE---------------------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 768 HALSALrdhVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLrgLRTEAERArQAQSRAQEAL 847
Cdd:TIGR02168 722 EELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL--AEAEAEIE-ELEAQIEQLK 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 848 DKAKEKDKKITDLSKEVFTLKEALKVQQSTPASSKEE-EALRGQVTALQQQIqEEAREHGAVVALYRTHL 916
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRiAATERRLEDLEEQI-EELSEDIESLAAEIEEL 864
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
691-852 |
9.18e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 691 AEAEEAARGRSRELEALRELLA--TATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGA--SVPADEH 766
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 767 EH----------ALSALRDHVTRLQAQLADLARRHEkTSAEVFQVQREalfmkserhAAEAQLATAEQQLRGLRTEAERA 836
Cdd:COG4913 341 EQlereierlerELEERERRRARLEALLAALGLPLP-ASAEEFAALRA---------EAAALLEALEEELEALEEALAEA 410
|
170
....*....|....*.
gi 568968514 837 RQAQSRAQEALDKAKE 852
Cdd:COG4913 411 EAALRDLRRELRELEA 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-829 |
9.49e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 201 EIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENER 280
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 281 ENTSYDVATLQDEEgempdfpgadalmpknqspsaEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQAE 360
Cdd:COG1196 312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 361 VvplvlyESLRAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKDkgitiqngpsvpdlngttyAETKANGME 440
Cdd:COG1196 371 E------AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL-------------------ERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 441 LQAggskgvwnTEAGVSEAAPIEPEAAGSEATGKDRLAAKEMDTSATMAEALNVKALGDNAESEPVAAEDTggkenpgmK 520
Cdd:COG1196 426 LEE--------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--------A 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 521 ADEVDVLAqagltgtvirnmEAIGVRDTGIQATGLEAKAVKTTGVQATVAEVIGVK-----VTGVQTTAIEAIGVKDTTQ 595
Cdd:COG1196 490 AARLLLLL------------EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEaayeaALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 596 VATGAQADCWQATEADCTGAQDTAMEPTGAQATVTETTEAETSGTEDPCAAIlhpgaaaaaLQAELETRIRGLEEALRRR 675
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR---------EADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 676 EREAAAELEAARGRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELER 755
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968514 756 MRGASVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFmksERHAAEAQLATAEQQLRGL 829
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP---DLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
674-904 |
1.29e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 674 RREREAAAEleaargRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREEL 753
Cdd:COG1196 224 ELEAELLLL------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 754 ERMRGASVPADEHEHALSALRDhvtRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQlrgLRTEA 833
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAE 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968514 834 ERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQstpassKEEEALRGQVTALQQQIQEEARE 904
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL------ERLERLEEELEELEEALAELEEE 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
689-907 |
2.38e-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: 54.00 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHEH 768
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 ALSALRdhvtrlQAQLADLARRHEKTSAEVFQVQREALFMKSERhaaeAQLATAEQQLRGLRTEAERARQAQSRAQEALD 848
Cdd:COG4942 122 LALLLS------PEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 849 KAK-EKDKKITDLSKEVFTLKEALKVQQstpassKEEEALRGQVTALQQQIQEEAREHGA 907
Cdd:COG4942 192 ALKaERQKLLARLEKELAELAAELAELQ------QEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-910 |
4.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 702 RELEALRELLATATATGERARTEAAELRQALAA---------SEARVAELSSTVDAAREELERMRGASvpadehehalsa 772
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASS------------ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 773 lrDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGL--RTEAERARQAQSRAQEALDKA 850
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 851 KEKDKKiTDLSKEVFTLKEALkvqqstpasSKEEEALRGQVTALQQQIQEEAREHGAVVA 910
Cdd:COG4913 763 VERELR-ENLEERIDALRARL---------NRAEEELERAMRAFNREWPAETADLDADLE 812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
741-904 |
5.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 741 ELSSTVDAARE---ELERMRGASVPADEHEHALSALRDHVTRLQAQLADLAR-RHEKTSAEVFQVQREALFMKSERHAAE 816
Cdd:COG4913 222 DTFEAADALVEhfdDLERAHEALEDAREQIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 817 AQLATAEQQLRGLRTEAERARQAQSRAQEALDKA------------KEKDKKITDLSKEVFTLKEALK-VQQSTPASSKE 883
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlereiERLERELEERERRRARLEALLAaLGLPLPASAEE 381
|
170 180
....*....|....*....|.
gi 568968514 884 EEALRGQVTALQQQIQEEARE 904
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA 402
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
17-118 |
5.34e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.04 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALML 96
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
90 100
....*....|....*....|..
gi 568968514 97 ACEGGSPETVEVLLQGGAQLSI 118
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMN 218
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
65-186 |
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 568968514 65 AQMCHTDLC-----------RLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALT 133
Cdd:PTZ00322 79 AHMLTVELCqlaasgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 134 GDKLILQLL-------HESARRSSPPSASLEEDSGEASsqnSVSSHekqgAPKKRKAPQP 186
Cdd:PTZ00322 159 GFREVVQLLsrhsqchFELGANAKPDSFTGKPPSLEDS---PISSH----HPDFSAVPQP 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
689-899 |
2.38e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSR---ELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADE 765
Cdd:PRK02224 500 RAEDLVEAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 766 HEHALSALRDHVTRLQAQLADLA-------RRHEKTS--AEVFQVQREALFMKSERHaaeAQLATA--EQQLRGLRTEAE 834
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIAdaedeieRLREKREalAELNDERRERLAEKRERK---RELEAEfdEARIEEAREDKE 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968514 835 RARQAQSRAQEALDkakEKDKKITDLSKEVFTLKEALkvqqstpassKEEEALRGQVTALQQQIQ 899
Cdd:PRK02224 657 RAEEYLEQVEEKLD---ELREERDDLQAEIGAVENEL----------EELEELRERREALENRVE 708
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
719-940 |
6.16e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 719 ERART--EAAELrqALAASEARVAELSSTVDAAREEL----ERMRGASVPADEHEHALSALR---DHVTRLQAQladlar 789
Cdd:PRK04863 424 ERAKQlcGLPDL--TADNAEDWLEEFQAKEQEATEELlsleQKLSVAQAAHSQFEQAYQLVRkiaGEVSRSEAW------ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 790 rhektsaevfQVQREALfmksERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKE 869
Cdd:PRK04863 496 ----------DVARELL----RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 870 ALKVQQSTPASSKEE-----EALRGQVTALQQQIQE-EARE---HGAVVALYRthlLYAIQGQMDEDVQCILSQILQMQR 940
Cdd:PRK04863 562 ELEARLESLSESVSEarerrMALRQQLEQLQARIQRlAARApawLAAQDALAR---LREQSGEEFEDSQDVTEYMQQLLE 638
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
727-904 |
6.54e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 727 ELRQALAASEARVAELSstVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREAL 806
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEE---LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 807 FMKSERHAAEAQLATAEQQLRGLRTEAERA----RQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKvqqstpASSK 882
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELeaqlEELESKLDELAEELAELEEKLEELKEELESLEAELE------ELEA 365
|
170 180
....*....|....*....|..
gi 568968514 883 EEEALRGQVTALQQQIQEEARE 904
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSK 387
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-384 |
9.58e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 196 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 275
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 276 LENERENTSYDVATLQDEEGEmpdfpgadalmpknqspSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAE 355
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEA-----------------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180
....*....|....*....|....*....
gi 568968514 356 ESQAEVVPLVLYESLRAELEQLRRQYTEA 384
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-900 |
1.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 692 EAEEAARGR-SRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAR--EELERMRGASVPADEHEH 768
Cdd:PTZ00121 1165 KAEEARKAEdAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKK 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 ALSALRDHVTRL--QAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQA---QSRA 843
Cdd:PTZ00121 1245 AEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKA 1324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968514 844 QEALDKAKEKDKKITDLSK--------EVFTLKEALKVQQSTPASSKEEEALRGQVTALQQQIQE 900
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKaaeaakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
28-110 |
1.16e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 28 LHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVE 107
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 568968514 108 VLL 110
Cdd:PTZ00322 166 LLS 168
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
132-413 |
1.27e-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: 48.97 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 132 LTGDKLILQLLHESARRSSPpSASLEEDSGEASSQNSVSSHEKQGA---PKKRKAPQPPASTPVPDDRDA--YEEIVRLR 206
Cdd:pfam17380 265 MTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKArevERRRKLEEAEKARQAEMDRQAaiYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 207 QERGRLLQKIRGLEQHKE--RRRKEPLEAEASSVHSLERqvqelqqMLAEKQEEKESLGREVESLQsRLSLLENERENTs 284
Cdd:pfam17380 344 MERERELERIRQEERKREleRIRQEEIAMEISRMRELER-------LQMERQQKNERVRQELEAAR-KVKILEEERQRK- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 285 ydvatLQDEEGEMPDfpgadalMPKNQSPSAEEIVASLQEQVA-QLTRQNQELLEKVQILE----------------EFE 347
Cdd:pfam17380 415 -----IQQQKVEMEQ-------IRAEQEEARQREVRRLEEERArEMERVRLEEQERQQQVErlrqqeeerkrkklelEKE 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568968514 348 KDEAQMAEESQAEVVPLVLYESLRAELEQLRRQY---TEAMHSQQQQQEGEPPRAQEGEETAYQEIKDK 413
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlleKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
688-908 |
1.97e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 688 GRFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEAR-------------------VAELSSTVDA 748
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelskleeeVSRIEARLRE 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 749 AREELER-----------MRGASVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEA 817
Cdd:TIGR02169 817 IEQKLNRltlekeylekeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 818 QLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEvftlkealkvqqstPASSKEEEALRGQVTALQQQ 897
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--------------DEEIPEEELSLEDVQAELQR 962
|
250
....*....|.
gi 568968514 898 IQEEAREHGAV 908
Cdd:TIGR02169 963 VEEEIRALEPV 973
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
691-877 |
2.65e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 691 AEAEEAargrsreLEALRE--LLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHEh 768
Cdd:COG3206 192 EEAEAA-------LEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQRealfmksERHAAEAQLATAEQQ-LRGLRTEAERARQAQSRAQEAL 847
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQL 336
|
170 180 190
....*....|....*....|....*....|
gi 568968514 848 DKAKEKDKKITDLSKEVFTLKEALKVQQST 877
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-886 |
3.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 692 EAEEAARGRSRELEALRELLATATATGERARTEAAELRQA---------LAASEARVAELSSTVDAAREELERMRgasvP 762
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkkaeekKKADEAKKAEEKKKADEAKKKAEEAK----K 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 763 ADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARqaqsR 842
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK----K 1392
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568968514 843 AQEALDKAKEKDKKITDLSKEVFTLKEALKVQQSTPASSKEEEA 886
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
11-97 |
3.17e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 47.71 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 11 TEASCVVDIEDSSGWTALHHAAAGGclSCSKLLCSF----KAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQ 86
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
|
90
....*....|.
gi 568968514 87 DLQGRTALMLA 97
Cdd:PHA03095 287 SSDGNTPLSLM 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
142-904 |
3.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 142 LHESARRSSPPSASLEEDSGEA--SSQNSVSSHEKQGAPKKRKAPQP---PASTPVPDDRDAYE----EIVRLRQERGRL 212
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAkkKAEDARKAEEARKAEDARKAEEArkaEDAKRVEIARKAEDarkaEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 213 LQKIRGLEQHKE---RRRKEPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENERENTSydvaT 289
Cdd:PTZ00121 1179 EAARKAEEVRKAeelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE----I 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 290 LQDEEGEMPDFPGADALMPKNQSPSAEEIVASLQEQVAQLTRQNQEllekVQILEEFEK--DEAQMAEESQAEVvplvly 367
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE----KKKADEAKKkaEEAKKADEAKKKA------ 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 368 ESLRAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKDKgitiqngpsvpdlNGTTYAETKANGMELQAGGSK 447
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE-------------KKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 448 GVWNTEAGVSEAAPIEPEAAGSEATGKDRLAAKEMDTSATMAEALNVKA-LGDNAESEPVAAEDTGGKENPGMKADEVDv 526
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKAEEAKKKAEEAK- 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 527 laqagltgtvirnmeaigvrdtgiqatglEAKAVKTTGVQATVAEVIGVKVTGVQTTAIEAIGVKDTTQVATGAQadcwQ 606
Cdd:PTZ00121 1471 -----------------------------KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK----K 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 607 ATEADCTGAQDTAMEPTGAQATVTETteaetsgtedpcaailhpgAAAAALQAELETRIRGLEEALRRREREAAAELEAA 686
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAE-------------------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 687 RGRFAE-AEEAARGRSRELEALREllatatatgERARTEAAELRQalaASEARVAelSSTVDAAREELERMRGASVPADE 765
Cdd:PTZ00121 1579 ALRKAEeAKKAEEARIEEVMKLYE---------EEKKMKAEEAKK---AEEAKIK--AEELKKAEEEKKKVEQLKKKEAE 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 766 HEHALSALRDHVTRLQAQLADLARRHE--KTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTE----AERARQA 839
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKA 1724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568968514 840 QS----RAQEALDKAKEKDKKITDLSKEVftlKEALKVQQSTPASSKEEEALRGQVTALqqqIQEEARE 904
Cdd:PTZ00121 1725 EEenkiKAEEAKKEAEEDKKKAEEAKKDE---EEKKKIAHLKKEEEKKAEEIRKEKEAV---IEEELDE 1787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
689-872 |
3.63e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpADEHEH 768
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE---LRELES 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 ALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQrEALfmkSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQ---- 844
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ-ERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikel 984
|
170 180 190
....*....|....*....|....*....|...
gi 568968514 845 -----EALDKAKEKDKKITDLSKEVFTLKEALK 872
Cdd:TIGR02168 985 gpvnlAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
12-125 |
4.31e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 46.88 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 12 EASCVVDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAaqMCHTDLCRLLLQQGAATNDQDLQGR 91
Cdd:PHA02874 178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGS 255
|
90 100 110
....*....|....*....|....*....|....*
gi 568968514 92 TALMLACE-GGSPETVEVLLQGGAQLSITDALGQD 125
Cdd:PHA02874 256 TPLHHAINpPCDIDIIDILLYHKADISIKDNKGEN 290
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-380 |
5.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 190 TPVPDDRDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEP-LEAEASSVHSLERQVQELQQMLAEKQEEKESL------ 262
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELeaqirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 263 --GREVESLQSRLSLLENERENTSYDVATLQDeegempdfpGADALmpKNQSPSAEEIVASLQEQVAQLTRQNQELLEKV 340
Cdd:COG4913 335 ngGDRLEQLEREIERLERELEERERRRARLEA---------LLAAL--GLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568968514 341 QiLEEFEKDEAQMAEESQaevvplvlYESLRAELEQLRRQ 380
Cdd:COG4913 404 E-EALAEAEAALRDLRRE--------LRELEAEIASLERR 434
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
90-143 |
5.63e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 5.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568968514 90 GRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLH 143
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
14-114 |
5.90e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.17 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 14 SCVVDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPrdRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTA 93
Cdd:PLN03192 581 ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
90 100
....*....|....*....|.
gi 568968514 94 LMLACEGGSPETVEVLLQGGA 114
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGA 679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-380 |
6.31e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 200 EEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEASSVHSLERQvQELQQMLAEKQEEKESLGREVESLQSRLSLLENE 279
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 280 RENTSYDVATLQDEEgempdfpgadalmpKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQA 359
Cdd:COG1196 346 LEEAEEELEEAEAEL--------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180
....*....|....*....|.
gi 568968514 360 EvvpLVLYESLRAELEQLRRQ 380
Cdd:COG1196 412 L---LERLERLEEELEELEEA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-383 |
7.25e-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: 46.98 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 196 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAE-----------------ASSVHSLERQVQELQQMLAEKQEE 258
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkekreyegyelLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 259 KESLGREVESLQSRLSLLENERENTSYDVATLQDEEgempdfpgadALMPKNQSPSAEEIVASLQEQVAQLTRQNQELLE 338
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE----------QLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568968514 339 KVQILE-EFEKDEAQMA------EESQAEVVPLV-LYESLRAELEQLRRQYTE 383
Cdd:TIGR02169 323 RLAKLEaEIDKLLAEIEelereiEEERKRRDKLTeEYAELKEELEDLRAELEE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
770-929 |
7.57e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 770 LSALRDHVTRLQAQLADLARRHE--KTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEAL 847
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 848 DKAKEKDKKITDLSKEVFTLKEALKvqqstpASSKEEEALRGQVTALQQQIQEEAREHGAvvALYRTHLLYAIQGQMDED 927
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELE------QAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDAVERELREN 770
|
..
gi 568968514 928 VQ 929
Cdd:COG4913 771 LE 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-409 |
8.50e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 200 EEIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENE 279
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 280 RENTSYDVATLQDEEGEMpdfpgadalmpknqspsAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQA 359
Cdd:COG1196 367 LLEAEAELAEAEEELEEL-----------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568968514 360 EVVPLVLYESLRAELEQLRRQYTEAmhsQQQQQEGEPPRAQEGEETAYQE 409
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAEL---EEEEEALLELLAELLEEAALLE 476
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-129 |
8.89e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.03 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 41 KLLCSFKAHMNPRDR-SGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSIT 119
Cdd:PHA02878 151 KLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230
|
90
....*....|
gi 568968514 120 DALGQDATHY 129
Cdd:PHA02878 231 DKCGNTPLHI 240
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
54-154 |
1.04e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.40 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 54 DRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALT 133
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
|
90 100
....*....|....*....|.
gi 568968514 134 GDKLILQLLHESARRSSPPSA 154
Cdd:PLN03192 602 KHHKIFRILYHFASISDPHAA 622
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
24-128 |
1.19e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 45.79 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 24 GWTALH---HAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIiaAQMCHT---DLCRLLLQQGAATNDQDLQGRTALMLA 97
Cdd:PHA03095 47 GKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLH--LYLYNAttlDVIKLLIKAGADVNAKDKVGRTPLHVY 124
|
90 100 110
....*....|....*....|....*....|...
gi 568968514 98 CEGGS--PETVEVLLQGGAQLSITDALGQDATH 128
Cdd:PHA03095 125 LSGFNinPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
94-147 |
1.62e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.25 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568968514 94 LMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLHESAR 147
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
240-354 |
1.86e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 240 SLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENERENtsydVATLQDE-EGEMPDFPGADALMP------KNQS 312
Cdd:PRK09039 57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSR----LQALLAElAGAGAAAEGRAGELAqeldseKQVS 132
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568968514 313 PSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKD-EAQMA 354
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDREsQAKIA 175
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
758-871 |
1.87e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 758 GASVPADEHEHALSALRDHVTRLQAQLADLARrhektsaEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAErar 837
Cdd:PRK11448 132 GPFVPPEDPENLLHALQQEVLTLKQQLELQAR-------EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE--- 201
|
90 100 110
....*....|....*....|....*....|....
gi 568968514 838 QAQSRAQEALDKAKEKDKKITDLSKEVFTLKEAL 871
Cdd:PRK11448 202 QLQEKAAETSQERKQKRKEITDQAAKRLELSEEE 235
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
719-874 |
1.90e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 719 ERARTEAAELRQALAASEARVAELSSTVDAAREELERMRgasvpadehehalSALRDHVTRLQAQLADLARRHEKTSAEV 798
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------------RELESRVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968514 799 FQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQ 874
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
737-904 |
2.70e-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: 45.06 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 737 ARVAELSSTVDAAREELERMRgasVPADEHEHALSALRDHVTRLQAQLADLAR----RHEKTSAEVFQVQREALFMKSER 812
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVE---ENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 813 HAAEAQLATAEQQLRGLRTEAERARQaqsRAQEALDKAKEKDKKITDLSKEvftlkEALKVQQSTPASSKEEEALRGQVT 892
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEK---RLEEIEQLLEELNKKIKDLGEE-----EQLRVKEKIGELEAEIASLERSIA 311
|
170
....*....|..
gi 568968514 893 ALQQQIQEEARE 904
Cdd:TIGR02169 312 EKERELEDAEER 323
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
691-900 |
2.74e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 691 AEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEHEHAL 770
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 771 SALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKA 850
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568968514 851 KEKDKKITDLSKEVFTLKEALKVQQSTPASSKEE------------EALRGQVTALQQQIQE 900
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEealeelpeppdlEELERELERLEREIEA 778
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
50-142 |
3.17e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.18 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 50 MNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHY 129
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
90
....*....|...
gi 568968514 130 GALTGDKLILQLL 142
Cdd:PHA02874 197 AAEYGDYACIKLL 209
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
18-255 |
3.32e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.47 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 18 DIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQdlQGRTALMLA 97
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 98 CEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTGDKLILQLLHESArrssppsasleEDSGEASSQNSVSSHEKQGA 177
Cdd:PLN03192 630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG-----------ADVDKANTDDDFSPTELREL 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 178 PKKRK------APQPPASTPVPDDRDAYEEIVRLRQERGRLLQKIR-GLEQHKERRRKEPLEAEASSVHSLERQVQELQQ 250
Cdd:PLN03192 699 LQKRElghsitIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRvSIYKGHPLLRNERCCNEAGKLINLPPSLEELKA 778
|
....*
gi 568968514 251 MLAEK 255
Cdd:PLN03192 779 IAGEK 783
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
76-124 |
3.58e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568968514 76 LLQQG-AATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQ 124
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
695-875 |
4.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 695 EAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERmrgasvpaDEHEHALSALR 774
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--------EALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 775 DHVTRLQAQLADLARRHEK---TSAEVFQVQRE-ALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKA 850
Cdd:COG4717 146 ERLEELEERLEELRELEEEleeLEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180
....*....|....*....|....*
gi 568968514 851 KEkdkKITDLSKEVFTLKEALKVQQ 875
Cdd:COG4717 226 EE---ELEQLENELEAAALEERLKE 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-387 |
5.24e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 197 DAYEEIVRLRQERGRLLQKIRGLEQHKE--RRRKEPLEAEASSVHSLERQ------VQELQQMLAEKQEEKESLGR---E 265
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDAssdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 266 VESLQSRLSLLENERENTSYDVATLQDEEGEMpdfpgadalmpKNQSPSAEEIVASLQEQVAQLTRQNQ----ELLEKVQ 341
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRL-----------EKELEQAEEELDELQDRLEAAEDLARlelrALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568968514 342 ILEEFEKDEAQMAEESQAEVvplvlyESLRAELEQLRRQYTEAMHS 387
Cdd:COG4913 756 AAALGDAVERELRENLEERI------DALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
701-832 |
5.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 701 SRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGASVPADEhehalsalrdhvTRL 780
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR------------ALL 751
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568968514 781 QAQLADLARRhektsaEVFQVQREALfmKSERHAAEAQLATAEQQLRGLRTE 832
Cdd:COG4913 752 EERFAAALGD------AVERELRENL--EERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
694-851 |
6.75e-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: 43.52 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 694 EEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELErmrGASVPADEHEHALSAL 773
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE---KLKREINELKRELDRL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 774 RDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAE-------AQLATAEQQLRGLRTEAERARQAQSRAQEA 846
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
....*
gi 568968514 847 LDKAK 851
Cdd:TIGR02169 492 LAEAE 496
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
26-141 |
6.83e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.33 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 26 TALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEG-GSPE 104
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 568968514 105 TVEVLLQGGAQLSITDA-LGQDATHYGALTGDKLILQL 141
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLL 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-380 |
7.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 196 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKE----PLEAEassVHSLERQ----------VQELQQMLAEKQEEKES 261
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvaSAERE---IAELEAElerldassddLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 262 LGREVESLQSRLSLLENERENTSYDVATLQDEEGEMPD------FPGADALMPK-NQSPSAEEIVASLQEQVAQLTRQNQ 334
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelRALLEERFAAaLGDAVERELRENLEERIDALRARLN 783
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568968514 335 ELLEK-VQILEEFEKDEAQMAEESQAEVvplVLYESLRAELEQLRRQ 380
Cdd:COG4913 784 RAEEElERAMRAFNREWPAETADLDADL---ESLPEYLALLDRLEED 827
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
689-853 |
7.52e-04 |
|
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: 42.22 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMRGAsvpadeheh 768
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 769 alsalrDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALD 848
Cdd:COG1579 89 ------KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*
gi 568968514 849 KAKEK 853
Cdd:COG1579 163 AEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-349 |
7.86e-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: 43.52 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 196 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEASSVHsLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 275
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 276 LENERENTSYDVATLQDEEGEMPDFPGADALMPK-------------------NQSPSAEEIVA----SLQEQVAQLTRQ 332
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqrveeeiralepvnMLAIQEYEEVLkrldELKEKRAKLEEE 1001
|
170
....*....|....*..
gi 568968514 333 NQELLEKVQILEEFEKD 349
Cdd:TIGR02169 1002 RKAILERIEEYEKKKRE 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-385 |
7.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 196 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRkepLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 275
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELEYLRAALR---LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 276 LENERENTSYD-VATLQDEegempdfpgadalmpknqspsaeeiVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMA 354
Cdd:COG4913 328 LEAQIRGNGGDrLEQLERE-------------------------IERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190
....*....|....*....|....*....|.
gi 568968514 355 EESQAEVVPLVlyESLRAELEQLRRQYTEAM 385
Cdd:COG4913 383 AALRAEAAALL--EALEEELEALEEALAEAE 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
764-900 |
8.01e-04 |
|
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: 42.22 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 764 DEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTE----------- 832
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeie 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 833 --AERARQAQSRAQEALDKAKEKDKKITDLSKEVFTLKEALKVQQStpASSKEEEALRGQVTALQQQIQE 900
Cdd:COG1579 100 slKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA--ELDEELAELEAELEELEAEREE 167
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
18-114 |
8.51e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.67 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 18 DIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLA 97
Cdd:PHA02875 96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
90
....*....|....*..
gi 568968514 98 CEGGSPETVEVLLQGGA 114
Cdd:PHA02875 176 MAKGDIAICKMLLDSGA 192
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
17-64 |
8.68e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 8.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIA 64
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
195-384 |
8.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 195 DRDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEA---------SSVHSLERQVQELQQMLAEKQEEKESLGRE 265
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleeheerrEELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 266 VESLQSRLSLLENERENT---------SYDVATLQDEEGEMPDFPGADALMPKNQSPSA-EEIVASLQEQVAQLTRQNQE 335
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddaDAEAVEARREELEDRDEELRDRLEECRVAAQAhNEEAESLREDADDLEERAEE 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568968514 336 LLEKVQILEEFEKDEAQMAEESQAEVvplvlyESLRAELEQLRRQYTEA 384
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEI------EELEEEIEELRERFGDA 403
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
707-875 |
1.07e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 707 LRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELErmrgasvpadehehALSALRDhvtRLQAQLAD 786
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS--------------AAEAERS---RLQALLAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 787 LARRheKTSAEvfqvQREALfMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDK----KITDLSK 862
Cdd:PRK09039 107 LAGA--GAAAE----GRAGE-LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDResqaKIADLGR 179
|
170
....*....|....*
gi 568968514 863 EvftLKEAL--KVQQ 875
Cdd:PRK09039 180 R---LNVALaqRVQE 191
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
680-806 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 680 AAELEAARGRFAEAEEAARGRS-RELEALRELLATATATGERARTEAAELRQALA-------ASEARVAELSSTVDAARE 751
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLE 394
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568968514 752 ELERMRGA-SVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVqREAL 806
Cdd:COG4913 395 ALEEELEAlEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDAL 449
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
695-846 |
1.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 695 EAARGRSRELEALRELLATATATGERARTEA------AELRQALAASEARVAELSST-------VDAAREELERMRGASv 761
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQL- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 762 pADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVfqvqrealfmkserhaaeAQLATAEQQLRGLRTEAERAR---- 837
Cdd:COG3206 308 -QQEAQRILASLEAELEALQAREASLQAQLAQLEARL------------------AELPELEAELRRLEREVEVARelye 368
|
....*....
gi 568968514 838 QAQSRAQEA 846
Cdd:COG3206 369 SLLQRLEEA 377
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
89-120 |
1.41e-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: 36.88 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|...
gi 568968514 89 QGRTALMLAC-EGGSPETVEVLLQGGAQLSITD 120
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
664-850 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 664 RIRgleealrrREREAAAELEAARGRFAEAEEAARGRSRELEALREL----LATATATGERARTEAAelRQALAASEARV 739
Cdd:COG4913 618 ELA--------ELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeIDVASAEREIAELEAE--LERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 740 AELSSTVDAAREELERMRGAsvpADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALfmkSERHAAEAQL 819
Cdd:COG4913 688 AALEEQLEELEAELEELEEE---LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---EERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|.
gi 568968514 820 ATAEQQLRGLRTEAERARQAQSRAQEALDKA 850
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
232-380 |
1.68e-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: 41.48 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 232 EAEASSVHSLERQVQELQQMLAEKQEEKESLG----REVESLQSRLSLLENERENTSydvATLQDEE--------GEMPD 299
Cdd:pfam15397 77 EKEESKLNKLEQQLEQLNAKIQKTQEELNFLStykdKEYPVKAVQIANLVRQLQQLK---DSQQDELdeleemrrMVLES 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 300 FpgADALMPKNQ---SPSAEEIVASLQEQVAQLTRQNQELLEKvqiLEEFEKDEAQMAEESQAevvplvlyesLRAELEQ 376
Cdd:pfam15397 154 L--SRKIQKKKEkilSSLAEKTLSPYQESLLQKTRDNQVMLKE---IEQFREFIDELEEEIPK----------LKAEVQQ 218
|
....
gi 568968514 377 LRRQ 380
Cdd:pfam15397 219 LQAQ 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
196-282 |
1.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 196 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSL 275
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
....*..
gi 568968514 276 LENEREN 282
Cdd:COG4717 232 LENELEA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
695-927 |
1.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 695 EAARGRSRELEALRELLATAtatgERARTEAAELRQALAASEA-----RVAELSSTVDAAREELERMRGASVPADEHEHA 769
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKA----EEDKKKADELKKAAAAKKKadeakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 770 LSALRDHVTRLQAQLADLARR--HEKTSAEVFQVQREALFMKSE--RHAAEAQLATAEQQLRGLRTEAERARQAQ-SRAQ 844
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKADEAKKAEEAKKADEAKKAEeAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 845 EALDKAKEKdKKITDLSK--EVFTLKEALKVQQSTPASSKEEEALRGQVTALQQqiqEEAREHGAVVALYRTHLLYAIQG 922
Cdd:PTZ00121 1537 DEAKKAEEK-KKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEA 1612
|
....*
gi 568968514 923 QMDED 927
Cdd:PTZ00121 1613 KKAEE 1617
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-94 |
1.82e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 41.48 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968514 17 VDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTAL 94
Cdd:COG0666 212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
758-912 |
2.56e-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: 41.29 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 758 GASVPADEHEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERAR 837
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 838 QAQSRAQEALDKAKEKDKKITDLSKEVF---------TLKEALKVQQSTPASSKEEEALRGQVTALQQQIQEEAREHGAV 908
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
....
gi 568968514 909 VALY 912
Cdd:COG4942 177 EALL 180
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
57-87 |
2.57e-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: 36.11 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|..
gi 568968514 57 GATPLIIAAQMC-HTDLCRLLLQQGAATNDQD 87
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-853 |
2.63e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 691 AEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELErmrgasvpADEHEHAL 770
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE--------ELLEALDE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 771 SALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSER--HAAEAQLATAEQQLRglrtEAERARQAQSRAQEALD 848
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELR----ELAEEWAALKLALELLE 503
|
....*
gi 568968514 849 KAKEK 853
Cdd:COG4717 504 EAREE 508
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
90-118 |
3.58e-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: 3.58e-03
10 20
....*....|....*....|....*....
gi 568968514 90 GRTALMLACEGGSPETVEVLLQGGAQLSI 118
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
688-855 |
3.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 688 GRFAEAEEAArgrsRELEALRELLATATATGERARTEAAELRQALAASEA--RVAELSSTVDAAREELERMRGASVPADE 765
Cdd:COG4717 78 EELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 766 HEHALSALRDHVTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERH-AAEAQLATAEQQLRGLRTEAERARQAQSRAQ 844
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|.
gi 568968514 845 EALDKAKEKDK 855
Cdd:COG4717 234 NELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
194-281 |
3.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 194 DDRDAYEEIVRLRQERGRLLQKIRGLEQHKERRRKEPLE-AEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSR 272
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
....*....
gi 568968514 273 LSLLENERE 281
Cdd:COG4717 462 LEQLEEDGE 470
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
17-142 |
3.98e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.80 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 17 VDIEDSSGWTALHHAAAGGC--LSCSKLLCSFKAHMNPRDR----------------SGATPLIIAAQMCHTDLCRLLLQ 78
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLD 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968514 79 QGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDA--LGQDATHYGALTGDKLILQLL 142
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtlLYFKDKDLNTITKIKMLKKSI 279
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
219-355 |
5.36e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 219 LEQHKERRRK--EPLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENERENTSYDVATLQDEEGE 296
Cdd:pfam15921 470 LESTKEMLRKvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968514 297 mpdfpgADALmpKNQSPSAEEIVASLQEQVAQLTR--------QNQELLEKVQILEEFEKDEAQMAE 355
Cdd:pfam15921 550 ------CEAL--KLQMAEKDKVIEILRQQIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQE 608
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
206-434 |
5.51e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 206 RQERGRLLQKIRGLEQHKER-----RRKEPLEAEASSVHSLERQVQELQQMLAE-KQEEKESLGREVESLQSRLSLLEN- 278
Cdd:COG5022 857 AKKRFSLLKKETIYLQSAQRvelaeRQLQELKIDVKSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKKl 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 279 ----------ERENTSYD-VATLQDEEGEMpdfpgadalmpKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFE 347
Cdd:COG5022 937 lnnidleegpSIEYVKLPeLNKLHEVESKL-----------KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 348 KD-EAQMAEESQAEVVPLVLyeslrAELEQLRRQYTEAMHSQQQQQEGEPPRAQEGEETAYQEIKDKGITIQNGPSVPDL 426
Cdd:COG5022 1006 KQyGALQESTKQLKELPVEV-----AELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDD 1080
|
....*...
gi 568968514 427 NGTTYAET 434
Cdd:COG5022 1081 KQLYQLES 1088
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
691-852 |
5.69e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 691 AEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALA---ASEARVAELSSTVDAAREEL-ERMRGASVPADEH 766
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELrDRLEECRVAAQAH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 767 EHALSALRDHVTRLQAQLADLarrhektsaevfqvQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEA 846
Cdd:PRK02224 341 NEEAESLREDADDLEERAEEL--------------REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
....*.
gi 568968514 847 LDKAKE 852
Cdd:PRK02224 407 LGNAED 412
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
689-900 |
6.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 689 RFAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREELERMR----GASVPAD 764
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfgDAPVDLG 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 765 EHEHALSALRDHVTRLQAQLADLarRHEKTSAEVFQVQREALF-----------MKSERHAAEaqLATAEQQLRGLRTEA 833
Cdd:PRK02224 409 NAEDFLEELREERDELREREAEL--EATLRTARERVEEAEALLeagkcpecgqpVEGSPHVET--IEEDRERVEELEAEL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968514 834 ERARQAQSRAQEALDKAK---EKDKKITDLSKEVFTLKEALKVQQSTPASSKEE-EALRGQVTALQQQIQE 900
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEdlvEAEDRIERLEERREDLEELIAERRETIEEKRERaEELRERAAELEAEAEE 555
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
89-114 |
6.65e-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: 6.65e-03
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
15-85 |
6.98e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.03 E-value: 6.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968514 15 CVVDIEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMNPRDRSGATPLIIAAQMCHTDLCRLLLQQGAATND 85
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-294 |
7.76e-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: 40.04 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 139 LQLLHESARRSSPPSASLEEDSGEASSQNSVSSHEKQGAPKKRKAPQPPASTPVPDDRDAYEEIVRLRQERGRLLQKIRG 218
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968514 219 LEQHKERRRKEPLEAEASSVhslERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENERENTSYDVATLQDEE 294
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLE---EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
55-145 |
8.62e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 39.59 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 55 RSGATPLIIAAQMCHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSPETVEVLLQGGAQLSITDALGQDATHYGALTG 134
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
90
....*....|.
gi 568968514 135 DKLILQLLHES 145
Cdd:PHA02875 180 DIAICKMLLDS 190
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
694-904 |
9.02e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 694 EEAARGRSRELEALR----ELLATATATGERARTEAAElrqaLAASEARVAElsSTVDAAREELERMRgasvpADEHEHA 769
Cdd:NF041483 476 EEAARTAEELLTKAKadadELRSTATAESERVRTEAIE----RATTLRRQAE--ETLERTRAEAERLR-----AEAEEQA 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 770 LSalrdhvTRLQAQLADLARRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARqaQSRAQEALDK 849
Cdd:NF041483 545 EE------VRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIR--REAAEETERL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968514 850 AKEKDKKITDLSKEVFTLKEALKVQQSTPASSKEEEA------LRGQVTALQQQIQEEARE 904
Cdd:NF041483 617 RTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGenvavrLRSEAAAEAERLKSEAQE 677
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
26-116 |
9.37e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 39.66 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 26 TALHHAAAGGCLSCS-KLLCSFKAHMNPRDRSGATPLIIAAQM-CHTDLCRLLLQQGAATNDQDLQGRTALMLACEGGSp 103
Cdd:PHA02876 410 TALHFALCGTNPYMSvKTLIDRGANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG- 488
|
90
....*....|...
gi 568968514 104 eTVEVLLQGGAQL 116
Cdd:PHA02876 489 -IVNILLHYGAEL 500
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
690-836 |
9.74e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 690 FAEAEEAAR-GRSREL-EALRELLATATATGERARTEAAELRQALAASEARVAELSSTVDAAREEL----ERMRGASVPA 763
Cdd:COG3096 970 FSYEDAVGLlGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLqeleQELEELGVQA 1049
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968514 764 DehEHALSALRDHVTRLQAQLAdlARRHEKTSAEVfQVQRealfMKSERHAAEAQLATAEQQLRGLRTEAERA 836
Cdd:COG3096 1050 D--AEAEERARIRRDELHEELS--QNRSRRSQLEK-QLTR----CEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
200-385 |
9.74e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 200 EEIVRLRQERGRLLQKIRGLEQHKERRRKEpLEAEASSVHSLERQVQELQQMLAEKQEEKESLGREVESLQSRLSLLENE 279
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 280 RENTSYDVATLQDEEGEMPDFPGADALMPKNQSPSAEEIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQMAEESQA 359
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180
....*....|....*....|....*.
gi 568968514 360 evvplvlyesLRAELEQLRRQYTEAM 385
Cdd:COG4942 179 ----------LLAELEEERAALEALK 194
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
248-380 |
9.85e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968514 248 LQQMLAEKQEEKESLGREVESLQSRLSLLENERENTSYDVATLQDEegempdfpgadalmpknqSPSAEEIVASLQEQVA 327
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS------------------LSAAEAERSRLQALLA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568968514 328 QLTRQNQELLEKVQILEEFEKDEAQMAEESQAEVvplvlyESLRAELEQLRRQ 380
Cdd:PRK09039 106 ELAGAGAAAEGRAGELAQELDSEKQVSARALAQV------ELLNQQIAALRRQ 152
|
|
| |
