|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
22-279 |
8.16e-147 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 428.68 E-value: 8.16e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 22 VLCAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELL 101
Cdd:pfam04849 52 LLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 102 QFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKE 181
Cdd:pfam04849 132 QIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 182 LRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 261
Cdd:pfam04849 212 LSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAE 291
|
250
....*....|....*...
gi 388454134 262 CMEMLHEAQEELKNLRNK 279
Cdd:pfam04849 292 CLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
340-509 |
2.59e-76 |
|
Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.
Pssm-ID: 463588 Cd Length: 171 Bit Score: 241.80 E-value: 2.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 340 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDIGNVVLDNKTNSIILETEAADLGNDERSKKPGTPGTPGSH 419
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 420 DLETALRRLSLRRENYLSERRFFEEEQERKLQELAE----KGELRSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 495
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157
|
170
....*....|....
gi 388454134 496 LPEKLQIVKPLEGS 509
Cdd:pfam12448 158 LPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-279 |
1.66e-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: 74.32 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 38 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 117
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 118 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 194
Cdd:TIGR02168 777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 195 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 267
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 388454134 268 EAQEELKNLRNK 279
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-279 |
3.05e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 25 AERVGQMTKTYNDIDAVTRLL--EEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQ 102
Cdd:COG1196 212 AERYRELKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 103 FYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcVKEL 182
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----EEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 183 RDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 262
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|....*..
gi 388454134 263 MEMLHEAQEELKNLRNK 279
Cdd:COG1196 448 AEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-277 |
7.51e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE 109
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 110 ESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETityEEKEQQLVnDCVKELRDANVQI 189
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI---AATERRLE-DLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 190 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 269
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
....*...
gi 388454134 270 QEELKNLR 277
Cdd:TIGR02168 935 EVRIDNLQ 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-279 |
4.63e-08 |
|
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: 56.61 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 26 ERVGQMTKTYNDID-AVTRLLEEKERDLELAARIGQslLKKnktltERNELLEEQvEHIREEVSQLRHELS--------- 95
Cdd:TIGR02169 650 EKSGAMTGGSRAPRgGILFSRSEPAELQRLRERLEG--LKR-----ELSSLQSEL-RRIENRLDELSQELSdasrkigei 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 96 MKD-ELLQFYTSAA----EESEPE-SVCSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEE 169
Cdd:TIGR02169 722 EKEiEQLEQEEEKLkerlEELEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 170 KE-QQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 248
Cdd:TIGR02169 794 PEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
250 260 270
....*....|....*....|....*....|.
gi 388454134 249 TAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-279 |
7.55e-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: 55.83 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 30 QMTKTYNDIDAVTRLLEEKERDLELaarigqslLKKNKTLTERNELLEEQVEHIREEVSQLRHElSMKDELLQFYTSAAE 109
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLRLE-ELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 110 ESEpesvcstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQI 189
Cdd:TIGR02168 251 AEE----------------------ELEELTAELQELEEKLEELRLEVSELEEE----IEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 190 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 269
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250
....*....|
gi 388454134 270 QEELKNLRNK 279
Cdd:TIGR02168 385 RSKVAQLELQ 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-292 |
6.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 25 AERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKD 98
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 99 E----LLQFYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL 174
Cdd:PRK03918 293 EeyikLSEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 175 VN--------------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHlgA 240
Cdd:PRK03918 372 EElerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--H 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 388454134 241 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHSL 292
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-225 |
9.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 45 LEEKERDLELAarigQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstplKRN 124
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---------LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 125 ESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEK----EQQLVNDCVKELRDANVQIASISEELAKKT 200
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 388454134 201 EDAARQQEEITHLLSQIVDLQKKAK 225
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-279 |
1.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 49 ERDLELAARIgQSLlKKNKTLTE--RNELLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 111
Cdd:COG4913 191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 112 EpesvcstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIAS 191
Cdd:COG4913 269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 192 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:COG4913 335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
250 260
....*....|....*....|
gi 388454134 260 AECMEMLHEAQEELKNLRNK 279
Cdd:COG4913 415 RDLRRELRELEAEIASLERR 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-319 |
2.33e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKKTEDAARQQEEITHLLS 215
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN----EQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 216 QIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME-----MLHEAQEELKNLRNKTMPNTTSRRYH 290
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180
....*....|....*....|....*....
gi 388454134 291 SLGLFPMDSLAAEIEGTMRKELQLEEAES 319
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-342 |
2.58e-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: 50.15 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 180 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 260 AECMEML--HEAQEELKNLRNKTMPNTTSRRYHSLGLFpMDSLAAEIEgTMRKELQLEEAESPDITHQKRVFETVRNINQ 337
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAE-ELRADLAELAALRAELEAERAELEALLAELE 184
|
....*
gi 388454134 338 VVKQR 342
Cdd:COG4942 185 EERAA 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-297 |
6.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLktetityeEKEQQLVNDcVKELRDANVQIASISEELAK---KTEDAARQQEEITH 212
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKL--------EKLLQLLPL-YQELEALEAELAELPERLEEleeRLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 213 LLSQIVDLQKK-AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHS 291
Cdd:COG4717 168 LEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
....*.
gi 388454134 292 LGLFPM 297
Cdd:COG4717 248 ARLLLL 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
45-284 |
8.75e-06 |
|
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: 48.95 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 45 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDEllqfytsaAEESEPESVCSTPLKRN 124
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKE 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 125 ESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAS--------------QLKTETITYEEKEQQLVNDCVKELRDA 185
Cdd:pfam05483 587 KQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSaenkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDK 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 186 NVQIASISEELAKK---TEDAARQQEEI----THLLSQIVDLQKKAKACAVE-NEELVQHLGAAKDAQRQ-------LTA 250
Cdd:pfam05483 667 KISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKiIEERDSELGLYKNKEQEqssakaaLEI 746
|
250 260 270
....*....|....*....|....*....|....
gi 388454134 251 ELRELEDKYAECMEMLHEAQEELKNLRNKTMPNT 284
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-272 |
2.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdcVKELRDANVQIASISEELAkktedaaRQQEEITHLL- 214
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIA-------ELEAELERLDa 682
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 215 --SQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 272
Cdd:COG4913 683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
67-276 |
2.44e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 67 KTLTERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESV--CSTPLKRNESSSSvqnyfHLDS 138
Cdd:PRK04863 841 QLNRRRVELeraladHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVeeIREQLDEAEEAKR-----FVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 139 LQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLL 214
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--------RDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388454134 215 SQivdLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:PRK04863 988 EK---LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9-275 |
2.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 9 YYELDWYYEECSDVLCAERVGQMTKTYndiDAVTRL--------LEEKERDLELAAR--IGQSLLKKNKTLTERNELLEE 78
Cdd:COG4913 548 RAWLEAELGRRFDYVCVDSPEELRRHP---RAITRAgqvkgngtRHEKDDRRRIRSRyvLGFDNRAKLAALEAELAELEE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 79 QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplkrnESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEAS 158
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWDE----------IDVASAER--EIAELEAELERLDASSDDLAALEE 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 159 QLktetityeEKEQQLVNDCVKELRDANVQIASISEELakktEDAARQQEEITHLLSQIVDLqkkakACAVENEELVQHL 238
Cdd:COG4913 693 QL--------EELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDL-----ARLELRALLEERF 755
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 388454134 239 GAA------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 275
Cdd:COG4913 756 AAAlgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-318 |
3.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 33 KTYNDIDAVTRLLEEKERdlELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESe 112
Cdd:PRK03918 362 ELYEEAKAKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 113 peSVCSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEASQLktETITYEEKEQQLVNDCVKELRDANVQIAS 191
Cdd:PRK03918 439 --PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELAEQLKELEEKLKK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 192 IS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 270
Cdd:PRK03918 515 YNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 388454134 271 EELKNLRNKTMPNTTSRRYHSLGLFPMDSLAAEIEGTmRKELQLEEAE 318
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKR 641
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-283 |
3.97e-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: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 38 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREE--VSQLRHELSMKDELLQfytsAAEESEPEs 115
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELE----RLDASSDD- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 116 vcstplkrnessssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCvKELRDANVQIASIS-- 193
Cdd:COG4913 687 --------------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLArl 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 194 ------EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEEL-----------VQHLGAAKDAQRQLTAELRELE 256
Cdd:COG4913 746 elrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPEYLALLDRLE 825
|
250 260
....*....|....*....|....*..
gi 388454134 257 DkyaecmEMLHEAQEELKNLRNKTMPN 283
Cdd:COG4913 826 E------DGLPEYEERFKELLNENSIE 846
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-277 |
4.84e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 38 IDAVTRLLEEKERDLELAArigqslLKKNKTLTERNELLEEqVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvc 117
Cdd:TIGR02169 197 RQQLERLRREREKAERYQA------LLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISELE----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 118 stplKRNESSSSVqnyfhLDSLQKKLKDL-EEENVVLRSEASQLKTETI----TYEEKEQQLvNDCVKELRDANVQIASI 192
Cdd:TIGR02169 265 ----KRLEEIEQL-----LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 272
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
....*
gi 388454134 273 LKNLR 277
Cdd:TIGR02169 415 LQRLS 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
78-276 |
9.39e-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: 45.14 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 78 EQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEA 157
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ------LAALERR--------IAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 158 SQLKTETITYEEKEQQLVNDCVKELRDANVQ------------------------IASISEELAKKTEDAARQQEEITHL 213
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 388454134 214 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
53-277 |
1.10e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 53 ELAARIGQSLLK--KNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstplkrnESSSSV 130
Cdd:COG3206 148 ELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---------EAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 131 QNyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCV-----KELRDANVQIASISEELAKKTEDAAR 205
Cdd:COG3206 219 QQ---LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388454134 206 QQEEITHLLSQIVDLQKKAKAcAVENEelvqhLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLR 277
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILA-SLEAE-----LEALQAREASLQAQLAQLEARLAE----LPELEAELRRLE 357
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
56-269 |
1.37e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 56 ARIgQSLLKKNKTLTERnelleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESVCSTPLK-RNE-SSSSVQNY 133
Cdd:PLN02939 150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 134 FHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdCVKE--LRDANVQiasiseELAKKTEDAarqQEEIt 211
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388454134 212 hllSQIVDLQKKAKACAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA 269
Cdd:PLN02939 288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEA 343
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
46-268 |
1.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 46 EEKERDLE-LAARIGQSLLKKNKTLTERNELLEEqVEHIREEVSQLRHELsmkDELLQfyTSAAEESEPESVCStplkrn 124
Cdd:PRK02224 247 EERREELEtLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEER---DDLLA--EAGLDDADAEAVEA------ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 125 essssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvNDCVKELRDanvQIASISEELAKKTEDAA 204
Cdd:PRK02224 315 ----------RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388454134 205 RQQEEITHLLSQIVDLQKKAKACAVE-------NEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 268
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDlgnaedfLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-319 |
2.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 33 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESE 112
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 113 pesvcstPLKRNESsssvqnyfhldSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASI 192
Cdd:PRK03918 242 -------ELEKELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKacavENEELVQHLGAAKDAQRQLTAELRELEdKYAECMEMLHEAQEE 272
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 388454134 273 LKNLRNKtmpnttsrryhsLGLFPMDSLAAEIEGTMRKELQLEEAES 319
Cdd:PRK03918 374 LERLKKR------------LTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-226 |
2.80e-04 |
|
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: 43.60 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkdELLQFYTSAAE 109
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 110 ESEPESVcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQI 189
Cdd:COG4942 119 QPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 388454134 190 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 226
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-281 |
2.82e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 32 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEeQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 110
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 111 SEPE-SVCSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETIT-YEEKEQQL---------VNDCV 179
Cdd:PRK03918 537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 180 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcaVENEELVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260
....*....|....*....|..
gi 388454134 260 AECMEMLHEAQEELKNLRNKTM 281
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKK 711
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
136-279 |
3.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTEtITYEEKEQQLVNdcvKELRDANVQIASISEEL--AKKTEDAARQQEEITHL 213
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLE---LEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388454134 214 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-319 |
3.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 43 RLLEEKERdLELAARIGQSLLKKNKTLTErnelLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstPLK 122
Cdd:PRK03918 443 RELTEEHR-KELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE----KLK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 123 RNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQ---LKTETITYEEKEQQL---VNDCVKELRDANVQIASISEEL 196
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEER 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 197 AKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemlheaqEELKNL 276
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EEYEEL 664
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 388454134 277 RNKTMpnTTSRRYHSL--GLFPMDSLAAEIEGTMRK-ELQLEEAES 319
Cdd:PRK03918 665 REEYL--ELSRELAGLraELEELEKRREEIKKTLEKlKEELEEREK 708
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-276 |
3.33e-04 |
|
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: 43.86 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 48 KERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTS---AAEESEPESVcsTPLKRN 124
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIK--KQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 125 EsSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQ-----LKTETITYEEKEQQLVNDCV---KELRDANVQIASISEEL 196
Cdd:TIGR04523 273 Q-KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQLKKEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 197 AKKTEDAARQQEEITHLLSQIVDLQKkakacavENEELvqhlgaaKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKK-------ENQSY-------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-279 |
4.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 77 EEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESvcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEenvvLRS 155
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERAEE----LRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 156 EASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENE 232
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 388454134 233 ELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
42-276 |
4.69e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 42 TRLLEEKERDLELAARIGQsllkknKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpl 121
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE------- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 122 kRNE----SSSSVQNY-FHLDSLQKKLKDLEEEnvvlrsEASQLKTETITYEEKEQQLVndcVKELRDANVQiasiseEL 196
Cdd:TIGR00618 720 -FNEienaSSSLGSDLaAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVT---AALQTGAELS------HL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 197 AKKTEDAARQQEEITHLLSQI-VDLQKKAK----ACAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAECMEMLHE 268
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLeAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQ 863
|
....*...
gi 388454134 269 AQEELKNL 276
Cdd:TIGR00618 864 LTQEQAKI 871
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-287 |
6.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 38 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAE-----ES 111
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRREEIEEleeeiEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 112 EPESVCSTPLKRNESSSsvqnyfHLDSLQKKLKDLEEENVVLRS----------EASQLKTE---------------TIT 166
Cdd:PRK02224 396 LRERFGDAPVDLGNAED------FLEELREERDELREREAELEAtlrtarerveEAEALLEAgkcpecgqpvegsphVET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 167 YEEKEQQlVNDCVKELRDANVQIASISEEL--AKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDa 244
Cdd:PRK02224 470 IEEDRER-VEELEAELEDLEEEVEEVEERLerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA- 547
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 388454134 245 qrQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSR 287
Cdd:PRK02224 548 --ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
36-226 |
6.86e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 36 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS--------MKDELLQF---- 103
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 104 YTSAAEESEPESVCSTPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL--- 174
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeal 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 388454134 175 VNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 226
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
45-279 |
8.67e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.86 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 45 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS----MKDELlqfytsaaeesepESVCSTp 120
Cdd:pfam09728 13 LDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailAKSKL-------------EKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 121 lkrnessssvqnyfhldsLQKKLKDLEEENVVLRSEASQLKTETItyeEKEQQLVND---CVKELRDANVQIASISEELA 197
Cdd:pfam09728 79 ------------------LQKQNKKLKEESKKLAKEEEEKRKELS---EKFQSTLKDiqdKMEEKSEKNNKLREENEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 198 KKTEDAARQQEeithLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEM---LHEAQEELK 274
Cdd:pfam09728 138 EKLKSLIEQYE----LRELHFEKLLKTK-------ELEVQLAEAKLQQATEEEEKKAQEKEVAKARELkaqVQTLSETEK 206
|
....*
gi 388454134 275 NLRNK 279
Cdd:pfam09728 207 ELREQ 211
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
31-279 |
8.72e-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: 42.65 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 31 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMK-------DELLQF 103
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELlrdeqeeIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 104 YTSAAEESEPESvcstpLKRNESSSSVQNYfhLDSLQKKLKDLEEEnvvLRSEASQLKTETITYEEKEQQLVNDCVKELR 183
Cdd:pfam02463 259 EIEKEEEKLAQV-----LKENKEEEKEKKL--QEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 184 DANVQIASISEELAKKTEDAARQQEEIThllsQIVDLQKKAKAcavENEELVQHLGAAKDAQRQLTAELRELEDKYAECM 263
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEE----EEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250
....*....|....*.
gi 388454134 264 EMLHEAQEELKNLRNK 279
Cdd:pfam02463 402 EEEKEAQLLLELARQL 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-277 |
8.91e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELAKKTEDAARQ------ 206
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388454134 207 ---QEEITHLLSQ--IVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 277
Cdd:COG4942 116 lgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-274 |
1.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQ-------------------------IA 190
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 191 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 270
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....
gi 388454134 271 EELK 274
Cdd:COG3883 206 AAAE 209
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-276 |
1.26e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 40 AVTRLLEEKERDLE-LAARIGQsllKKNKTLTER-NEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 111
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 112 EP---------ESVCSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEASqlktetitYEEKEQQLVNDCVKEL 182
Cdd:PRK02224 254 ETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 183 RDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 262
Cdd:PRK02224 320 ED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250
....*....|....
gi 388454134 263 MEMLHEAQEELKNL 276
Cdd:PRK02224 397 RERFGDAPVDLGNA 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
42-275 |
1.58e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 42 TRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIrEEVSQLrhelsmKDELLQFYTSAAEESEPEsvcstpL 121
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQ------KDEQIKKLQQEKELLEKE------I 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 122 KRNESSSSVQNyfhldslqKKLKDLEEENVVLRSEASQLKTETityEEKEQQLvndcvKELrdaNVQIASISEELAKKTE 201
Cdd:TIGR04523 429 ERLKETIIKNN--------SEIKDLTNQDSVKELIIKNLDNTR---ESLETQL-----KVL---SRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388454134 202 DAARQQEEITHLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 275
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVK-------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-226 |
2.04e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 29 GQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS-MKDELLQFytsa 107
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdLEDELNKD---- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 108 aeesepesvcSTPLKRNESSSSVqnyfhlDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKeqqlVNDCVKELRDANV 187
Cdd:TIGR04523 551 ----------DFELKKENLEKEI------DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE----KKDLIKEIEEKEK 610
|
170 180 190
....*....|....*....|....*....|....*....
gi 388454134 188 QIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 226
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
43-279 |
2.47e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 43 RLLEEKERDL---ELAARIGQSLLKKNKTLTERNELLEEQ----VEHIREEVSQLRHELSMKDEL-LQFYTSAAEESEpe 114
Cdd:COG5022 833 RETEEVEFSLkaeVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVELAERQLQELKIDVKSISSLkLVNLELESEIIE-- 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 115 svcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEEN--VVLRSEASQLKTETITYEEKEQQLvNDCVKELRDANVQIASI 192
Cdd:COG5022 911 ------LKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKL-KETSEEYEDLLKKSTIL 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEElVQHLGAAKDAQRQLTAELR---ELEDKYAECMEMLHEA 269
Cdd:COG5022 984 VREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE-VAELQSASKIISSESTELSilkPLQKLKGLLLLENNQL 1062
|
250
....*....|
gi 388454134 270 QEELKNLRNK 279
Cdd:COG5022 1063 QARYKALKLR 1072
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
42-262 |
2.50e-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: 41.31 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 42 TRLLEEKERDLELAARIGQSLLKKNKTL-TERNELLEE--QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcs 118
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALeSENAELQAElrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 119 tplkRNESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEASQLK-----TETITYEEKEQQLVNDcvKELRDANVQIASIS 193
Cdd:pfam01576 431 ----LAEKLSKLQS--ELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLS--TRLRQLEDERNSLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 388454134 194 EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQhlgAAKDAQRQLTAELRELEDKYAEC 262
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE---GKKRLQRELEALTQQLEEKAAAY 568
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-279 |
2.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 123 RNESS-SSVQNYFH---LDSLQKKLKDLeeenvvLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASISEELAK 198
Cdd:COG4717 31 PNEAGkSTLLAFIRamlLERLEKEADEL------FKPQGRKPELNLKELKELEEEL-----KEAEEKEEEYAELQEELEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 199 KTEDAARQQEEITHLLSQIVDLQKkakacAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLRN 278
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEA 170
|
.
gi 388454134 279 K 279
Cdd:COG4717 171 E 171
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
44-279 |
2.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 44 LLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEEsepesvcstplkR 123
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 124 NESSSSVQNYF-HLDSLQKKLKDLEEENV---VLRSEASQL----KTETITyEEKEQQLVNdcvkelrdanvQIASISEE 195
Cdd:COG1340 81 DELNEKLNELReELDELRKELAELNKAGGsidKLRKEIERLewrqQTEVLS-PEEEKELVE-----------KIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 196 LaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 275
Cdd:COG1340 149 L-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
....
gi 388454134 276 LRNK 279
Cdd:COG1340 228 LHEE 231
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
74-279 |
2.89e-03 |
|
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: 41.19 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 74 ELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVL 153
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 154 RSEASQL---KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEeithLLSQIVDLQKKAKACAVE 230
Cdd:TIGR00606 715 ESELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTD 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 388454134 231 NEELVQHLGAAKDAQR---QLTAELR--ELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:TIGR00606 791 VTIMERFQMELKDVERkiaQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
43-211 |
3.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 43 RLLEEKERDLELA--ARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstp 120
Cdd:COG1579 8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 121 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKT 200
Cdd:COG1579 80 ----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|.
gi 388454134 201 EDAARQQEEIT 211
Cdd:COG1579 152 AELEAELEELE 162
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
61-281 |
3.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 61 SLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEEsepesvcstplKRNESSSSVQNYFHLDSLQ 140
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE-----------LRKELAELNKAGGSIDKLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 141 KKLKDLEEEnvvlrseasqLKTETITyEEKEQQLVNdcvkelrdanvQIASISEELaKKTEDAARQQEEITHLLSQIVDL 220
Cdd:COG1340 116 KEIERLEWR----------QQTEVLS-PEEEKELVE-----------KIKELEKEL-EKAKKALEKNEKLKELRAELKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 221 QKKAKACAVENEELVQHLGAAKDAQRQLT---------------------AELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1340 173 RKEAEEIHKKIKELAEEAQELHEEMIELYkeadelrkeadelhkeiveaqEKADELHEEIIELQKELRELRKELKKLRKK 252
|
..
gi 388454134 280 TM 281
Cdd:COG1340 253 QR 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
133-281 |
3.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 133 YFHLDSLQKKLKDLEEENVVL----RSEASQLKTETIT-YEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQ 207
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388454134 208 EEITHllsqivdlqkkakacavENEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTM 281
Cdd:PRK12704 103 ELLEK-----------------REEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-279 |
3.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHlls 215
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---LEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388454134 216 QIVDLQKKAKACAVEN--------EELVQHLGAAK---DAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-342 |
4.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 180 KELRDANVQIasisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQR--QLTAELRELED 257
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 258 KYAEcmemLHEAQEELKNLRNKtmpnttsrryhslglfpMDSLAAEIEgtmRKELQLEEA-ESPDITHQKRVFETVRNIN 336
Cdd:COG4717 147 RLEE----LEERLEELRELEEE-----------------LEELEAELA---ELQEELEELlEQLSLATEEELQDLAEELE 202
|
....*.
gi 388454134 337 QVVKQR 342
Cdd:COG4717 203 ELQQRL 208
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
77-259 |
4.74e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 39.68 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 77 EEQVEHIREEVSQLRHEL-----SMKDELLQFYTSAAEEsepESVCSTPLKRNESSSSVQNYFH-LDSLQKKLKDLEE-- 148
Cdd:pfam04108 111 EDSVEILRDALKELIDELqaaqeSLDSDLKRFDDDLRDL---QKELESLSSPSESISLIPTLLKeLESLEEEMASLLEsl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 149 ----ENVVLRSEASQ-LKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKK 223
Cdd:pfam04108 188 tnhyDQCVTAVKLTEgGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSR 267
|
170 180 190
....*....|....*....|....*....|....*.
gi 388454134 224 AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:pfam04108 268 LPEYLAALKEFEERWEEEKETIEDYLSELEDLREFY 303
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
39-273 |
4.76e-03 |
|
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: 40.21 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 39 DAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAEesepesvc 117
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELeALEDQHGAFLDADIE-------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 118 stplkrnessSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLVNDCVKElrdanvqIASISEELA 197
Cdd:pfam12128 341 ----------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK---YNRRRSKIKEQNNRD-------IAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 198 KKTEDAARQQEEITHLL----SQIVDLQKKAKACAVENEE-LVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEE 272
Cdd:pfam12128 401 KIREARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYrLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREE 479
|
.
gi 388454134 273 L 273
Cdd:pfam12128 480 Q 480
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
67-279 |
4.84e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 67 KTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSV----QNYFHLDSLQKK 142
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVeeakTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 143 LKDLEEENVVLRSEASQLKTETITYEEKEQQLVND------------CVKELRDANVQIASISE---ELAKKTEDAARQQ 207
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptCTQQISEGPDRITKIKDklkELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388454134 208 EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
190-282 |
4.87e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 37.75 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 190 ASISEELAKKTEDAArqqeEITHLLSQIVDLQKKAKACAveNEELVQHLGAAKD-AQRQLTAELRELEDKYAECMEMLHE 268
Cdd:PRK08476 41 ASIKNDLEKVKTNSS----DVSEIEHEIETILKNAREEA--NKIRQKAIAKAKEeAEKKIEAKKAELESKYEAFAKQLAN 114
|
90
....*....|....
gi 388454134 269 AQEELKNLRNKTMP 282
Cdd:PRK08476 115 QKQELKEQLLSQMP 128
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
70-276 |
5.90e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 70 TERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTplkRNESSSSVQNYFHLDSLQKKL 143
Cdd:COG3096 843 QRRSELerelaqHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEEL---REELDAAQEAQAFIQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 144 KDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLlsqivd 219
Cdd:COG3096 920 AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--------RRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDL------ 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388454134 220 lqkkakacaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECM--------------EMLHEAQEELKNL 276
Cdd:COG3096 986 -----------NEKLRARLEQAEEARREAREQLRQAQAQYSQYNqvlaslkssrdakqQTLQELEQELEEL 1045
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-277 |
6.09e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 140 QKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLV------NDCVKELRDANVQIASISEELAKKTEDAARQQEEITHL 213
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388454134 214 LSQIVDLQKKAKACAVENEELVQHLG-------AAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 277
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
43-277 |
6.81e-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: 39.95 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 43 RLLEEKERDLELAArigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYtSAAEESEPESVCSTPLK 122
Cdd:TIGR00618 504 CPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL-KEQMQEIQQSFSILTQC 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 123 RNESSSSvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTED 202
Cdd:TIGR00618 579 DNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388454134 203 AARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLgaakdaQRQLTAELRELEdkyaECMEMLHEAQEELKNLR 277
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSE------KEQLTYWKEMLA----QCQTLLRELETHIEEYD 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-277 |
8.82e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAA 108
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeSLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 109 E-ESEPESVcstplkRNESSSSVQnyfHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANV 187
Cdd:TIGR02168 870 ElESELEAL------LNERASLEE---ALALLRSELEELSEELRELESKRSELRRE---LEELREKL-AQLELRLEGLEV 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 188 QIASISEELAkktEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAkdaqrQLTA--ELRELEDKYAECMEM 265
Cdd:TIGR02168 937 RIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV-----NLAAieEYEELKERYDFLTAQ 1008
|
250
....*....|..
gi 388454134 266 LHEAQEELKNLR 277
Cdd:TIGR02168 1009 KEDLTEAKETLE 1020
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
180-279 |
8.92e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 180 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQH-------LGAAKDAqRQLTA-- 250
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqLGNVRNN-KEYEAlq 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 388454134 251 --------ELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1579 96 keieslkrRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
26-279 |
9.67e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.07 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 26 ERVGQMTKTYNDIdaVTRLLEEKERDL----ELAARIgqSLLKKNKTLTERNELL---EEQVEHIREEVSQLR--HELSM 96
Cdd:pfam06160 45 EKFEEWRKKWDDI--VTKSLPDIEELLfeaeELNDKY--RFKKAKKALDEIEELLddiEEDIKQILEELDELLesEEKNR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 97 K--DELLQFYtsaaeesepESVCSTPLKRNESSSSVqnyfhLDSLQKKLKDLEEENVVL------------RSEASQLKT 162
Cdd:pfam06160 121 EevEELKDKY---------RELRKTLLANRFSYGPA-----IDELEKQLAEIEEEFSQFeeltesgdyleaREVLEKLEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 163 ETITYEEK-EQ--QLVNDCVKELRDA---------------------NV--QIASISEELAK--------KTEDAARQQE 208
Cdd:pfam06160 187 ETDALEELmEDipPLYEELKTELPDQleelkegyremeeegyalehlNVdkEIQQLEEQLEEnlallenlELDEAEEALE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388454134 209 EITHLLSQIVDL---QKKAKACAVEN-EELVQHLGAAKDAQRQLTAELRELEDKY---AECMEMLHEAQEELKNLRNK 279
Cdd:pfam06160 267 EIEERIDQLYDLlekEVDAKKYVEKNlPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKR 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-279 |
9.87e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 136 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE---DAARQQ----- 207
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEE---YNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREelgERARALyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388454134 208 -----------EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNL 276
Cdd:COG3883 101 svsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE----LEAAKAELEAQ 176
|
...
gi 388454134 277 RNK 279
Cdd:COG3883 177 QAE 179
|
|
| |
