|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
45-401 |
1.63e-73 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 238.67 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 45 QEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRL 124
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 125 WEENDDLKPRLDKKTKEATVAENNarlyenrynevngkynqsladrkkfedqakelalenerlrrqLDDLRKQLEAETLA 204
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAEND------------------------------------------LVGLRKDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 205 RVDLENQNQSLREELAFKDQVHTQELTETRSRRQIE--ISEIDGrlSRQYEakLQQSLQELRDQYEGQMRINREEIELLY 282
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTqvNVEMDA--ARKLD--LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 283 DNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQR 362
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 442623692 363 MRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGEERR 401
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
474-574 |
6.22e-15 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 70.91 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 474 AAAKGDLEIIEADVEG-----RFIKLHNKGTEEINLTGWQLTRIAGDeelAFKFSRGSKVLGGASVTIWS----VDAGTA 544
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG---TYTFPNGTTLAPGQTVVVWTgsgtNSATAG 77
|
90 100 110
....*....|....*....|....*....|
gi 442623692 545 HDPPNNLVMKkkwpvANSMRSVLANADKEV 574
Cdd:pfam00932 78 YWGPSNAVWN-----NGGDAVALYDANGEL 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-333 |
1.72e-14 |
|
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: 77.40 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 47 KEELQHLndRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAV-------------YEKELAAARKLLDETAKE 113
Cdd:TIGR02168 219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekleelrlevseLEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 114 KAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDD 193
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 194 LRKQLEAETLARVDLENQNQSLREELAFKDQvHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRI 273
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEA-RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 274 NREEIELLYdnEIQNLKAAANRAAQGsalATEEVRLMRTKIDGLNAKLQNLEDTNAGLNA 333
Cdd:TIGR02168 456 LERLEEALE--ELREELEEAEQALDA---AERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-373 |
1.75e-13 |
|
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: 73.94 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 40 RTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNL------KAVYEKELAAARKLLDETAKE 113
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 114 KAKLEIDIKRLWEENDDLKPRLDKKtkeatvaennarlyENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDD 193
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDEL--------------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 194 LRKQLEAETLARVDLENQNQSLREELAFKDQ---VHTQELTETRSRRQIEISEIDGRLSRQYEakLQQSLQELRDQyEGQ 270
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNeraSLEEALALLRSELEELSEELRELESKRSE--LRRELEELREK-LAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 271 MRINREEIELLYDNEIQNLKAAANRAAQG----SALATEEVRLMRTKIDGLNAKLQNLEDTNagLNArIRELENL----- 341
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEYSLTLEEaealENKIEDDEEEARRRLKRLENKIKELGPVN--LAA-IEEYEELkeryd 1003
|
330 340 350
....*....|....*....|....*....|...
gi 442623692 342 -LDTERQRHNQYIASLEAELQRMRDEMAHQLQE 373
Cdd:TIGR02168 1004 fLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-372 |
1.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 97 EKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQ 176
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 177 AKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAfkdqVHTQELTETRSRRQIEISEIDGRLSRQYEAKL 256
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 257 QQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIR 336
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270
....*....|....*....|....*....|....*.
gi 442623692 337 ELENLLDTERQRHNQyIASLEAELQRMRDEMAHQLQ 372
Cdd:COG1196 474 LLEAALAELLEELAE-AAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-362 |
3.22e-12 |
|
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: 70.10 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 107 LDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENER 186
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 187 LRRQLDDLRKQLEAETLA----RVDLENQNQSLREELAFKDQVHTQELTETRSRRQIEISEIDGRLSR-----QYEAKLQ 257
Cdd:TIGR02169 756 VKSELKELEARIEELEEDlhklEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlekEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 258 QSLQELRDQYEGQMRINREEIELLyDNEIQNLKAAANRAAqgSALATEEVRL--MRTKIDGLNAKLQNLEDtnaglnaRI 335
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENL-NGKKEELEEELEELE--AALRDLESRLgdLKKERDELEAQLRELER-------KI 905
|
250 260
....*....|....*....|....*..
gi 442623692 336 RELENLLDTERQRHNQYIASLEAELQR 362
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-315 |
3.44e-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: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 40 RTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVN------RETSNLKAVYEKELAAARKLLDETAKE 113
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 114 KAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDD 193
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 194 LRKQLEAETLARVDLENQNQSLREELAfKDQVHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRI 273
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 442623692 274 NREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKID 315
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-373 |
5.86e-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: 62.77 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 66 NLENENSRLTQELNLAQDTVnRETsnlkavyEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVA 145
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKI-AEL-------EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 146 ENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAetlarvdLENQNQSLREEL-AFKDQ 224
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-------LREALDELRAELtLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 225 VHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEgQMRINREEIEL---LYDNEIQNLKAAANRAAQGSA 301
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEELESeleALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442623692 302 LATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQR-HNQYIASLE--AELQRMRDEMAHQLQE 373
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEeaEALENKIEDDEEEARR 972
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-344 |
3.70e-09 |
|
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: 59.65 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 66 NLENENSRLTQELNLAQD---TVNRET-SNLKAVY--EKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKT 139
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNeieKLKKENqSYKQEIKnlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 140 KEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREEL 219
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 220 A-FKDQVhtQELTETRSRRQIEISEIDGRLSrQYEAKLQQSLQEL-RDQYEGQMRINREEIELLyDNEIQNLKA------ 291
Cdd:TIGR04523 513 KdLTKKI--SSLKEKIEKLESEKKEKESKIS-DLEDELNKDDFELkKENLEKEIDEKNKEIEEL-KQTQKSLKKkqeekq 588
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 442623692 292 --AANRAAQGSALaTEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDT 344
Cdd:TIGR04523 589 elIDQKEKEKKDL-IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-390 |
8.30e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 109 ETAKEKAKL--EIDIKRLWE---ENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALE 183
Cdd:COG1196 210 EKAERYRELkeELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 184 NERLRRQLDDLRKQLEAETLARVDLENQNQSLREE---LAFKDQVHTQELTETRSRRQIEISEIdgrlsRQYEAKLQQSL 260
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEEL-----EEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 261 QELRDQyEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELEN 340
Cdd:COG1196 365 EALLEA-EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 442623692 341 LLDTERQRhnqyiASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAA 390
Cdd:COG1196 444 LEEAAEEE-----AELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-399 |
1.50e-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: 58.14 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 146 ENNARLYENRyNEVNGKYNqsladrkKFEDQAkELALENERLRRQLDDLR--------KQLEAETLARVDLENQNQSLRE 217
Cdd:TIGR02168 186 ENLDRLEDIL-NELERQLK-------SLERQA-EKAERYKELKAELRELElallvlrlEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 218 ELAFKDQVHTQELTETRSRR---QIEISEIDGRLSRQYE--AKLQQSLQELRDQYEgQMRINREEIELlydnEIQNLKAA 292
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVselEEEIEELQKELYALANeiSRLEQQKQILRERLA-NLERQLEELEA----QLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 293 ANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQR---HNQYIASLEAELQRMRDEMAH 369
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLER 411
|
250 260 270
....*....|....*....|....*....|
gi 442623692 370 QLQEYQGLMDIKVSLDLEIAAYDKLLCGEE 399
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-390 |
2.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 104 RKLLDETA--------KEKAKLEID-----IKRLweeND---DLKPRLDKKTKEATVAEnnarlyenRYNEVngkynqsl 167
Cdd:COG1196 158 RAIIEEAAgiskykerKEEAERKLEateenLERL---EDilgELERQLEPLERQAEKAE--------RYREL-------- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 168 adrkkfedQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELafkdQVHTQELTETRSRRQIEISEIDGR 247
Cdd:COG1196 219 --------KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 248 LSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDT 327
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442623692 328 NAGLNARIRELENLLDTERQRH----------NQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAA 390
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELlealraaaelAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-277 |
3.42e-08 |
|
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: 55.93 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 32 ATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAqdtvnretsnlkavyEKELAAARKLLDETA 111
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---------------ERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 112 KEKAKLEIDIKRLWEENDDLKPRLDKKTKEatVAENNARLYEN-RYNEVNGKYNQSlaDRKKFEDQAKELALENERLRRQ 190
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEE--LAELLRALYRLgRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 191 LDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHtQELTETRSRRQIEISEIDGRLS--RQYEAKLQQSLQELRDQYE 268
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAelAAELAELQQEAEELEALIA 230
|
....*....
gi 442623692 269 GQMRINREE 277
Cdd:COG4942 231 RLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
43-375 |
8.06e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 43 RQQEKEELQHLNDRLA---CYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEI 119
Cdd:COG4717 134 LEALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 120 DIKRLWEENDDLKPRLDKKTKEATVAENNARLYENR----------------------------------------YNEV 159
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallFLLL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 160 NGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQvHTQELTETRSRRQI 239
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-LEEELQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 240 E-------ISEIDGRLSRQYEAKLQQSLQELRDQYEGQMR-INREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMR 311
Cdd:COG4717 373 AallaeagVEDEEELRAALEQAEEYQELKEELEELEEQLEeLLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442623692 312 TKIDGLNAKLQNLEDTNAgLNARIRELENLLDTERQRHNQYiASLEAELQRMRDEMAHQLQEYQ 375
Cdd:COG4717 453 EELAELEAELEQLEEDGE-LAELLQELEELKAELRELAEEW-AALKLALELLEEAREEYREERL 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
43-378 |
9.09e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 43 RQQEkEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYE------KELAAARKLLDETAKEKAK 116
Cdd:pfam01576 492 RQLE-DERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgkkrlqRELEALTQQLEEKAAAYDK 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 117 LEIDIKRLWEENDDLKPRLDKKTKEATVAENNARlyenrynevngKYNQSLADRKKFEDQAKELALENERLRRQLD---- 192
Cdd:pfam01576 571 LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQK-----------KFDQMLAEEKAISARYAEERDRAEAEAREKEtral 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 193 DLRKQLEAETLARVDLENQNQSLREEL----AFKDQVHTQELTETRSRRQIEiseidgrlsrQYEAKLQQSLQELRDQYE 268
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMedlvSSKDDVGKNVHELERSKRALE----------QQVEEMKTQLEELEDELQ 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 269 GQmrinrEEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMrtkidglnaklqnledtnagLNARIRELENLLDTERQR 348
Cdd:pfam01576 710 AT-----EDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQ--------------------LVKQVRELEAELEDERKQ 764
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 442623692 349 HNQYIAS---LEAELQRM----------RDEMAHQLQEYQGLM 378
Cdd:pfam01576 765 RAQAVAAkkkLELDLKELeaqidaankgREEAVKQLKKLQAQM 807
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
67-343 |
1.03e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 67 LENENSRLTQELNLAQDTVNRETSNLkAVYEKELAAARKLLDETAKEKAKLEIDIKR---LWEENDDLKPRLDKKTKEA- 142
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISEFTSNL-AEEEEKAKSLSKLKNKHEAMISDLEERLKKeekGRQELEKAKRKLEGESTDLq 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 143 -TVAENNARLYENRY-NEVNGKYNQSLADRKKFEDQAKELALENER-LRRQLDDLRKQLEAETLARVDLENQNQSLREEL 219
Cdd:pfam01576 222 eQIAELQAQIAELRAqLAKKEEELQAALARLEEETAQKNNALKKIReLEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 220 -AFK-------DQVHTQEltETRSRRQIEISEIDGRL---SRQYEAKLQ-------QSLQELRDQYEGQMR--INREEIE 279
Cdd:pfam01576 302 eALKteledtlDTTAAQQ--ELRSKREQEVTELKKALeeeTRSHEAQLQemrqkhtQALEELTEQLEQAKRnkANLEKAK 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442623692 280 LLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLD 343
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELE 443
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
41-406 |
1.58e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 41 TSRQQEKEELQHLNDRLA------CYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYE--KELAAARKLLDETAK 112
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQqtqqshAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 113 EKAKLEIDIKRlWEENDDLKPRLDKKTKE----ATVAENNARLYENRYNEvngkyNQSLADRKKFEDQAKELALENERLR 188
Cdd:TIGR00618 299 IKAVTQIEQQA-QRIHTELQSKMRSRAKLlmkrAAHVKQQSSIEEQRRLL-----QTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 189 RQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQElTETRSRR-----------QIEISEIDGRLSRQYEAKLQ 257
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATID-TRTSAFRdlqgqlahakkQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 258 QSL-QELRDQYEGQMRInREEIELLYDNE---------------IQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKL 321
Cdd:TIGR00618 452 QCEkLEKIHLQESAQSL-KEREQQLQTKEqihlqetrkkavvlaRLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 322 QNLEDTNAGLNARIRELENLLDTERQRhnqyIASLEAELQRMRDE---MAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGE 398
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQ----RASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
....*...
gi 442623692 399 ERRLNIES 406
Cdd:TIGR00618 607 EDMLACEQ 614
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-373 |
4.64e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 104 RKLLDETA--------KEKAKLEID-----IKRLWEENDDLKPRLDKKTKEATVAEnnarlyenRYNEVNgkynqsladR 170
Cdd:TIGR02169 156 RKIIDEIAgvaefdrkKEKALEELEeveenIERLDLIIDEKRQQLERLRREREKAE--------RYQALL---------K 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 171 KKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQ------ELTETRSRR-QIEISE 243
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRvKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 244 IDGRLSrQYEAKLQQSLQELRDQyEGQMRINREEIElLYDNEIQNLKaaanraaqgsalatEEVRLMRTKIDGLNAKLQN 323
Cdd:TIGR02169 299 LEAEIA-SLERSIAEKERELEDA-EERLAKLEAEID-KLLAEIEELE--------------REIEEERKRRDKLTEEYAE 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442623692 324 LEDTNAGLNARIRELENLLDTERQRHNQYIASLEA------ELQRMRDEMAHQLQE 373
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinELKRELDRLQEELQR 417
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
107-374 |
1.25e-06 |
|
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: 51.76 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 107 LDETAKEKAKLEIDIKRLWEENDDLKPRLDKK--TKEATVAENNARLyenrynevNGKYNQSLADRKKFEDQAKelALEN 184
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLlrTLDDQWKEKRDEL--------NGELSAADAAVAKDRSELE--ALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 185 ERLRRQLDDLRK---QLEAETLARVDLENQNQSLrEELAFKDQVHTQELTETRSRRQIE----ISEIDGRLSRQYEAK-- 255
Cdd:pfam12128 330 QHGAFLDADIETaaaDQEQLPSWQSELENLEERL-KALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARdr 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 256 --------LQQSLQELRDQYEGQMRINREEiELLYDNEIQNLKAAANRAAQGSALAT------EEVRLMRTKIDGLNAKL 321
Cdd:pfam12128 409 qlavaeddLQALESELREQLEAGKLEFNEE-EYRLKSRLGELKLRLNQATATPELLLqlenfdERIERAREEQEAANAEV 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 442623692 322 QNLEDTNAGLNARIRELENLLDTERQRHNQyIASLEAELQRMRDEMAHQLQEY 374
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEE-RQSALDELELQLFPQAGTLLHF 539
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
174-395 |
7.65e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 174 EDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLreELAFKDQVHTQELTETRSRRQieiseidgrlsrQYE 253
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLA------------EAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 254 AKLQQsLQELRDQYEGQMRINREEI-ELLYDNEIQNLKAaaNRAAQGSALATEEVRLMRT--KIDGLNAKLQNLEdtnAG 330
Cdd:COG3206 233 AELAE-AEARLAALRAQLGSGPDALpELLQSPVIQQLRA--QLAELEAELAELSARYTPNhpDVIALRAQIAALR---AQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442623692 331 LNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLL 395
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
77-264 |
7.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 77 ELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARL--YEN 154
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELaeLPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 155 RYNEVNgkynQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARV-DLENQNQSLREELAFkdqvHTQELTET 233
Cdd:COG4717 147 RLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAE----LEEELEEA 218
|
170 180 190
....*....|....*....|....*....|.
gi 442623692 234 RSRRQIEISEIDGRLSRQYEAKLQQSLQELR 264
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
43-394 |
8.57e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 43 RQQEKEelqhLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVyEKELAAARKLLDETAKEKAKLEIDIK 122
Cdd:TIGR04523 81 EQQIKD----LNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKL-EKQKKENKKNIDKFLTEIKKKEKELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 123 RLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKY---NQSLADRKKFEDQAKELALENERLRRQLDDLRKQLE 199
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 200 AETLARVDLENQNQSLREELAFKDQVHTQELTETrSRRQIEISEIDGRLSrQYEAKLQQ---SLQELRDQYE-GQMRINR 275
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL-SEKQKELEQNNKKIK-ELEKQLNQlksEISDLNNQKEqDWNKELK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 276 EEIELLyDNEIQNLKAAANRAAQgsalateevrlmrtKIDGLNAKLQNLEdtnaglnariRELENLlDTERQRHNQYIAS 355
Cdd:TIGR04523 314 SELKNQ-EKKLEEIQNQISQNNK--------------IISQLNEQISQLK----------KELTNS-ESENSEKQRELEE 367
|
330 340 350
....*....|....*....|....*....|....*....
gi 442623692 356 LEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKL 394
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-368 |
9.09e-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: 48.22 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 175 DQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAfkdqvhtqELTETRSRRQIEISEIDGRLSR--QY 252
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA--------ALARRIRALEQELAALEAELAEleKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 253 EAKLQQSLQELRDQYEGQMRI-----NREEIELLYDNEiqnlkaAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDT 327
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyrlgRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442623692 328 NAGLNARIRELENL----------LDTERQRHNQYIASLEAE---------------------LQRMRDEMA 368
Cdd:COG4942 166 RAELEAERAELEALlaeleeeraaLEALKAERQKLLARLEKElaelaaelaelqqeaeelealIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-374 |
1.59e-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: 48.14 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 65 RNLENENSRLTQELnlaqDTVNRETSNLkavyEKELAAARKLLDETAKEkakleidIKRLWE-ENDDLKPRLDKKTKEAT 143
Cdd:TIGR02169 240 EAIERQLASLEEEL----EKLTEEISEL----EKRLEEIEQLLEELNKK-------IKDLGEeEQLRVKEKIGELEAEIA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 144 VAENNARLYENRynevngkynqsladRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAfkd 223
Cdd:TIGR02169 305 SLERSIAEKERE--------------LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE--- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 224 qvhtqeltetRSRRQIEiseidgrlsrQYEAKLQQSLQELRDQyegqmrinREEIELLyDNEIQNLKAAANRAAQGSALA 303
Cdd:TIGR02169 368 ----------DLRAELE----------EVDKEFAETRDELKDY--------REKLEKL-KREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442623692 304 TEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDT---ERQRHNQYIASLEAELQRMRDEMAHQLQEY 374
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaaDLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
100-340 |
1.61e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 100 LAAARKLLDETAKEKAKLEIDIKRLweenddlKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKE 179
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAEL-------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 180 LALENERLRRQLDDLRKQleaetLARVDLENQNQSLREELAFKdqVHTQELTETRSRRQI--EISEIDGRLSRQYEAKLQ 257
Cdd:COG4942 88 LEKEIAELRAELEAQKEE-----LAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYlkYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 258 QsLQELRDQYEGQmrinREEIELLYDN---EIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNAR 334
Cdd:COG4942 161 E-LAALRAELEAE----RAELEALLAEleeERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*.
gi 442623692 335 IRELEN 340
Cdd:COG4942 236 AAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
46-347 |
2.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 46 EKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYE--KELAAARKLLDETAKEKAKLEIDIKR 123
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 124 LWEENDDLKPRLDKKTKEATVAENNARlyenRYNEVNGK---YNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLE- 199
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVK----ELKELKEKaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKe 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 200 -AETLARV-DLENQNQSLREELAFKDQVHtqELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEgqmRINREE 277
Cdd:PRK03918 333 lEEKEERLeELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 278 IELL-----YDNEIQNLKAAAN--RAAQG-----SALATEEVR--LMRT---KIDGLNAKLQNLEDTNAGLNARIRELEN 340
Cdd:PRK03918 408 SKITarigeLKKEIKELKKAIEelKKAKGkcpvcGRELTEEHRkeLLEEytaELKRIEKELKEIEEKERKLRKELRELEK 487
|
....*..
gi 442623692 341 LLDTERQ 347
Cdd:PRK03918 488 VLKKESE 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-371 |
2.94e-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: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 169 DRKKFEDQAKELaLEN----ERLRRQLDDLRKQLE--------AETLARVDLE-NQNQSLREEL-AFKDQVHTQELTETR 234
Cdd:COG4913 219 EEPDTFEAADAL-VEHfddlERAHEALEDAREQIEllepirelAERYAAARERlAELEYLRAALrLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 235 SRRQIEISEIDGRLSR--QYEAKLQQSLQELRDQYEGQMRINREEIEllydNEIQNLKAAANRAAQGSALATEEVRLMRT 312
Cdd:COG4913 298 EELRAELARLEAELERleARLDALREELDELEAQIRGNGGDRLEQLE----REIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 313 KI----DGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQY----------IASLE-------AELQRMRDEMAHQL 371
Cdd:COG4913 374 PLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrrelreleaeIASLErrksnipARLLALRDALAEAL 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
49-253 |
3.57e-05 |
|
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: 45.69 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 49 ELQHLNDRLAcyidrmrNLENENSRLTQELNLAQDTVNRetsnlkavYEKELAAARKLLDETAKEKAKLEIDIKrlween 128
Cdd:COG1579 11 DLQELDSELD-------RLEHRLKELPAELAELEDELAA--------LEARLEAAKTELEDLEKEIKRLELEIE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 129 dDLKPRLDKKTKEATVAENNaRLYENRYNEVngkynQSLADRKKF-EDQAKELALENERLRRQLDDLRKQLEAetlARVD 207
Cdd:COG1579 70 -EVEARIKKYEEQLGNVRNN-KEYEALQKEI-----ESLKRRISDlEDEILELMERIEELEEELAELEAELAE---LEAE 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442623692 208 LENQNQSLREELAfkdqVHTQELTETRSRRQIEISEIDGRLSRQYE 253
Cdd:COG1579 140 LEEKKAELDEELA----ELEAELEELEAEREELAAKIPPELLALYE 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
97-385 |
5.85e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 97 EKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQ 176
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 177 AKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQvhtqeltetrSRRQIEISEIDGRLSRQYEAKL 256
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ----------ELQALSEAEAEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 257 QQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIR 336
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442623692 337 ELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLD 385
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
153-402 |
6.74e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 153 ENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDD-------LRKQLEAETLARVDLENQNQSLREELAFKDQV 225
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDktaqaeaLERQLAAETEQNRALEEENKALREEAQAAEKA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 226 HT---QELTETRSRRQIEISEiDGRLSRQYE------AKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRA 296
Cdd:pfam19220 155 LQraeGELATARERLALLEQE-NRRLQALSEeqaaelAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 297 AQGSALATEEVRLmRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYI---ASLEAELQRMRDEMAHQLQE 373
Cdd:pfam19220 234 EAVEAHRAERASL-RMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASierDTLERRLAGLEADLERRTQQ 312
|
250 260
....*....|....*....|....*....
gi 442623692 374 YQGLMDIKVSLDLEIAAYDKLLCGEERRL 402
Cdd:pfam19220 313 FQEMQRARAELEERAEMLTKALAAKDAAL 341
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-360 |
7.22e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 107 LDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNevngkYNQSLADRkkfEDQAKELALENER 186
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED-----LEELIAER---RETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 187 LRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQvHTQELTETRSR------RQIEISEIDGRLSRQYEaKLQQsL 260
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS-KLAELKERIESlerirtLLAAIADAEDEIERLRE-KREA-L 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 261 QELRDQYEGQMRINREEI----ELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAK----------LQNLED 326
Cdd:PRK02224 619 AELNDERRERLAEKRERKreleAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaveneleeLEELRE 698
|
250 260 270
....*....|....*....|....*....|....
gi 442623692 327 TNAGLNARIRELENLLDTERQRHNQYiASLEAEL 360
Cdd:PRK02224 699 RREALENRVEALEALYDEAEELESMY-GDLRAEL 731
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
174-373 |
7.64e-05 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 45.73 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 174 EDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVhTQELTETRSRRQIEISEID---GRLSR 250
Cdd:pfam14643 192 EFIASEEIQNPPERKKELEEMLKEQKKLQQKRLELLQKISDLLPPAYSKSKV-EEWWASLEALNEQLDQYHDqcmTKLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 251 QYEAKLQQSLQE---LRDQYEGQMRINREEIELLYDNEIqnLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNL--- 324
Cdd:pfam14643 271 EYEEVWQECLARvqkLKQELLDYKVCSEEEAEALVNEEF--LPLVGKLQRDAEDELEKLDKFLEELAKQTEAQSEDLfkf 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442623692 325 --------EDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQE 373
Cdd:pfam14643 349 freaaqlwDVHQTELAKQELELEKKLEQCRQKHDQENQAKEAALDKKLDQLRQASTE 405
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
63-376 |
8.81e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 63 RMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLD---------ETAKEKAKLEIDIKRLWEENDDLKP 133
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKrirllekreAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 134 RLdKKTKEATVAEnnarlyenrYNEVNGKYNQSLADRK----KFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLE 209
Cdd:pfam05557 90 KK-LNEKESQLAD---------AREVISCLKNELSELRrqiqRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 210 NQNQSLRE------ELAFKDQVHTQELTETRSRRQieiseidgRLSRQyeAKLQQSLQELRDQYEgQMRINREEIELLyD 283
Cdd:pfam05557 160 KQQSSLAEaeqrikELEFEIQSQEQDSEIVKNSKS--------ELARI--PELEKELERLREHNK-HLNENIENKLLL-K 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 284 NEIQNLKAAANRAAQgsalATEEVRLMRTKIDGLNAKLQNLE--DTNAGLNARI-----RELENLLDTE--RQRHNQYIA 354
Cdd:pfam05557 228 EEVEDLKRKLEREEK----YREEAATLELEKEKLEQELQSWVklAQDTGLNLRSpedlsRRIEQLQQREivLKEENSSLT 303
|
330 340
....*....|....*....|..
gi 442623692 355 SLEAELQRMRDEMAHQLQEYQG 376
Cdd:pfam05557 304 SSARQLEKARRELEQELAQYLK 325
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
47-347 |
1.06e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 47 KEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVyEKELAAARKLLDETAKEKAKLEIDIKRLWE 126
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA-QAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 127 ENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQslADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARV 206
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES--LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 207 DLENQNQSLREELAFKDQVHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEI 286
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442623692 287 QNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQ 347
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
39-394 |
1.26e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 39 TRTSRQQEKEELQHLNDRLACyiDRMRNLENENSrlTQELNLAQDTVNRETSNLKAvyekELAAARKLLDETAKEKAKLE 118
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEK--EKLKNIELTAH--CDKLLLENKELTQEASDMTL----ELKKHQEDIINCKKQEERML 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 119 IDIKRLWEENDDLKPRLDKKTKEatvaennarlYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQL 198
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREE----------FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 199 EAETLARVDLENQNQSLREElafkdqvhtqeltETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEI 278
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKK-------------GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 279 ELLYDnEIQNLKAAANRAAQgsaLATEEVRLMRTKIDGLNAKLQ-NLEDTNAGLNARIRELeNLLDTERQRHNQYIASLE 357
Cdd:pfam05483 671 EKLLE-EVEKAKAIADEAVK---LQKEIDKRCQHKIAEMVALMEkHKHQYDKIIEERDSEL-GLYKNKEQEQSSAKAALE 745
|
330 340 350
....*....|....*....|....*....|....*..
gi 442623692 358 AELQRMRDEmahqlqeyqgLMDIKVSLDLEIAAYDKL 394
Cdd:pfam05483 746 IELSNIKAE----------LLSLKKQLEIEKEEKEKL 772
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
64-365 |
1.71e-04 |
|
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: 44.94 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 64 MRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKeLAAARKLL-------DETAKEKAkleidikrlweenDDLKPRLD 136
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQ-LQLLNKLLpqanllaDETLADRL-------------EELREELD 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 137 kktkEATVAENNARLYENRYNEVNGKYNQSLADRKKFEdqakELALENERLRRQLDDLRKQLEA--ETLAR--------- 205
Cdd:COG3096 904 ----AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLKQQIFAlsEVVQRrphfsyeda 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 206 VDLENQNQSLREELafKDQVHTQELTETRSRRQIEisEIDGRLSrQYeaklQQSLQELRDQYEGQMRINREEIELLYDNE 285
Cdd:COG3096 976 VGLLGENSDLNEKL--RARLEQAEEARREAREQLR--QAQAQYS-QY----NQVLASLKSSRDAKQQTLQELEQELEELG 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 286 IQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRD 365
Cdd:COG3096 1047 VQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARD 1126
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
82-217 |
2.00e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 82 QDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKktKEATVAEnnarlYENRYNEVNG 161
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEE--KDERIER-----LERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442623692 162 KYNQSLADRKKFedqaKELALENERLRRQLDDLRKQLEaetlarvDLENQNQSLRE 217
Cdd:COG2433 456 EERREIRKDREI----SRLDREIERLERELEEERERIE-------ELKRKLERLKE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-389 |
2.61e-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: 44.28 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 40 RTSRQQEKEELQHLNDRLACYIDRMRNLE----------NENSRLTQELNLAQDTVNREtsnlkAVYEKELAAA-----R 104
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEgfsegvkallKNQSGLSGILGVLSELISVD-----EGYEAAIEAAlggrlQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 105 KLLDETAkEKAKLEIDI-------KRLWEENDDLKPRLDKKTKEATV--------------------------------- 144
Cdd:TIGR02168 549 AVVVENL-NAAKKAIAFlkqnelgRVTFLPLDSIKGTEIQGNDREILkniegflgvakdlvkfdpklrkalsyllggvlv 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 145 ------AENNARLYENRYNEV----------------NGKYNQSL-----------ADRKKFEDQAKELALENERLRRQL 191
Cdd:TIGR02168 628 vddldnALELAKKLRPGYRIVtldgdlvrpggvitggSAKTNSSIlerrreieeleEKIEELEEKIAELEKALAELRKEL 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 192 DDLRKQLEAETLARVDLENQNQSLREELAFKDQVHtQELTETRSRRQIEISEIDGRLsRQYEAKLQ-------------Q 258
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLSKELTELEAEI-EELEERLEeaeeelaeaeaeiE 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 259 SLQELRDQYEGQMRINREEIELLyDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIREL 338
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442623692 339 ENLLDT----------ERQRHNQYIASLEAELQRMRDEM------AHQL-QEYQGLMDIKVSLDLEIA 389
Cdd:TIGR02168 865 EELIEEleseleallnERASLEEALALLRSELEELSEELreleskRSELrRELEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
241-395 |
3.34e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 241 ISEIDGR---LSRQYEAKLQ-QSLQELRDQYEGQMRINR-----EEIELLyDNEIQNLKAAANRAAQGSALATEEVRLMR 311
Cdd:COG1196 195 LGELERQlepLERQAEKAERyRELKEELKELEAELLLLKlreleAELEEL-EAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 312 TKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRhnqyIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAY 391
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
....
gi 442623692 392 DKLL 395
Cdd:COG1196 350 EEEL 353
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
62-367 |
3.35e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 62 DRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKE 141
Cdd:pfam10174 3 AQLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 142 ATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEaETLARVDLENQNQSLREELAF 221
Cdd:pfam10174 83 LRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLE-EMELRIETQKQTLGARDESIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 222 KdqvhTQELTETRSRRQIEISEIDGRLSRQYEAKLQ-QSLQELRDQYEGQMRINREEIEllYDNEIQnlkaaaNRAAQGS 300
Cdd:pfam10174 162 K----LLEMLQSKGLPKKSGEEDWERTRRIAEAEMQlGHLEVLLDQKEKENIHLREELH--RRNQLQ------PDPAKTK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442623692 301 ALATeEVRLMRTKIDGLNAKLQNLED------TNAGLNARIRElENLLDTERQR-HNQY----IASLEAELQRMRDEM 367
Cdd:pfam10174 230 ALQT-VIEMKDTKISSLERNIRDLEDevqmlkTNGLLHTEDRE-EEIKQMEVYKsHSKFmknkIDQLKQELSKKESEL 305
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-338 |
3.52e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVnRETSNLKAVYEKELAAARKLLDETA--KEKAKLEIDI 121
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKLKELEKRLEelEERHELYEEA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 122 KRLWEENDDLKPRLDKKTKEATVAEnnARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLR----------RQL 191
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgREL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 192 DDlrkQLEAETLARVDLENQNqsLREELafkdqvhtQELTETRSRRQIEISEIDGRLSRQYE-AKLQQSLQELRDQYEGQ 270
Cdd:PRK03918 446 TE---EHRKELLEEYTAELKR--IEKEL--------KEIEEKERKLRKELRELEKVLKKESElIKLKELAEQLKELEEKL 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442623692 271 MRINREEIELLYDnEIQNLKAAANR-AAQGSALATE--EVRLMRTKIDGLNAKLQNLEDTNAGLNARIREL 338
Cdd:PRK03918 513 KKYNLEELEKKAE-EYEKLKEKLIKlKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-362 |
4.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 131 LKPRLDKKTKEATVAENNARLYENRYNEVN--GKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDL 208
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 209 ENQNQslreelafkdqvhTQELTETRSRRQIEISEIDGRLSRQYEA--KLQQSLQELRDQYEGQMRINREEIEllydNEI 286
Cdd:COG3206 260 LQSPV-------------IQQLRAQLAELEAELAELSARYTPNHPDviALRAQIAALRAQLQQEAQRILASLE----AEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442623692 287 QNLKAaanraaqgsalateEVRLMRTKIDGLNAKLQNLedtnAGLNARIRELENLLDTERQRHNQYIASL-EAELQR 362
Cdd:COG3206 323 EALQA--------------REASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLeEARLAE 381
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-348 |
4.24e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 45 QEKEElQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKelaaaRKLLDETAKEKAKLEIDIKRL 124
Cdd:PRK02224 197 EEKEE-KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-----REELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 125 WEENDDLKPRLD--KKTKEATVAENNARLYENRYNEvngkynqslADRKKFEDQAKELALENERLRRQLDDLR------- 195
Cdd:PRK02224 271 EREREELAEEVRdlRERLEELEEERDDLLAEAGLDD---------ADAEAVEARREELEDRDEELRDRLEECRvaaqahn 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 196 KQLEAETLARVDLENQNQSLREElAFKDQVHTQELTETRSRRQIEISEIDGRLSRQYEA---------KLQQSLQELRDQ 266
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREE-AAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 267 YEgqmRINREEIELLYDneiqnLKAAANRAAQGSALA-----------------TEEVRLMRTKIDGLNAKLQNLEDTNA 329
Cdd:PRK02224 421 RD---ELREREAELEAT-----LRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVE 492
|
330
....*....|....*....
gi 442623692 330 GLNARIRELENLLDTERQR 348
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRI 511
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
25-375 |
5.46e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 25 STSSRVGATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQEL-NLAQDTVNRETSNLkavyekelaaa 103
Cdd:PLN02939 77 NTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLeDLVGMIQNAEKNIL----------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 104 rkLLDEtAKEKAkLEiDIKRLWEENDDLKPRLDkkTKEATVAENNARLYENRYNEVNGKYNQSLadrkkFEDQAKELALE 183
Cdd:PLN02939 146 --LLNQ-ARLQA-LE-DLEKILTEKEALQGKIN--ILEMRLSETDARIKLAAQEKIHVEILEEQ-----LEKLRNELLIR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 184 NERLRRQLDDLRKQLEAETLARVDLENQNQSLREELafkdqVHTQELTETRSRRQIEISEIDGRLsRQYEAKLQQSLQEL 263
Cdd:PLN02939 214 GATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL-----IEVAETEERVFKLEKERSLLDASL-RELESKFIVAQEDV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 264 RDQYEGQMRINREEIELLYDNeiqnLKAAANRAAQgSALATEEVRLMRTKIDGLNAklqNLEDTNAGlnariRELENLLD 343
Cdd:PLN02939 288 SKLSPLQYDCWWEKVENLQDL----LDRATNQVEK-AALVLDQNQDLRDKVDKLEA---SLKEANVS-----KFSSYKVE 354
|
330 340 350
....*....|....*....|....*....|..
gi 442623692 344 TERQRhnqyIASLEAELQRMRDEMAHQLQEYQ 375
Cdd:PLN02939 355 LLQQK----LKLLEERLQASDHEIHSYIQLYQ 382
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
43-367 |
5.64e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 43 RQQEKEELQHLNDRLACYIDRMRNLENENSRLTQ----ELNLAQDTVNrETSNLKAVYEKELAAARKLLDETAK-EKAKL 117
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimpEEESAKVCLT-DVTIMERFQMELKDVERKIAQQAAKlQGSDL 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 118 EIDIKRLWEENDDLKPRLDKKTKEAtvaENNARLYENRYNEVN---GKYNQ----------SLADRKKFEDQAKELALEN 184
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKI---ELNRKLIQDQQEQIQhlkSKTNElkseklqigtNLQRRQQFEEQLVELSTEV 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 185 ERLRRQLDDLRKQLEAETLARVDLENQNQSLreelafkdqVHTQEltETRSRRQIEISEIDGRLSRQ--YEAKLQQSLQE 262
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEEL---------ISSKE--TSNKKAQDKVNDIKEKVKNIhgYMKDIENKIQD 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 263 LRDQYEGQMrinreeiellyDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLED--TNAGLNARIRELEN 340
Cdd:TIGR00606 967 GKDDYLKQK-----------ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDnlTLRKRENELKEVEE 1035
|
330 340
....*....|....*....|....*...
gi 442623692 341 LLDTERQRHNQ-YIASLEAELQRMRDEM 367
Cdd:TIGR00606 1036 ELKQHLKEMGQmQVLQMKQEHQKLEENI 1063
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-217 |
5.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYIDRMRNLENENSRLTQ------ELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKL 117
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPF 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 118 ----------EIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSlaDRKKFEDQAKELALENERL 187
Cdd:PRK03918 601 yneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGL 678
|
170 180 190
....*....|....*....|....*....|
gi 442623692 188 RRQLDDLRKQLEAETLARVDLENQNQSLRE 217
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-368 |
5.72e-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: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 100 LAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLD--KKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQA 177
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 178 KELalenERLRRQLDDLRKQLEAETLARVDLENQNQSLREELafkDQVHTQELTETRSRRQIEISEIDGRLSrqyEAKLQ 257
Cdd:COG4913 692 EQL----EELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFA---AALGD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 258 QSLQELRDQYEGQMRINREEIELLYDnEIQNLKAAANRAaqgsalATEEVRLMRTKIDGLN---AKLQNLEDTN-AGLNA 333
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEE-ELERAMRAFNRE------WPAETADLDADLESLPeylALLDRLEEDGlPEYEE 834
|
250 260 270
....*....|....*....|....*....|....*
gi 442623692 334 RIRELenLLDTERQRHNQYIASLEAELQRMRDEMA 368
Cdd:COG4913 835 RFKEL--LNENSIEFVADLLSKLRRAIREIKERID 867
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
44-469 |
6.70e-04 |
|
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: 42.80 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYIDRMRNLENENSRLT---QELNLAQDTVNRETSNLKAVYEKELAAARKLLDEtakekaklEID 120
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTaslQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE--------GDH 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 121 IKRLWEENDDLKPRLDKKTKEATV----AENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELAlENERLRRQLDDLRK 196
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEIlrqqIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIR 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 197 QLEAET----LARVDLENQ-NQSLReelAFKD--QVHTQELTETRSRRQI--EISEIDGRLSRQYEAKlQQSLQELRDQY 267
Cdd:pfam15921 622 ELEARVsdleLEKVKLVNAgSERLR---AVKDikQERDQLLNEVKTSRNElnSLSEDYEVLKRNFRNK-SEEMETTTNKL 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 268 EGQMRINREEIELLyDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARirelENLLDTERQ 347
Cdd:pfam15921 698 KMQLKSAQSELEQT-RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKE----KHFLKEEKN 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 348 RHNQYIASLEAELQRMRDEM----AHQLQEYQGLMDIKVSLD---LEIAAYDKLLCGEERR---------LNIESPGRPT 411
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELevlrSQERRLKEKVANMEVALDkasLQFAECQDIIQRQEQEsvrlklqhtLDVKELQGPG 852
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442623692 412 TDSGISSNGSHLTASASSRSGRVTPSGRRSAT---------------PGISGSSAVKRRRTVIDESEDRTLSE 469
Cdd:pfam15921 853 YTSNSSMKPRLLQPASFTRTHSNVPSSQSTASflshhsrktnalkedPTRDLKQLLQELRSVINEEPTVQLSK 925
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
45-286 |
6.75e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 45 QEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVyEKELAAARKLLDETAKEKAKLEIDIKRL 124
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA-EKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 125 WEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELaleNERLRRQLDDLRKQLEAETLA 204
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL---LELARQLEDLLKEEKKEELEI 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 205 RVDLENQNQSLREELAF-KDQVHTQELTETRSRRQIEISEIDgRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYD 283
Cdd:pfam02463 432 LEEEEESIELKQGKLTEeKEELEKQELKLLKDELELKKSEDL-LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
...
gi 442623692 284 NEI 286
Cdd:pfam02463 511 VLL 513
|
|
| PRK09174 |
PRK09174 |
F0F1 ATP synthase subunit B; |
67-142 |
8.75e-04 |
|
F0F1 ATP synthase subunit B;
Pssm-ID: 169692 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 8.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442623692 67 LENENSRLTQELNLAQdTVNRETSNLKAVYEKELAAARK---LLDETAKEKAKLEIDikrlwEENDDLKPRLDKKTKEA 142
Cdd:PRK09174 82 IETRRDRIAQDLDQAA-RLKQEADAAVAAYEQELAQARAkahSIAQAAREAAKAKAE-----AERAAIEASLEKKLKEA 154
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
45-373 |
1.01e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 45 QEKEELQHLNDRLACYIDRMRNLENENSRLtqelnlAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRL 124
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIKELEFEIQSQ------EQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 125 WEENDDLKPRLDK----KTKEATVAENNARL------YENRYNEVNGKYNQSLADRKKFED-QAKELALENERLR----- 188
Cdd:pfam05557 227 KEEVEDLKRKLEReekyREEAATLELEKEKLeqelqsWVKLAQDTGLNLRSPEDLSRRIEQlQQREIVLKEENSSltssa 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 189 RQLDDLRKQLEAETLA-RVDLENQNQSLREELAFKDQVHTQELTETRSR---RQI--------EISEIDGRLSRQYE--A 254
Cdd:pfam05557 307 RQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyRAIlesydkelTMSNYSPQLLERIEeaE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 255 KLQQSLQELRDQYEGQMRINREEIELLYDN------EIQNLKAAANRAAQGSAlaTEEVRLMRTKIDGLNAKLQNLEDTN 328
Cdd:pfam05557 387 DMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtlerELQALRQQESLADPSYS--KEEVDSLRRKLETLELERQRLREQK 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 442623692 329 AGLNARI--RELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQE 373
Cdd:pfam05557 465 NELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
97-372 |
1.08e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 97 EKELAAARKLLDETAKEKAKLEIDIKrlwEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQ 176
Cdd:COG5185 207 IKESETGNLGSESTLLEKAKEIINIE---EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 177 AKELALENERLRRQLDDLRKQLEAETLARvDLENQNQSLREELAFKDQV---------HTQELTETRSRRQIEISEIDGR 247
Cdd:COG5185 284 ANNLIKQFENTKEKIAEYTKSIDIKKATE-SLEEQLAAAEAEQELEESKretetgiqnLTAEIEQGQESLTENLEAIKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 248 LS--------RQYEAKL---QQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQ------------------ 298
Cdd:COG5185 363 IEnivgevelSKSSEELdsfKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEElqrqieqatssneevskl 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442623692 299 GSALATEEVRLMRTKIDGLNAKLQNledTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQ 372
Cdd:COG5185 443 LNELISELNKVMREADEESQSRLEE---AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLE 513
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
178-224 |
1.32e-03 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 41.12 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 442623692 178 KELALENERLRRQLDDLRKQLeaetLARVDLENQNQSLREELAFKDQ 224
Cdd:PRK13922 72 FDLREENEELKKELLELESRL----QELEQLEAENARLRELLNLKES 114
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
97-373 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 97 EKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDkkTKEATVAEnnarlYENRYNEVngkynQSL-ADRKKFED 175
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD--EADEVLEE-----HEERREEL-----ETLeAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 176 QAKELALENERLRRQLDDLRKQLEaetlarvDLENQNQSLREELAFKDQvhTQELTETRsrrqieISEIDGRlsrqyEAK 255
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAGLDDA--DAEAVEAR------REELEDR-----DEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 256 LQQSLQELR---DQYEGQMRINREEIELLyDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLN 332
Cdd:PRK02224 326 LRDRLEECRvaaQAHNEEAESLREDADDL-EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 442623692 333 ARIRELENLLD---TERQRHNQYIASLEAELQRMRD--EMAHQLQE 373
Cdd:PRK02224 405 VDLGNAEDFLEelrEERDELREREAELEATLRTARErvEEAEALLE 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
112-310 |
1.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 112 KEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVngkynqslaDRKKFEDQAKELALENERLRRQL 191
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL---------EKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 192 DDLR---KQLEAETLARVDLENQNQSLREELAFKDQvhtqELTETRSRRQIEISEIDGRLSRQYEAklqqsLQELRDQYE 268
Cdd:COG4717 142 AELPerlEELEERLEELRELEEELEELEAELAELQE----ELEELLEQLSLATEEELQDLAEELEE-----LQQRLAELE 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442623692 269 GQMRINREEIELLyDNEIQNLKAAANRAAQGSALATEEVRLM 310
Cdd:COG4717 213 EELEEAQEELEEL-EEELEQLENELEAAALEERLKEARLLLL 253
|
|
| MreC |
COG1792 |
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ... |
178-225 |
2.01e-03 |
|
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 441397 Cd Length: 282 Bit Score: 40.63 E-value: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 442623692 178 KELALENERLRRQLDDLRKQLEAetLARvdLENQNQSLREELAFKDQV 225
Cdd:COG1792 71 FNLREENERLKEENAELRAELQR--LEE--LEAENARLRELLDLKERL 114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-377 |
2.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAqdtvnretsnlkavyeKELAAARKLLDETAKEKAKLEIDIKR 123
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------------EKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 124 LWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETL 203
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 204 ARVDLENQNQSLREE----------------------------------------------------------------- 218
Cdd:COG4717 228 ELEQLENELEAAALEerlkearlllliaaallallglggsllsliltiagvlflvlgllallflllarekaslgkeaeel 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 219 --LAFKDQVHTQELTETRSRRQIEISEIDGRLSRQYE--AKLQQSLQELRDQyEGQMRINREEIE---LLYDNEIQNLKA 291
Cdd:COG4717 308 qaLPALEELEEEELEELLAALGLPPDLSPEELLELLDriEELQELLREAEEL-EEELQLEELEQEiaaLLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 292 AANRAAQGSAL--ATEEVRLMRTKIDGLNAKLQNLEDTN--AGLNARIRELE---NLLDTERQRHNQYIASLEAELQRMR 364
Cdd:COG4717 387 LRAALEQAEEYqeLKEELEELEEQLEELLGELEELLEALdeEELEEELEELEeelEELEEELEELREELAELEAELEQLE 466
|
410
....*....|....*
gi 442623692 365 --DEMAHQLQEYQGL 377
Cdd:COG4717 467 edGELAELLQELEEL 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
284-375 |
2.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 284 NEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELEnlldterqrhnQYIASLEAELQRM 363
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----------KEIAELRAELEAQ 102
|
90
....*....|..
gi 442623692 364 RDEMAHQLQEYQ 375
Cdd:COG4942 103 KEELAELLRALY 114
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
44-373 |
2.47e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKE--ELQHLNDRLACYIDRMRNLENENSRLtqelnlaqdtvnRETSNLKAVYEKELAAARKLLDETAKekakLEIDI 121
Cdd:pfam05622 91 ELEKEvlELQHRNEELTSLAEEAQALKDEMDIL------------RESSDKVKKLEATVETYKKKLEDLGD----LRRQV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 122 KRLWEENDDLKPR---LDKKTKEATVAENNARLYENRYNEVNGKYNQ--SLADRKKFED---QAKELAL--ENERLRRQL 191
Cdd:pfam05622 155 KLLEERNAEYMQRtlqLEEELKKANALRGQLETYKRQVQELHGKLSEesKKADKLEFEYkklEEKLEALqkEKERLIIER 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 192 DDLRKQLEAETLARVdlenQNQSLREELAFKDQVHTQELTETRSRRQIEISEIDGRLsrQYEAKLqqslqeLRDQYEGQM 271
Cdd:pfam05622 235 DTLRETNEELRCAQL----QQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRL--QHENKM------LRLGQEGSY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 272 RINREEIELLYD--NEIQNLKAAANRAAQgsalatEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLD------ 343
Cdd:pfam05622 303 RERLTELQQLLEdaNRRKNELETQNRLAN------QRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEklheaq 376
|
330 340 350
....*....|....*....|....*....|
gi 442623692 344 TERQRHNQYIASLEAELQRMRDEMAHQLQE 373
Cdd:pfam05622 377 SELQKKKEQIEELEPKQDSNLAQKIDELQE 406
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
115-276 |
2.66e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 115 AKLEIDIKRLWEENDDLKPRLdkktkeatvaENNARLYENrynEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDL 194
Cdd:pfam07111 477 ADLSLELEQLREERNRLDAEL----------QLSAHLIQQ---EVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASV 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 195 RKQLEAETLARVDLENQNQSLREELAFKDQVHTQEL------TETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYE 268
Cdd:pfam07111 544 GQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALqekvaeVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRAT 623
|
....*...
gi 442623692 269 GQMRINRE 276
Cdd:pfam07111 624 QEKERNQE 631
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
97-361 |
2.69e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 97 EKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAEN-NARLyENRYNEVNGKYNQSLADRKKFED 175
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEmRARL-AARKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 176 QAKELALENERLRRQLDDLRKQLEAETLAR-------VDLENQNQSLREE-LAFKDQvhTQELTETRSRRQIEISEIDGR 247
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARqklqlekVTTEAKIKKLEEDiLLLEDQ--NSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 248 LSRQYEAklQQSLQELRDQYEGQM-----RINREEiellydNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQ 322
Cdd:pfam01576 168 LAEEEEK--AKSLSKLKNKHEAMIsdleeRLKKEE------KGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 442623692 323 NLEDTNAGLNARIRElENLLDTERQRHNQYIASLEAELQ 361
Cdd:pfam01576 240 KKEEELQAALARLEE-ETAQKNNALKKIRELEAQISELQ 277
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
170-375 |
2.71e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 170 RKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREE-----------LAFKDQV---------HTQE 229
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQwqavcaslnitLQPQDDIqpwldaqeeHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 230 LTETRSRRQIEiSEIDG--RLSRQYEAKLQQSLQELRDQYEGQMRINREEiellyDNEIQNLKAAANRAAQGSALATEEV 307
Cdd:PRK10246 612 LRLLSQRHELQ-GQIAAhnQQIIQYQQQIEQRQQQLLTALAGYALTLPQE-----DEEASWLATRQQEAQSWQQRQNELT 685
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442623692 308 RLmRTKIDGLNAKLQNLEDTNAglnARIRELENLLDTERQRHNQYIaSLEAELQRMRDEMAHQLQEYQ 375
Cdd:PRK10246 686 AL-QNRIQQLTPLLETLPQSDD---LPHSEETVALDNWRQVHEQCL-SLHSQLQTLQQQDVLEAQRLQ 748
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
228-402 |
2.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 228 QELTETRSRRQIEISEIDGRLSRQyeAKLQQSLQELRDQYEGQMRINREEIELLY-DNEIQNLKAAANRAAQGS---ALA 303
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEAL--EAELDALQERREALQRLAEYSWDEIDVASaEREIAELEAELERLDASSddlAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 304 TEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVS 383
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170
....*....|....*....
gi 442623692 384 LDLEIAAYDKLLCGEERRL 402
Cdd:COG4913 771 LEERIDALRARLNRAEEEL 789
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-381 |
2.90e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYIDRMRNLENENSRLTQELN-LAQDTVNRETS---NLKAVYEKELAAARKLLDETAKEKA--KL 117
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdLQGQLAHAKKQqelQQRYAELCAAAITCTAQCEKLEKIHlqES 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 118 EIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGK---YNQSLADRKKFE-DQAKELALENE--RLRRQL 191
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihPNPARQDIDNPGpLTRRMQRGEQTyaQLETSE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 192 DDLRKQLEAETLARVDLENQNQSLREE---LAFKDQVHTQELTETR-----------------------SRRQIEI--SE 243
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQnitvrlqdlteklseaedmlaceQHALLRKlqPE 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 244 IDGRLSRQYEAKLQQSLQELrdqyegQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQN 323
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALK------LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 324 LEDTNAGLNArirELENLLDTERQRHNQYIA--SLEAELQRMRDEMAHQLQEYQGLMDIK 381
Cdd:TIGR00618 699 LAQCQTLLRE---LETHIEEYDREFNEIENAssSLGSDLAAREDALNQSLKELMHQARTV 755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-220 |
2.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYID--RMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDI 121
Cdd:COG4913 268 RERLAELEYLRAALRLWFAqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 122 KRLWEENDDLKPRLDK-----KTKEATVAENNARLYENRyNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRK 196
Cdd:COG4913 348 ERLERELEERERRRARleallAALGLPLPASAEEFAALR-AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180
....*....|....*....|....
gi 442623692 197 QLEAETLARVDLENQNQSLREELA 220
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALA 450
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
44-277 |
3.61e-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: 40.49 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 44 QQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNlAQDTVNRETSNLKAVYEKELAAAR-----KLLDETAKEKAKLE 118
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERIRqeerkRELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 119 I----DIKRLWEE----NDDLKPRLDKKTKEATVAENNARLYENRYNEVNG-KYNQSLADRKKFEDQAKELALENERLR- 188
Cdd:pfam17380 374 IsrmrELERLQMErqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRl 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 189 ------RQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQELTETRSR-----------------RQIEISEID 245
Cdd:pfam17380 454 eeqerqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieeerkrkllekemeeRQKAIYEEE 533
|
250 260 270
....*....|....*....|....*....|..
gi 442623692 246 GRLSRQYEAKLQQSLQElRDQYEGQMRINREE 277
Cdd:pfam17380 534 RRREAEEERRKQQEMEE-RRRIQEQMRKATEE 564
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-363 |
5.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 40 RTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQ---DTVNRETSNLKAVYEKELAAARKLLDETAKEKAK 116
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 117 LEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYN--EVNGKYNQSLADRKK--------------FEDQAKEL 180
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEddEVAAAAIEYLKAAKAgratflpldkirarAALAAALA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 181 ALENERLRRQLDDLRKQLEAETLARVD--LENQNQSLREELAFKDQVHTQELTETRSRRQIEISE---IDGRLSRQYEAK 255
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDtlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAggsLTGGSRRELLAA 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 256 LQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARI 335
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
330 340
....*....|....*....|....*...
gi 442623692 336 RELENLLDTERQRhnQYIASLEAELQRM 363
Cdd:COG1196 754 EELPEPPDLEELE--RELERLEREIEAL 779
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
121-361 |
5.91e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 121 IKRLWEENDDLKPRLDkktkeatVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELAL----ENERLRRQLDDLRK 196
Cdd:PHA02562 176 IRELNQQIQTLDMKID-------HIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKtikaEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 197 QLEAET-------LARVDLENQNQSL-REELAFKDQVHTQELTETrsrrqieISEIDGRLSrqyeaKLQQSLQELRDQYE 268
Cdd:PHA02562 249 DIEDPSaalnklnTAAAKIKSKIEQFqKVIKMYEKGGVCPTCTQQ-------ISEGPDRIT-----KIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 269 gqmrinreeielLYDNEIQNLKAAANRAAQgsalATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELEnlldTERQR 348
Cdd:PHA02562 317 ------------KLDTAIDELEEIMDEFNE----QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ----AEFVD 376
|
250
....*....|...
gi 442623692 349 HNQYIASLEAELQ 361
Cdd:PHA02562 377 NAEELAKLQDELD 389
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
163-359 |
7.15e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.89 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 163 YNQSLADRKKFEDQAKELALEN--ERLRRQLDDLRKQLEaetlarvDLENQNQSLREEL-AFKDQ--VHTQELTETRSRR 237
Cdd:cd22656 93 YAEILELIDDLADATDDEELEEakKTIKALLDDLLKEAK-------KYQDKAAKVVDKLtDFENQteKDQTALETLEKAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 238 QIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAAnRAAQGSALATEEVRLMRTKIDGL 317
Cdd:cd22656 166 KDLLTDEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAAL-RLIADLTAADTDLDNLLALIGPA 244
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442623692 318 NAKLQNLEDTNAGLNARIRELENLLDT-ERQRHNQYIASLEAE 359
Cdd:cd22656 245 IPALEKLQGAWQAIATDLDSLKDLLEDdISKIPAAILAKLELE 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-394 |
8.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 258 QSLQELRDQYEG---QMRINREEIELLydneiQNLKAAANR--AAQGSALATEEVRLM------RTKIDGLNAKLQNLED 326
Cdd:COG4913 228 DALVEHFDDLERaheALEDAREQIELL-----EPIRELAERyaAARERLAELEYLRAAlrlwfaQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 327 TNAGLNARIRELENLLDTERQRHNQY-----------IASLEAELQRM---RDEMAHQLQEYQGLM-DIKVSLDLEIAAY 391
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELeaqirgnggdrLEQLEREIERLereLEERERRRARLEALLaALGLPLPASAEEF 382
|
...
gi 442623692 392 DKL 394
Cdd:COG4913 383 AAL 385
|
|
| mreC |
TIGR00219 |
rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape ... |
154-221 |
8.51e-03 |
|
rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped. Cells defective in MreC are round. Species with MreC include many of the Proteobacteria, Gram-positives, and spirochetes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129323 [Multi-domain] Cd Length: 283 Bit Score: 38.69 E-value: 8.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442623692 154 NRYNEVNGKYNQSLADRKKFEdqakelaLENERLRRQLDDLRKQLEAETLarvDLENQNQSLREELAF 221
Cdd:TIGR00219 52 NRPREVFDGISENLKDVNNLE-------YENYKLRQELLKKNQQLEILTQ---NLKQENVRLRELLNS 109
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
42-235 |
8.78e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 42 SRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELnlaqdtvnretSNLKAVYEKELAAARKLLDETAKEKAKLEI-- 119
Cdd:PHA02562 207 QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL-----------LNLVMDIEDPSAALNKLNTAAAKIKSKIEQfq 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442623692 120 DIKRLWEEND----------DLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENE---R 186
Cdd:PHA02562 276 KVIKMYEKGGvcptctqqisEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQsliT 355
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442623692 187 LRRQLDDLRKQLEAETLARVDLENQNQSLREELafkdqvhtQELTETRS 235
Cdd:PHA02562 356 LVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL--------DKIVKTKS 396
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|
| |
