|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
4-263 |
1.52e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 145.48 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 4 LLLEPRAPPAPRAPDAMKQLCLCAAASFASQDWGKSDERLLQAVENNDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMR 83
Cdd:COG0666 18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 84 GAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKA 163
Cdd:COG0666 98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 164 HLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAH 243
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
|
250 260
....*....|....*....|
gi 18916882 244 YGALAGDKLILHLLQEAAQR 263
Cdd:COG0666 258 LAAAAGAALIVKLLLLALLL 277
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
38-284 |
3.15e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.55 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 38 KSDERLLQAVENNDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYG 117
Cdd:COG0666 19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 118 HPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAA 197
Cdd:COG0666 99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 198 ANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLLQEAAQRPSPPSALTEDDSGE 277
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
|
....*..
gi 18916882 278 ASSQNSM 284
Cdd:COG0666 259 AAAAGAA 265
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
43-242 |
6.57e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.44 E-value: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 43 LLQAVENNDAPRVAALIArKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCL 122
Cdd:COG0666 91 LHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 123 KQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQD 202
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18916882 203 LQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAA 242
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-260 |
1.45e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 110.43 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 55 VAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDV 134
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 135 VDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACE 214
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18916882 215 GASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLLQEA 260
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
110-202 |
1.85e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.71 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 110 LHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSfKAHLNPQDrSGATPLIIAAQMCHTDLCR 189
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 18916882 190 LLLQQGAAANDQD 202
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
77-169 |
1.27e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 78.62 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 77 FHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQaSCVVDVVDsSGWTALHHAAAGGCLSCSE 156
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 18916882 157 VLCSFKAHLNPQD 169
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
58-233 |
9.32e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 58 LIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGS---NVMSTDGAgyNALHLAAKYGHPQCLKQLLQASCVVDV 134
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 135 VDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALM-LAC 213
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|
gi 18916882 214 EGASPETVEVLLQGGAQPGI 233
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
43-136 |
1.12e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 43 LLQAVENNDAPRVAALIaRKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDgaGYNALHLAAKYGHPQCL 122
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 18916882 123 KQLLQASCVVDVVD 136
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
70-229 |
1.18e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.82 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 70 DPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAG 149
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 150 GCLSCSEVLCSFKAHLNPQdrSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGA 229
Cdd:PLN03192 602 KHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
53-212 |
3.50e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.67 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 53 PRVAALIARKGLVPTKLDPEGKSAFHlAAMRGAASCLEV---MIAHGSNVMSTDGAGYNALHLAAKYGHP--QCLKQLLQ 127
Cdd:PHA03095 132 PKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELlrlLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 128 ASCVVDVVDSSGWTALHHAAAGGclSCSEVLCSF----KAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDL 203
Cdd:PHA03095 211 AGCDPAATDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
|
....*....
gi 18916882 204 QGRTALMLA 212
Cdd:PHA03095 289 DGNTPLSLM 297
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-863 |
5.92e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 309 DDRDAYEEIVRLRQERGRLLQKIRGLEQHKEQRQQESPEASSLHI----LERQVQELQQLLVERQEEKESLGREVESLQS 384
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAeleeLRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 385 RLSLLENERENTSYDVTTLQDEEGELpdlpgaevllsrqlspsaQEHLASLQEQVAVLTRQNQELMEKVQILENFEKDET 464
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL------------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 465 QMEVEALAEVIP-LALYDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAACGESEVAGATATKNgpthmELNGSVAP 543
Cdd:COG1196 365 EALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-----ELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 544 ETKVNGAETIDEEAAGDETMEARTMEAEATGAKATGAEATGAKVTETkpTGAEVREMETTEEEANMETKPTGAQATDTET 623
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 624 ---TGVEAMGVEATKTKAEEAEMQAYGVGAGQAeppvtgttnmeatGSRATGMEATGVSATGVENPGVEATvpgISAGPI 700
Cdd:COG1196 518 glrGLAGAVAVLIGVEAAYEAALEAALAAALQN-------------IVVEDDEVAAAAIEYLKAAKAGRAT---FLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 701 LHPGAAEASEKLQVELETRIRGLEEALRQREREAAAELEAALGKC-EAAEAEAGRLRERVREAEGSGASGGGGGDTTQLR 779
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 780 AALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQR 859
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
....
gi 18916882 860 TAAA 863
Cdd:COG1196 742 LEEE 745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
315-849 |
1.94e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRLLQKIRGLEQHKEQRQQEspeassLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERE 394
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 395 NTSYDVTTLQDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKDETQMEVEALAEV 474
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 475 IPLALYDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAACGESEVAGATATKNGPTHMELNGSVAPETKVNGAETID 554
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 555 EEAAGDETMEARTMEAEATGAKATGAEATGAKVTETKP-------TGAEVREMETTEEEANMETKPTGAQATDTETTGVE 627
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 628 AMGVEATKTKAEEAEMQAYGVGAGQAEPPVtgttnmEATGSRATGMEATGVSATGVENPGVEATVPGISAGPILHPGAAE 707
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALA------AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 708 ASEKLQVELETRIRGLEEALRQREREAAAELEAALGkcEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQARE 787
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE--LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18916882 788 DLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARL----EQSRELEVLREQLA 849
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIE 777
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
176-257 |
1.23e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.59 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 176 LIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDalGQDAAHYGALAGDKLILH 255
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
..
gi 18916882 256 LL 257
Cdd:pfam12796 79 LL 80
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
61-226 |
1.35e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.81 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 61 RKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDvvDSSGW 140
Cdd:PLN03192 546 KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAG 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 141 TALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQgrtalmlacEGASPET 220
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD---------DDFSPTE 694
|
....*.
gi 18916882 221 VEVLLQ 226
Cdd:PLN03192 695 LRELLQ 700
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
92-146 |
7.31e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 52.35 E-value: 7.31e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 18916882 92 MIAHGS-NVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHA 146
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
70-240 |
8.16e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 70 DPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAG 149
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 150 GCLSCSEVLCSFKAHLNPQDRSGATPLIIAaqMCHTDLCRLLLQQGAAANDQDLQGRTALMLACE-GASPETVEVLLQGG 228
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHK 278
|
170
....*....|..
gi 18916882 229 AQPGITDALGQD 240
Cdd:PHA02874 279 ADISIKDNKGEN 290
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
89-257 |
1.65e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.75 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 89 LEVMIAHGSNVMSTDGAGYNALHLAA--KYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGC--LSCSEVLCSFKAH 164
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 165 LNPQDRsgatpliiaaqmchtdlCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHY 244
Cdd:PHA03100 169 INAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
|
170
....*....|...
gi 18916882 245 GALAGDKLILHLL 257
Cdd:PHA03100 232 AILNNNKEIFKLL 244
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
106-158 |
3.14e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 3.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 18916882 106 GYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVL 158
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
174-225 |
6.36e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 6.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18916882 174 TPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLL 225
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
139-192 |
1.03e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.03e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 18916882 139 GWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLL 192
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-516 |
1.08e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRLLQKIRGLEQHKE---------QRQQESPEASSLHiLERQVQELQQLLVERQEEKESLGREVESLQSR 385
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQilrerlanlERQLEELEAQLEE-LESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 386 LSLLENERENTSYDVTTLQDE----EGELPDLPGAEVLLSRQLSpSAQEHLASLQEQVAVLTRQNQELMEKvqiLENFEK 461
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQletlRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEELLKK---LEEAEL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18916882 462 DETQMEVEALAEVIplalyDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAA 516
Cdd:TIGR02168 436 KELQAELEELEEEL-----EELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
50-200 |
1.18e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 55.06 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 50 NDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMR--GAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQC------ 121
Cdd:PHA03100 83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkll 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 122 ------------LKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCR 189
Cdd:PHA03100 163 idkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242
|
170
....*....|.
gi 18916882 190 LLLQQGAAAND 200
Cdd:PHA03100 243 LLLNNGPSIKT 253
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
86-235 |
2.24e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 86 ASCLEVMIAHGSNV-MSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAH 164
Cdd:PHA02878 147 AEITKLLLSYGADInMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18916882 165 LNPQDRSGATPLIIAAQMC-HTDLCRLLLQQGAAANDQD-LQGRTALMLACEgaSPETVEVLLQGGAQPGITD 235
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYCkDYDILKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYGADINSLN 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
311-509 |
4.88e-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: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 311 RDAYEEIVRLRQERGRLLQKIRGLEQHKEQRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLE 390
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 391 NERENTSYDVTTLQDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEK-VQILENF------EKDE 463
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaETAD 806
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18916882 464 TQMEVEALAEVipLALYDSLRAefDQLRRQHAEALQALRQQETREV 509
Cdd:COG4913 807 LDADLESLPEY--LALLDRLEE--DGLPEYEERFKELLNENSIEFV 848
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
75-126 |
1.48e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 1.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18916882 75 SAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLL 126
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
93-243 |
1.65e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.56 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 93 IAHGSNVMSTDGAGYNALHLAAKYGHPQClkqllqascvVDVVDssgwtALhhAAAGgclscsevlcsfkAHLNPQDRSG 172
Cdd:PHA03095 34 LAAGADVNFRGEYGKTPLHLYLHYSSEKV----------KDIVR-----LL--LEAG-------------ADVNAPERCG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18916882 173 ATPLIiaAQMCHT---DLCRLLLQQGAAANDQDLQGRTALMLACEGAS--PETVEVLLQGGAQPGITDALGQDAAH 243
Cdd:PHA03095 84 FTPLH--LYLYNAttlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
311-507 |
4.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 311 RDAYEEIVRLRQERgRLLQKIRGL-EQHKEQRQQESP-----EASSLHILERQVQELQQLLVERQEEKESLGREVESLQS 384
Cdd:COG4913 238 ERAHEALEDAREQI-ELLEPIRELaERYAAARERLAEleylrAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 385 RLSLLENERENtsydvttlqdeegelpdlpgaevlLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILenfekdet 464
Cdd:COG4913 317 RLDALREELDE------------------------LEAQIRGNGGDRLEQLEREIERLERELEERERRRARL-------- 364
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18916882 465 qmevEALAEVIPLALYDSlRAEFDQLRRQHAEALQALRQQETR 507
Cdd:COG4913 365 ----EALLAALGLPLPAS-AEEFAALRAEAAALLEALEEELEA 402
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
58-179 |
4.61e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.96 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 58 LIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGhpQCLKQLLQASCVVDVVDS 137
Cdd:PHA02874 175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDI 252
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18916882 138 SGWTALHHAAAGGC-LSCSEVLCSFKAHLNPQDRSGATPLIIA 179
Cdd:PHA02874 253 DGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
315-507 |
7.08e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRLLQKIRGLEQH-KEQRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENER 393
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKElAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 394 ENTSYDVTTLQDEEGELPDLPGAEVLLS--------------RQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENF 459
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSpedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18916882 460 eKDETQMEVEALAEVIplALYDSLRAEFDQLRRQHAEALQALRQQETR 507
Cdd:COG4942 180 -LAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
122-228 |
9.47e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 122 LKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQ 201
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
|
90 100
....*....|....*....|....*..
gi 18916882 202 DLQGRTALMLACEGASPETVEVLLQGG 228
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHG 213
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
341-479 |
1.06e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 341 RQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSYDVTTLQDEEGELP---DLPGAE 417
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEgraGELAQE 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18916882 418 VLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKdETQMEVEALAEVIPLAL 479
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAKIADLGRRLNVAL 185
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
73-246 |
1.08e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.87 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 73 GKSAFHLAAMRGA-ASCLEVMIAHGSNVMSTDGAGYNALH--LAAKYGHPQCLKQLLQASCVVDVVDSSGWTALH----- 144
Cdd:PHA03095 83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllks 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 145 HAAaggCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLC--RLLLQQGAAANDQDLQGRTALMLACEGASPETVE 222
Cdd:PHA03095 163 RNA---NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL 239
|
170 180
....*....|....*....|....*.
gi 18916882 223 V--LLQGGAQPGITDALGQDAAHYGA 246
Cdd:PHA03095 240 VlpLLIAGISINARNRYGQTPLHYAA 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-504 |
1.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 312 DAYEEIVRLRQERGRLLQKIRGLEQHKEQRQQEspeassLHILERQVQELQQLLVERQEEK--ESLGREVESLQSRLSLL 389
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAE------LDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 390 enerENTSYDVTTLQDEEGELpdlpGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKDETQMEVE 469
Cdd:COG4913 681 ----DASSDDLAALEEQLEEL----EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190
....*....|....*....|....*....|....*.
gi 18916882 470 A-LAEVIPLALYDSLRAEFDQLRRQHAEALQALRQQ 504
Cdd:COG4913 753 ErFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
41-237 |
1.89e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.52 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 41 ERLLQavennDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQ 120
Cdd:PHA02876 151 ERIQQ-----DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNID 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 121 CLKQLLQASCVVDVVDSSgwtaLHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMchTDLCRL---LLQQGAA 197
Cdd:PHA02876 226 TIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQA--PSLSRLvpkLLERGAD 299
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18916882 198 ANDQDLQGRTAL-MLACEGASPETVEVLLQGGAQPGITDAL 237
Cdd:PHA02876 300 VNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRL 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
708-863 |
2.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 708 ASEKLQvELETRIRGLEEALRQREREAaaeleaalgkcEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQARE 787
Cdd:COG4913 608 NRAKLA-ALEAELAELEEELAEAEERL-----------EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18916882 788 DLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAA 863
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
405-638 |
5.35e-05 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 47.16 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 405 DEEGELPDLPgaEVLLSRQLSPSAQEHLASLQeqVAVLTrqnqelMEKVQILENfEKDETQMEVEALAEVIPLALY---- 480
Cdd:PLN03237 1090 DDAAEEEEEI--DVSSSSGVRGSDYDYLLSMA--IGTLT------LEKVQELCA-DRDKLNIEVEDLKKTTPKSLWlkdl 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 481 DSLRAEFDQLRRQHAEALQALRQQetrevprEEGAACGESEvAGATATKNGPThmelngsvAPETKVNGAETIDEEAAgD 560
Cdd:PLN03237 1159 DALEKELDKLDKEDAKAEEAREKL-------QRAAARGESG-AAKKVSRQAPK--------KPAPKKTTKKASESETT-E 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 561 ETMEARTMEAE--ATGAKATGAEATGAKVTETKPTGAEVREMETTEE---EANMETKPTGAQATDTETTGVEAMGVEATK 635
Cdd:PLN03237 1222 ETYGSSAMETEnvAEVVKPKGRAGAKKKAPAAAKEKEEEDEILDLKDrlaAYNLDSAPAQSAKMEETVKAVPARRAAARK 1301
|
...
gi 18916882 636 TKA 638
Cdd:PLN03237 1302 KPL 1304
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
315-492 |
6.37e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRLLQKIrgLEQHKEQRQQESPEASSLHILERQVQELQQL---LVERQEEKESLGREVESLQSRLSLLEN 391
Cdd:PRK03918 189 ENIEELIKEKEKELEEV--LREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 392 ERENTSYDVTTLQDEEGELPDLPGAE---VLLSRQLSPSAQE------HLASLQEQVAVLTRQNQELMEKVQILENFEK- 461
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDElreiekRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190
....*....|....*....|....*....|..
gi 18916882 462 -DETQMEVEALAEviPLALYDSLRAEFDQLRR 492
Cdd:PRK03918 347 lKELEKRLEELEE--RHELYEEAKAKKEELER 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
315-491 |
9.51e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRLLQKIRGLEQHKEQRQQESPEA-SSLHILERQVQELQQLLVERQEE----------KE----SLGREV 379
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLqQEKELLEKEIERLKETIIKNNSEikdltnqdsvKEliikNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 380 ESLQSRLSLLENERENTSydvTTLQDEEGELpDLPGAEVLlsrqlspSAQEHLASLQEQVAVLTRQNQELMEKVQILEN- 458
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIK---QNLEQKQKEL-KSKEKELK-------KLNEEKKELEEKVKDLTKKISSLKEKIEKLESe 532
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18916882 459 --------------FEKDETQMEVEALAEVIplalyDSLRAEFDQLR 491
Cdd:TIGR04523 533 kkekeskisdledeLNKDDFELKKENLEKEI-----DEKNKEIEELK 574
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-516 |
1.16e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 321 RQERGRLLQKIRGLEQHKEQRQQEspeassLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSYDV 400
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 401 ttlQDEEGELPDLPGAEVLLSRQLSpSAQEHLASLQEQVAVLTRQNQELMEKVQILENfEKDETQMEVEALAEviplaLY 480
Cdd:TIGR02168 750 ---AQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNE-----EA 819
|
170 180 190
....*....|....*....|....*....|....*..
gi 18916882 481 DSLRAEFDQLRRQHAEALQALRQ-QETREVPREEGAA 516
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDlEEQIEELSEDIES 856
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-556 |
1.73e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 316 EIVRLRQERGRLLQKIRGLEQHKEQRQQESPEA-SSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERE 394
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELeEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 395 NtsyDVTTLQDEEGELPDLPGAEVLLSRQLSpSAQEHLASLQEQVAVLTRQNQELMEKVQILEN-FEKDETQMEVEALAE 473
Cdd:TIGR02168 313 N---LERQLEELEAQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 474 VIPLALYDSLRAEFDQLRRQhAEALQAlRQQETREVPREEGAACGESEVAGATATKNGPTHMELNGSVAPETKVNGAETI 553
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEAR-LERLED-RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
...
gi 18916882 554 DEE 556
Cdd:TIGR02168 467 REE 469
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
58-113 |
1.76e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 1.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 18916882 58 LIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLA 113
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
310-572 |
1.76e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 310 DRDAYEEIVRLRQErgrllqkIRGLEQHKEQRQQESPEASSLHI----LERQVQELQQLLVERQEEKESLGRE------- 378
Cdd:pfam12128 229 DIQAIAGIMKIRPE-------FTKLQQEFNTLESAELRLSHLHFgyksDETLIASRQEERQETSAELNQLLRTlddqwke 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 379 -VESLQSRLSLLENERENTSYDVTTLQDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILE 457
Cdd:pfam12128 302 kRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 458 NFEKDETQMEVEALaeviplalYDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAACGESEVAGATATKNGPTHMEL 537
Cdd:pfam12128 382 SKIKEQNNRDIAGI--------KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRL 453
|
250 260 270
....*....|....*....|....*....|....*.
gi 18916882 538 NGSVA-PETKVNGAETIDEEAAGDETMEARTMEAEA 572
Cdd:pfam12128 454 NQATAtPELLLQLENFDERIERAREEQEAANAEVER 489
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
143-225 |
1.89e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 143 LHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVE 222
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 18916882 223 VLL 225
Cdd:PTZ00322 166 LLS 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
706-861 |
3.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 706 AEASEKLQVELETRIRGLEEALRQREREAaaeleaalgkcEAAEAEAGRLRERVREAEGSGASGGGGGDTtqLRAALEQA 785
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAA-----------QAHNEEAESLREDADDLEERAEELREEAAE--LESELEEA 375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18916882 786 REDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTA 861
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
319-508 |
4.94e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 319 RLRQERGRLLQKIRGLEQHKEQRQQESPEASSLHILErQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSY 398
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ-QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 399 DvTTLQDEEGELPDLPGAEVLLSRQLSPSAQEhLASLQEQVAVLTRQNQELMEKVQILENFEKDETQMEVEALAEVIpla 478
Cdd:COG3206 262 S-PVIQQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL--- 336
|
170 180 190
....*....|....*....|....*....|
gi 18916882 479 lyDSLRAEFDQLRRQHAEALQALRQQETRE 508
Cdd:COG3206 337 --AQLEARLAELPELEAELRRLEREVEVAR 364
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
205-257 |
5.03e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 5.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 18916882 205 GRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLL 257
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
96-230 |
7.25e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.13 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 96 GSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCS-EVLCSFKAHLNPQDRSGAT 174
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKDLST 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18916882 175 PLIIAAQM-CHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASpeTVEVLLQGGAQ 230
Cdd:PHA02876 445 PLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
319-507 |
7.84e-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: 43.13 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 319 RLRQERgrlLQKIRGLEQHKEQRQQESPE-ASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENEREnts 397
Cdd:TIGR02169 202 RLRRER---EKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE--- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 398 ydvttlqDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENfEKDETQMEVEALAEVIP- 476
Cdd:TIGR02169 276 -------ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEe 347
|
170 180 190
....*....|....*....|....*....|..
gi 18916882 477 -LALYDSLRAEFDQLRRQHAEALQALRQQETR 507
Cdd:TIGR02169 348 eRKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
700-861 |
8.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 700 ILHPGAAEASEKLQVELETRIRGLEEALRQREreaaaeleaalGKCEAAEAEAGRLRERVReAEGSGASGGGGGDTTQLR 779
Cdd:COG4913 277 LRAALRLWFAQRRLELLEAELEELRAELARLE-----------AELERLEARLDALREELD-ELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 780 AALEQAREDLRDRDSRLRELEAAsacLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQR 859
Cdd:COG4913 345 REIERLERELEERERRRARLEAL---LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
..
gi 18916882 860 TA 861
Cdd:COG4913 422 RE 423
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
180-285 |
8.78e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 180 AQMCHTDLC-----------RLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALA 248
Cdd:PTZ00322 79 AHMLTVELCqlaasgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18916882 249 GDKLILHLLQEAAQRP------SPPSALTEDDSGEASSQNSMS 285
Cdd:PTZ00322 159 GFREVVQLLSRHSQCHfelganAKPDSFTGKPPSLEDSPISSH 201
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
106-134 |
1.17e-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: 37.18 E-value: 1.17e-03
10 20
....*....|....*....|....*....
gi 18916882 106 GYNALHLAAKYGHPQCLKQLLQASCVVDV 134
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
122-261 |
1.18e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 122 LKQLLQASCVVDVVD-SSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAAND 200
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18916882 201 QDLQGRTALMLACEGA-SPETVEVLLQGGAQPGITDA-LGQDAAHYGALAGDKLILhLLQEAA 261
Cdd:PHA02878 230 RDKCGNTPLHISVGYCkDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKL-LLEYGA 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
337-507 |
1.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 337 HKEQRQQESPEASSLHILERQVQELQQLLVERQEEKES---LGREVESLQSRLSLLENERENTSYDVTTLQDEEGELPDL 413
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 414 PGAEvllsrqlspSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKD--ETQMEVEALAEVIPLALYDSLR---AEFD 488
Cdd:COG4717 132 QELE---------ALEAELAELPERLEELEERLEELRELEEELEELEAElaELQEELEELLEQLSLATEEELQdlaEELE 202
|
170
....*....|....*....
gi 18916882 489 QLRRQHAEALQALRQQETR 507
Cdd:COG4717 203 ELQQRLAELEEELEEAQEE 221
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
132-179 |
1.53e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 18916882 132 VDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIA 179
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
80-264 |
1.60e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 41.90 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 80 AAMRGAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLC 159
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 160 SFKAHLNpqD---RSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDA 236
Cdd:PHA02875 89 DLGKFAD--DvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180
....*....|....*....|....*...
gi 18916882 237 LGQDAAHYGALAGDKLILHLLQEAAQRP 264
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
713-863 |
1.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 713 QVELETRIRGLEEALRQREREAAAELEAALG-KCEAAEAEAGRLRERVREAEGsgasgggggDTTQLRAALEQAREDLRD 791
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRA---------ELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18916882 792 RDSRLRELEAASACLDEARASRLlaEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAA 863
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
310-854 |
2.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 310 DRDAYEEIVRLRQERGRLLQKIRGLEQHKEQRQQESPEASS-----------LHILERQVQELQQLLVERQEEKESLGRE 378
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleeheerreeLETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 379 VESLQSRLSLLENERENT--SYDVTTLQDE--EGELPDLPGAEVLLSRQLS---PSAQEHLA---SLQEQVAVLTRQNQE 448
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaEAGLDDADAEavEARREELEDRDEELRDRLEecrVAAQAHNEeaeSLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 449 LMEKVQILENfEKDETQMEVEALAEVIplalyDSLRAEFDQLRRQHAEALQAL-RQQETREVPREEGAACGESEVAGATA 527
Cdd:PRK02224 361 LREEAAELES-ELEEAREAVEDRREEI-----EELEEEIEELRERFGDAPVDLgNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 528 TKNGPTHMELNGSVAPETKVNGAETIDEEAAGDETMEARTMEAEATGAKATGAEATGAKVTETKPTGAEVREMETtEEEA 607
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 608 NMETKPTGAQATDTETTGVEAMGVEATKTKAEEAEMQAygvgagqaeppvtgttnmEATGSRATGMEAtgvsatgvenpg 687
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEA------------------EAEEKREAAAEA------------ 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 688 veatvpgisagpilHPGAAEASEKLQvELETRIRGLEEALRQREREAAAELEAalgkcEAAEAEAGRLRERVReaegsga 767
Cdd:PRK02224 564 --------------EEEAEEAREEVA-ELNSKLAELKERIESLERIRTLLAAI-----ADAEDEIERLREKRE------- 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 768 sgggggdttQLRAALEQAREDLRDRDSRLRELEAA--SACLDEARASRLLAEEEARGLRAELAQREEARLE-QSR----- 839
Cdd:PRK02224 617 ---------ALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDlQAEigave 687
|
570
....*....|....*....
gi 18916882 840 ----ELEVLREQLATARAT 854
Cdd:PRK02224 688 neleELEELRERREALENR 706
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
321-862 |
2.43e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 321 RQERGRLLQKIRGLEQHKEQRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENtsydv 400
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN----- 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 401 ttlqdEEGELPDLPGAEVLLSRQLSPSAQEhlaslqeqvavlTRQNQEL--MEKVQILENFEKDETQMEVEAL---AEVI 475
Cdd:PTZ00121 1252 -----EEIRKFEEARMAHFARRQAAIKAEE------------ARKADELkkAEEKKKADEAKKAEEKKKADEAkkkAEEA 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 476 PLAlyDSLRAEFDQLRRQhAEALQalRQQETREVPREEGAACGESEVAGATATKNGPTHMELNGSVApETKVNGAETIDE 555
Cdd:PTZ00121 1315 KKA--DEAKKKAEEAKKK-ADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAE 1388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 556 EAAGDETMEARTMEAEATGAKATGAEATGAKVTETKPTGAEVREMETTEEEANMETKptgaqATDTETTGVEAMGVEATK 635
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKAEEAK 1463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 636 TKAEEAEMqaygvgAGQAEPPVTGTTNMEATGSRATGMEATGVSATGVENPGVEATvpgisagpilhpGAAEASEKLQVE 715
Cdd:PTZ00121 1464 KKAEEAKK------ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD------------EAKKAEEAKKAD 1525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 716 letRIRGLEEALRQRereaaaeleaalgkcEAAEAEAGRLRERVREAEGSGASGGgggdttqlRAALEQAREDLRDRDSR 795
Cdd:PTZ00121 1526 ---EAKKAEEAKKAD---------------EAKKAEEKKKADELKKAEELKKAEE--------KKKAEEAKKAEEDKNMA 1579
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18916882 796 LRELEAASAcLDEARASRL--LAEEEARGLRAELAQREEARL--EQSRELEVLREQLATARATGEQQRTAA 862
Cdd:PTZ00121 1580 LRKAEEAKK-AEEARIEEVmkLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
191-244 |
2.55e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18916882 191 LLQQG-AAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHY 244
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
106-136 |
2.83e-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: 2.83e-03
10 20 30
....*....|....*....|....*....|..
gi 18916882 106 GYNALHLAA-KYGHPQCLKQLLQASCVVDVVD 136
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-475 |
3.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 311 RDAYEEIVRLRQERGRLLQKIRGLEQHKEQRQQESPEASSLHILERQVQELQQLlverQEEKESLGREVESLQSRLSL-- 388
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL----EAELAELPERLEELEERLEElr 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 389 -LENERENTSYDVTTLQDEEGELPDLPGAEVLLSRQlspSAQEHLASLQEQVAVLTRQNQELMEKVQILEN-FEKDETQM 466
Cdd:COG4717 160 eLEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEAQEELEELEEeLEQLENEL 236
|
....*....
gi 18916882 467 EVEALAEVI 475
Cdd:COG4717 237 EAAALEERL 245
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
81-257 |
3.22e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 40.72 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 81 AMR-GAASCLEVMIAHGSNVMSTDGAGYNALHLAAKYGHPQCLKQLLqascvVDVVDSSGWTA--LHHAAAGGCLSCSev 157
Cdd:PHA02874 42 AIRsGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNGVDTSILPIpcIEKDMIKTILDCG-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 158 lcsfkAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDAL 237
Cdd:PHA02874 115 -----IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
|
170 180
....*....|....*....|
gi 18916882 238 GQDAAHYGALAGDKLILHLL 257
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLL 209
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
327-467 |
3.53e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 327 LLQKIRGLEQHKEQRQQESPEASSLhilERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSYDVTTLQDE 406
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNL---ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18916882 407 EGELPDLPGAEVLLSRQLSPSAQehlaSLQEQVAVLTRQ-----------NQELMEKVQILENFEKDETQME 467
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRE----SLETQLKVLSRSinkikqnleqkQKELKSKEKELKKLNEEKKELE 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-473 |
3.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 311 RDAYEEIVRLRQERGRLLQKIRGLEQhKEQRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLE 390
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 391 NERENTSYDVTTLQDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENfEKDETQMEVEA 470
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEQ 231
|
...
gi 18916882 471 LAE 473
Cdd:COG4717 232 LEN 234
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
172-202 |
5.48e-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: 35.34 E-value: 5.48e-03
10 20 30
....*....|....*....|....*....|..
gi 18916882 172 GATPLIIAAQMC-HTDLCRLLLQQGAAANDQD 202
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-504 |
6.55e-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: 40.43 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRLLQKIRGLEQHKEQRQQESPEASSLHI-LERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENER 393
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 394 ENTSYDVTTLQDEegelpdlpgAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENF-EKDETQMEVEALA 472
Cdd:TIGR02168 403 ERLEARLERLEDR---------RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeEALEELREELEEA 473
|
170 180 190
....*....|....*....|....*....|..
gi 18916882 473 EviplALYDSLRAEFDQLrRQHAEALQALRQQ 504
Cdd:TIGR02168 474 E----QALDAAERELAQL-QARLDSLERLQEN 500
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
315-394 |
6.78e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 315 EEIVRLRQERGRllQKIRGLEQHKEQRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERE 394
Cdd:pfam17380 460 QQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
165-212 |
7.05e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.40 E-value: 7.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 18916882 165 LNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLA 212
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-508 |
7.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 311 RDAYEEIVRLRQERGRLLQKIRGLEqhKEQRQQESPEASSLHILERQVQELQQLLVERQEEKESLG---REVESLQSRLS 387
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELE--REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 388 LLENERENTSYDVTTLQDEEGELPdlpgAEVLLSRQLSPSAQEHLASLQEQV----AVLTRQNQELMEKVQILENFEKDE 463
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLS----EELADLNAAIAGIEAKINELEEEKedkaLEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18916882 464 TQMEVEalaeviplalYDSLRAEFDQLRRQHAEALQALRQQETRE 508
Cdd:TIGR02169 472 YDLKEE----------YDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-515 |
7.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 355 ERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENEREN---------TSYDVTTLQDEEGELpdlpgaEVLLSRQLS 425
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAEL------EAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 426 PS-----AQEHLASLQEQVAVLTRQNQELMEKVQILEN------FEKDETQMEVEALAEVIPLALYDSLRAEFDQL---- 490
Cdd:COG4913 683 SSddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKeleqaeEELDELQDRLEAAEDLARLELRALLEERFAAAlgda 762
|
170 180
....*....|....*....|....*.
gi 18916882 491 -RRQHAEALQALRQQETREVPREEGA 515
Cdd:COG4913 763 vERELRENLEERIDALRARLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
705-851 |
9.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18916882 705 AAEASEKLQVELETRIRGLEEALRQREREAAAELEAalgKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQ--LRAAL 782
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALGLPLPASAeeFAALR 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18916882 783 EQAREDLRDRDSRLRELEAAsacLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATA 851
Cdd:COG4913 387 AEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| |
