|
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 |
5.95e-154 |
|
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: 453.33 E-value: 5.95e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 22 VLCAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELL 101
Cdd:pfam04849 52 LLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 102 QFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKE 181
Cdd:pfam04849 132 QIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 182 LRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 261
Cdd:pfam04849 212 LSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAE 291
|
250
....*....|....*...
gi 1154491805 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 |
7.90e-74 |
|
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: 238.72 E-value: 7.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 340 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDIGNVVLDNKTNSIILETEAADLGNDERSKKPGTPGTPGSH 419
Cdd:pfam12448 1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 420 DLETALRRLSLRRENYLSERRFFEEEQERKLQELAE----KGELRSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 495
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157
|
170
....*....|....
gi 1154491805 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 |
3.52e-15 |
|
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: 80.10 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 38 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 117
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 118 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 194
Cdd:TIGR02168 777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 195 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 267
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925
|
250
....*....|..
gi 1154491805 268 EAQEELKNLRNK 279
Cdd:TIGR02168 926 QLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-279 |
1.59e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 25 AERVGQMTKTYNDIDAVTRLL--EEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQ 102
Cdd:COG1196 212 AERYRELKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 103 FYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcVKEL 182
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----EEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 183 RDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 262
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250
....*....|....*..
gi 1154491805 263 MEMLHEAQEELKNLRNK 279
Cdd:COG1196 448 AEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-278 |
3.67e-12 |
|
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: 70.47 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE 109
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 110 ESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETityEEKEQQLVnDCVKELRDANVQI 189
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI---AATERRLE-DLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 190 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEA 269
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----LELR 930
|
....*....
gi 1154491805 270 QEELKNLRN 278
Cdd:TIGR02168 931 LEGLEVRID 939
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-279 |
3.17e-10 |
|
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: 64.32 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 26 ERVGQMTKTYNDID-AVTRLLEEKERDLELAARIGQslLKKnktltERNELLEEQvEHIREEVSQLRHELS--------- 95
Cdd:TIGR02169 650 EKSGAMTGGSRAPRgGILFSRSEPAELQRLRERLEG--LKR-----ELSSLQSEL-RRIENRLDELSQELSdasrkigei 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 96 MKD-ELLQFYTSAA----EESEPE-SVCSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEE 169
Cdd:TIGR02169 722 EKEiEQLEQEEEKLkerlEELEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 170 KE-QQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQL 248
Cdd:TIGR02169 794 PEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
250 260 270
....*....|....*....|....*....|.
gi 1154491805 249 TAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERK 904
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-319 |
1.45e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.69 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKKTEDAARQQEEITHLLS 215
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN----EQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 216 QIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME-----MLHEAQEELKNLRNKTMPNTTSRRYH 290
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180
....*....|....*....|....*....
gi 1154491805 291 SLGLFPMDSLAAEIEGTMRKELQLEEAES 319
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-279 |
2.71e-09 |
|
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: 61.23 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 25 AERvgQMTKTYNDIDAVTRLLEEKERDLELaarigqslLKKNKTLTERNELLEEQVEHIREEVSQLRHElSMKDELLQFY 104
Cdd:TIGR02168 177 TER--KLERTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLRLE-ELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 105 TSAAEESEpesvcstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRD 184
Cdd:TIGR02168 246 EELKEAEE----------------------ELEELTAELQELEEKLEELRLEVSELEEE----IEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 185 ANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECME 264
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250
....*....|....*
gi 1154491805 265 MLHEAQEELKNLRNK 279
Cdd:TIGR02168 380 QLETLRSKVAQLELQ 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-318 |
4.69e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 25 AERVGQMTKTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKD 98
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 99 E----LLQFYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL 174
Cdd:PRK03918 293 EeyikLSEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 175 VN--------------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHlgA 240
Cdd:PRK03918 372 EElerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--H 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 241 AKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTsrryhslgLFPMDSLAAEIEGTMRK--ELQLEEAE 318
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKELEEKlkKYNLEELE 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-225 |
2.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 45 LEEKERDLELAarigQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstplKRN 124
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---------LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 125 ESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEK----EQQLVNDCVKELRDANVQIASISEELAKKT 200
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 1154491805 201 EDAARQQEEITHLLSQIVDLQKKAK 225
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-279 |
6.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 49 ERDLELAARIgQSLlKKNKTLTE--RNELLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 111
Cdd:COG4913 191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 112 EpesvcstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIAS 191
Cdd:COG4913 269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 192 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:COG4913 335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414
|
250 260
....*....|....*....|
gi 1154491805 260 AECMEMLHEAQEELKNLRNK 279
Cdd:COG4913 415 RDLRRELRELEAEIASLERR 434
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
45-284 |
8.47e-08 |
|
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: 55.88 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 45 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDEllqfytsaAEESEPESVCSTPLKRN 124
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKE 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 125 ESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAS--------------QLKTETITYEEKEQQLVNDCVKELRDA 185
Cdd:pfam05483 587 KQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSaenkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDK 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 186 NVQIASISEELAKK---TEDAARQQEEI----THLLSQIVDLQKKAKACAVE-NEELVQHLGAAKDAQRQ-------LTA 250
Cdd:pfam05483 667 KISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKiIEERDSELGLYKNKEQEqssakaaLEI 746
|
250 260 270
....*....|....*....|....*....|....
gi 1154491805 251 ELRELEDKYAECMEMLHEAQEELKNLRNKTMPNT 284
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-297 |
1.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEENVVLRSEASQLktetityeEKEQQLVNDcVKELRDANVQIASISEELAK---KTEDAARQQEEITH 212
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKL--------EKLLQLLPL-YQELEALEAELAELPERLEEleeRLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 213 LLSQIVDLQKK-AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHS 291
Cdd:COG4717 168 LEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
....*.
gi 1154491805 292 LGLFPM 297
Cdd:COG4717 248 ARLLLL 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-342 |
4.16e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 180 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 260 AECMEML--HEAQEELKNLRNKTMPNTTSRRYHSLGLFpMDSLAAEIEgTMRKELQLEEAESPDITHQKRVFETVRNINQ 337
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAE-ELRADLAELAALRAELEAERAELEALLAELE 184
|
....*
gi 1154491805 338 VVKQR 342
Cdd:COG4942 185 EERAA 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-318 |
6.64e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 33 KTYNDIDAvtrLLEEKER-DLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 111
Cdd:PRK03918 362 ELYEEAKA---KKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 112 epeSVCSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEASQLktETITYEEKEQQLVNDCVKELRDANVQIA 190
Cdd:PRK03918 439 ---PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELAEQLKELEEKLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 191 SIS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 269
Cdd:PRK03918 514 KYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1154491805 270 QEELKNLRNKTMPNTTSRRYHSLGLFPMDSLAAEIEGTmRKELQLEEAE 318
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKR 641
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-343 |
6.71e-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: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 38 IDAVTRLLEEKERDLELAArigqslLKKNKTLTERNELLEEqVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvc 117
Cdd:TIGR02169 197 RQQLERLRREREKAERYQA------LLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISELE----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 118 stplKRNESSSSVqnyfhLDSLQKKLKDL-EEENVVLRSEASQLKTETI----TYEEKEQQLvNDCVKELRDANVQIASI 192
Cdd:TIGR02169 265 ----KRLEEIEQL-----LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELreledkyaecmEMLHEAQEE 272
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----------EKLKREINE 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 273 LKnlRNKTMPNTTSRRYHSLGLFpmdsLAAEIEGTMRKELQLEEAESpdiTHQKRVFETVRNINQVVKQRS 343
Cdd:TIGR02169 404 LK--RELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLAADLS 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9-275 |
1.13e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 9 YYELDWYYEECSDVLCAERVGQMTKTYndiDAVTRL--------LEEKERDLELAAR--IGQSLLKKNKTLTERNELLEE 78
Cdd:COG4913 548 RAWLEAELGRRFDYVCVDSPEELRRHP---RAITRAgqvkgngtRHEKDDRRRIRSRyvLGFDNRAKLAALEAELAELEE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 79 QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplkrnESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEAS 158
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWDE----------IDVASAER--EIAELEAELERLDASSDDLAALEE 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 159 QLktetityeEKEQQLVNDCVKELRDANVQIASISEELakktEDAARQQEEITHLLSQIVDLqkkakACAVENEELVQHL 238
Cdd:COG4913 693 QL--------EELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDL-----ARLELRALLEERF 755
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1154491805 239 GAA------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 275
Cdd:COG4913 756 AAAlgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-283 |
2.13e-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: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 38 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREE--VSQLRHELSMKDELLQfytsAAEESEPEs 115
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELE----RLDASSDD- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 116 vcstplkrnessssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCvKELRDANVQIASIS-- 193
Cdd:COG4913 687 --------------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLArl 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 194 ------EELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEEL-----------VQHLGAAKDAQRQLTAELRELE 256
Cdd:COG4913 746 elrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPEYLALLDRLE 825
|
250 260
....*....|....*....|....*..
gi 1154491805 257 DkyaecmEMLHEAQEELKNLRNKTMPN 283
Cdd:COG4913 826 E------DGLPEYEERFKELLNENSIE 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-319 |
2.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 43 RLLEEKERdLELAARIGQSLLKKNKTLTErnelLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE----ESEPESVCS 118
Cdd:PRK03918 443 RELTEEHR-KELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 119 TPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEASQ---LKTETITYEEKEQQL---VNDCVKELRDANVQIASI 192
Cdd:PRK03918 518 EELEKKAEE--------YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELeeeLAELLKELEELGFESVEE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemlheaqEE 272
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EE 660
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1154491805 273 LKNLRNKTMpnTTSRRYHSL--GLFPMDSLAAEIEGTMRK-ELQLEEAES 319
Cdd:PRK03918 661 YEELREEYL--ELSRELAGLraELEELEKRREEIKKTLEKlKEELEEREK 708
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
67-276 |
2.92e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 67 KTLTERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESV--CSTPLKRNESSSSvqnyfHLDS 138
Cdd:PRK04863 841 QLNRRRVELeraladHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVeeIREQLDEAEEAKR-----FVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 139 LQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLL 214
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--------RDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154491805 215 SQivdLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:PRK04863 988 EK---LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-342 |
3.41e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 33 KTYNDIDAVTRLLEEKERDLE-LAARIG--QSLLKKNKtltERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE 109
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEkFIKRTEniEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 110 ESEpesvcstPLKRNESsssvqnyfhldSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQI 189
Cdd:PRK03918 239 EIE-------ELEKELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 190 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKacavENEELVQHLGAAKDAQRQLTAELRELEdKYAECMEMLHEA 269
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAK 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154491805 270 QEELKNLRNKtmpnttsrryhsLGLFPMDSLAAEIEGTMRKELQLEEAEspdithqKRVFETVRNINQVVKQR 342
Cdd:PRK03918 371 KEELERLKKR------------LTGLTPEKLEKELEELEKAKEEIEEEI-------SKITARIGELKKEIKEL 424
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
46-268 |
3.43e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 46 EEKERDLE-LAARIGQSLLKKNKTLTERNELLEEqVEHIREEVSQLRHELsmkDELLQfyTSAAEESEPESVCStplkrn 124
Cdd:PRK02224 247 EERREELEtLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEER---DDLLA--EAGLDDADAEAVEA------ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 125 essssvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvNDCVKELRDanvQIASISEELAKKTEDAA 204
Cdd:PRK02224 315 ----------RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 205 RQQEEITHLLSQIVDLQKKAKACAVE-------NEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 268
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDlgnaedfLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
30-281 |
3.62e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 30 QMTKTYNDIDAVTRLLEE-KERDLELaarigQSLLKKNKTltERNELLEeQVEHIREEVSQLRhelSMKDELLQFYTSAA 108
Cdd:COG1340 9 SLEELEEKIEELREEIEElKEKRDEL-----NEELKELAE--KRDELNA-QVKELREEAQELR---EKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 109 EEsepesvcstplkRNESSSSVQNYF-HLDSLQKKLKDLEEENV---VLRSEASQL----KTETITyEEKEQQLVNdcvk 180
Cdd:COG1340 78 EE------------RDELNEKLNELReELDELRKELAELNKAGGsidKLRKEIERLewrqQTEVLS-PEEEKELVE---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 181 elrdanvQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKD----------------- 243
Cdd:COG1340 141 -------KIKELEKEL-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEemielykeadelrkead 212
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1154491805 244 -AQRQLT---AELRELEDKYAECMEMLHEAQEELKNLRNKTM 281
Cdd:COG1340 213 eLHKEIVeaqEKADELHEEIIELQKELRELRKELKKLRKKQR 254
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
42-276 |
3.66e-06 |
|
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: 50.74 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 42 TRLLEEKERDLELAARIGQsllkknKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpl 121
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE------- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 122 kRNE----SSSSVQNY-FHLDSLQKKLKDLEEEnvvlrsEASQLKTETITYEEKEQQLVndcVKELRDANVQiasiseEL 196
Cdd:TIGR00618 720 -FNEienaSSSLGSDLaAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVT---AALQTGAELS------HL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 197 AKKTEDAARQQEEITHLLSQI-VDLQKKAK----ACAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAECMEMLHE 268
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLeAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQ 863
|
....*...
gi 1154491805 269 AQEELKNL 276
Cdd:TIGR00618 864 LTQEQAKI 871
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-279 |
4.96e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 32 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEeQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 110
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 111 SEPE-SVCSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEASQLKTETIT-YEEKEQQL---------VNDCV 179
Cdd:PRK03918 537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 180 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKK-------------------AKACAVENEELVQHLGA 240
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelreeylelsreLAGLRAELEELEKRREE 691
|
250 260 270
....*....|....*....|....*....|....*....
gi 1154491805 241 AKDAQRQLTAELRELEdKYAECMEMLHEAQEELKNLRNK 279
Cdd:PRK03918 692 IKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREK 729
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
31-279 |
5.63e-06 |
|
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: 50.36 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 31 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMK-------DELLQF 103
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELlrdeqeeIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 104 YTSAAEESEPESvcstpLKRNESSSSVQNYfhLDSLQKKLKDLEEEnvvLRSEASQLKTETITYEEKEQQLVNDCVKELR 183
Cdd:pfam02463 259 EIEKEEEKLAQV-----LKENKEEEKEKKL--QEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 184 DANVQIASISEELAKKTEDAARQQEEIThllsQIVDLQKKAKAcavENEELVQHLGAAKDAQRQLTAELRELEDKYAECM 263
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEE----EEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250
....*....|....*.
gi 1154491805 264 EMLHEAQEELKNLRNK 279
Cdd:pfam02463 402 EEEKEAQLLLELARQL 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-276 |
6.58e-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: 50.02 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 48 KERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTS---AAEESEPESVcsTPLKRN 124
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIK--KQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 125 EsSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQ-----LKTETITYEEKEQQLVNDCV---KELRDANVQIASISEEL 196
Cdd:TIGR04523 273 Q-KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISqnnKIISQLNEQISQLKKEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 197 AKKTEDAARQQEEITHLLSQIVDLQKkakacavENEELvqhlgaaKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKK-------ENQSY-------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
135-279 |
9.23e-06 |
|
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: 48.00 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 135 HLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE--DAARQQEEITH 212
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEAR---LEAAKTEL-EDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154491805 213 LLSQI-------VDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1579 94 LQKEIeslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
45-279 |
1.08e-05 |
|
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: 48.41 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 45 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS----MKDELlqfytsaaeesepESVCSTp 120
Cdd:pfam09728 13 LDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailAKSKL-------------EKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 121 lkrnessssvqnyfhldsLQKKLKDLEEENVVLRSEASQLKTETItyeEKEQQLVND---CVKELRDANVQIASISEELA 197
Cdd:pfam09728 79 ------------------LQKQNKKLKEESKKLAKEEEEKRKELS---EKFQSTLKDiqdKMEEKSEKNNKLREENEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 198 KKTEDAARQQEeithLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEM---LHEAQEELK 274
Cdd:pfam09728 138 EKLKSLIEQYE----LRELHFEKLLKTK-------ELEVQLAEAKLQQATEEEEKKAQEKEVAKARELkaqVQTLSETEK 206
|
....*
gi 1154491805 275 NLRNK 279
Cdd:pfam09728 207 ELREQ 211
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
26-279 |
1.16e-05 |
|
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: 49.08 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 26 ERVGQMTKTYNDIdaVTRLLEEKERDL----ELAARIgqSLLKKNKTLTERNELL---EEQVEHIREEVSQLR--HELSM 96
Cdd:pfam06160 45 EKFEEWRKKWDDI--VTKSLPDIEELLfeaeELNDKY--RFKKAKKALDEIEELLddiEEDIKQILEELDELLesEEKNR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 97 K--DELLQFYtsaaeesepESVCSTPLKRNESSSSVqnyfhLDSLQKKLKDLEEENVVL------------RSEASQLKT 162
Cdd:pfam06160 121 EevEELKDKY---------RELRKTLLANRFSYGPA-----IDELEKQLAEIEEEFSQFeeltesgdyleaREVLEKLEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 163 ETITYEEK-EQ--QLVNDCVKELRDA---------------------NV--QIASISEELAK--------KTEDAARQQE 208
Cdd:pfam06160 187 ETDALEELmEDipPLYEELKTELPDQleelkegyremeeegyalehlNVdkEIQQLEEQLEEnlallenlELDEAEEALE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154491805 209 EITHLLSQIVDL---QKKAKACAVEN-EELVQHLGAAKDAQRQLTAELRELEDKY---AECMEMLHEAQEELKNLRNK 279
Cdd:pfam06160 267 EIEERIDQLYDLlekEVDAKKYVEKNlPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKR 344
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
78-276 |
1.19e-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: 48.61 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 78 EQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEA 157
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ------LAALERR--------IAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 158 SQLKTETITYEEKEQQLVNDCVKELRDANVQ------------------------IASISEELAKKTEDAARQQEEITHL 213
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154491805 214 LSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-287 |
1.19e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 38 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAE-----ES 111
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRREEIEEleeeiEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 112 EPESVCSTPLKRNESSSsvqnyfHLDSLQKKLKDLEEENVVLRS----------EASQLKTE---------------TIT 166
Cdd:PRK02224 396 LRERFGDAPVDLGNAED------FLEELREERDELREREAELEAtlrtarerveEAEALLEAgkcpecgqpvegsphVET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 167 YEEKEQQlVNDCVKELRDANVQIASISEEL--AKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDa 244
Cdd:PRK02224 470 IEEDRER-VEELEAELEDLEEEVEEVEERLerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA- 547
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1154491805 245 qrQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSR 287
Cdd:PRK02224 548 --ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
53-277 |
1.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 53 ELAARIGQSLLK--KNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstplkrnESSSSV 130
Cdd:COG3206 148 ELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---------EAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 131 QNyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCV-----KELRDANVQIASISEELAKKTEDAAR 205
Cdd:COG3206 219 QQ---LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154491805 206 QQEEITHLLSQIVDLQKKAKAcAVENEelvqhLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLR 277
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILA-SLEAE-----LEALQAREASLQAQLAQLEARLAE----LPELEAELRRLE 357
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
68-279 |
1.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 68 TLTERnellEEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESvcstpLKRNESSSSVQNYFHLDSLQKKLKDL 146
Cdd:PRK02224 469 TIEED----RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 147 EEenvvLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKK 223
Cdd:PRK02224 540 EE----LRERAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREK 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 224 AKACAVENEELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:PRK02224 615 REALAELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
42-275 |
2.16e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 42 TRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIrEEVSQLrhelsmKDELLQFYTSAAEESEPEsvcstpL 121
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQ------KDEQIKKLQQEKELLEKE------I 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 122 KRNESSSSVQNyfhldslqKKLKDLEEENVVLRSEASQLKTETityEEKEQQLvndcvKELrdaNVQIASISEELAKKTE 201
Cdd:TIGR04523 429 ERLKETIIKNN--------SEIKDLTNQDSVKELIIKNLDNTR---ESLETQL-----KVL---SRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154491805 202 DAARQQEEITHLLSQIVDLQKKAKacaveneELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 275
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVK-------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
40-328 |
2.27e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 40 AVTRLLEEKERDLELAARIGQSL---LKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQfytsAAEESEpes 115
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLrkaLFELDKLQEELEQLREELEQAREELEQLEEELeQARSELEQ----LEEELE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 116 vcstplKRNESSSSVQNYfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelrdaNVQIASISEE 195
Cdd:COG4372 84 ------ELNEQLQAAQAE--LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-----------EAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 196 LAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVEN-EELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELK 274
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1154491805 275 NLRNKTMPNTTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEEAESPDITHQKRV 328
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
42-276 |
2.74e-05 |
|
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: 47.86 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 42 TRLLEEKERDLELAARIGQSLLKKNKTL-TERNELLEE--QVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcs 118
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALeSENAELQAElrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 119 tplkRNESSSSVQNyfHLDSLQKKLKDLEEENVVLRSEASQLK-----TETITYEEKEQQLVNDcvKELRDANVQIASIS 193
Cdd:pfam01576 431 ----LAEKLSKLQS--ELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLS--TRLRQLEDERNSLQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 194 EELAKKTEDAARQQEEITHLLSQIVDLQKKAK--ACAVENEElvqhlGAAKDAQRQLTAELRELEDKyAECMEMLHEA-- 269
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEedAGTLEALE-----EGKKRLQRELEALTQQLEEK-AAAYDKLEKTkn 576
|
....*....
gi 1154491805 270 --QEELKNL 276
Cdd:pfam01576 577 rlQQELDDL 585
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-276 |
2.86e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 40 AVTRLLEEKERDLE-LAARIGQsllKKNKTLTER-NEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 111
Cdd:PRK02224 177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 112 EP---------ESVCSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEASqlktetitYEEKEQQLVNDCVKEL 182
Cdd:PRK02224 254 ETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 183 RDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 262
Cdd:PRK02224 320 ED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250
....*....|....
gi 1154491805 263 MEMLHEAQEELKNL 276
Cdd:PRK02224 397 RERFGDAPVDLGNA 410
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-279 |
3.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 123 RNESS-SSVQNYFH---LDSLQKKLKDLeeenvvLRSEASQLKTETITYEEKEQQLvndcvKELRDANVQIASISEELAK 198
Cdd:COG4717 31 PNEAGkSTLLAFIRamlLERLEKEADEL------FKPQGRKPELNLKELKELEEEL-----KEAEEKEEEYAELQEELEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 199 KTEDAARQQEEITHLLSQIVDLQKkakacAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemLHEAQEELKNLRN 278
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEA 170
|
.
gi 1154491805 279 K 279
Cdd:COG4717 171 E 171
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
56-269 |
4.05e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 56 ARIgQSLLKKNKTLTERnelleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESVCSTPLK-RNE-SSSSVQNY 133
Cdd:PLN02939 150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 134 FHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNdCVKE--LRDANVQiasiseELAKKTEDAarqQEEIt 211
Cdd:PLN02939 219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 212 hllSQIVDLQKKAKACAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA 269
Cdd:PLN02939 288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEA 343
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-226 |
5.66e-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: 46.30 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkdELLQFYTSAAE 109
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 110 ESEPESVcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQI 189
Cdd:COG4942 119 QPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154491805 190 ASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 226
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-342 |
5.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 180 KELRDANVQIasisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQR--QLTAELRELED 257
Cdd:COG4717 71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 258 KYAEcmemLHEAQEELKNLRNKtmpnttsrryhslglfpMDSLAAEIEgtmRKELQLEEA-ESPDITHQKRVFETVRNIN 336
Cdd:COG4717 147 RLEE----LEERLEELRELEEE-----------------LEELEAELA---ELQEELEELlEQLSLATEEELQDLAEELE 202
|
....*.
gi 1154491805 337 QVVKQR 342
Cdd:COG4717 203 ELQQRL 208
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-274 |
6.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQ-------------------------IA 190
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 191 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 270
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....
gi 1154491805 271 EELK 274
Cdd:COG3883 206 AAAE 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
36-226 |
9.47e-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: 45.53 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 36 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS--------MKDELLQF---- 103
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 104 YTSAAEESEPESVCSTPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL--- 174
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeal 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154491805 175 VNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 226
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-226 |
9.93e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 29 GQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS-MKDELLQFytsa 107
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdLEDELNKD---- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 108 aeesepesvcSTPLKRNESSSSVqnyfhlDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKeqqlVNDCVKELRDANV 187
Cdd:TIGR04523 551 ----------DFELKKENLEKEI------DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE----KKDLIKEIEEKEK 610
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154491805 188 QIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKA 226
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-279 |
1.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHlls 215
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE---LEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154491805 216 QIVDLQKKAKACAVEN--------EELVQHLGAAK---DAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
43-211 |
1.13e-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: 44.53 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 43 RLLEEKERDLELA--ARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstp 120
Cdd:COG1579 8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 121 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKT 200
Cdd:COG1579 80 ----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|.
gi 1154491805 201 EDAARQQEEIT 211
Cdd:COG1579 152 AELEAELEELE 162
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-378 |
1.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE---DAARQQ----- 207
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEE---YNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREelgERARALyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 208 -----------EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:COG3883 101 svsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 277 RNKtmpnttsrryhslglfpMDSLAAEIEGTMRKELQLE-EAESPDITHQKRVFETVRNINQVVKQRSLTPSPMNIPGSN 355
Cdd:COG3883 181 EAL-----------------LAQLSAEEAAAEAQLAELEaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 1154491805 356 QSSAMNSLLSSCVSTPRSSFYGS 378
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-317 |
1.23e-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: 45.14 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELAKKTEDAARQ------ 206
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 207 ---QEEITHLLSQ--IVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL----- 276
Cdd:COG4942 116 lgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALealka 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154491805 277 -RNKTMPNTTSRRyhslglfpmDSLAAEIEGTMRKELQLEEA 317
Cdd:COG4942 196 eRQKLLARLEKEL---------AELAAELAELQQEAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-279 |
1.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 36 NDIDAVTRLLEEKERDLELAARIG--------QSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELsmkDELLQFYTSA 107
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEEL---EQLENELEAA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 108 AEESEPESVCST--------------------------------------PLKRNESSSSVQNYFHLDSLQKKLKDLEEE 149
Cdd:COG4717 240 ALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 150 NvvLRSEASQLKTETITYEEKEQQLVNDcVKELRDANVQIASISEELAKKTEDAARQQ----------EEITHLLSQIVD 219
Cdd:COG4717 320 E--LEELLAALGLPPDLSPEELLELLDR-IEELQELLREAEELEEELQLEELEQEIAAllaeagvedeEELRAALEQAEE 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154491805 220 LQKKAKACAVENEELVQHLGAAKDAQR-----QLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAE 461
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
37-280 |
1.96e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 37 DIDAVTRLLEEkerdlELAARigQSLLKKNKTLTErnelleeQVEHIREEVSQLRHELsmkDELLQFYTSAAEESEpesv 116
Cdd:PRK04778 290 RIDQLYDILER-----EVKAR--KYVEKNSDTLPD-------FLEHAKEQNKELKEEI---DRVKQSYTLNESELE---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 117 cstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEasqLKTETITYEEKEQQLvNDCVKELRDANVQIASISEEL 196
Cdd:PRK04778 349 ------------------SVRQLEKQLESLEKQYDEITER---IAEQEIAYSELQEEL-EEILKQLEEIEKEQEKLSEML 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 197 AKKTEDAARQQEEITHLLSQIVDLQKKakacaVEN-------EELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEA 269
Cdd:PRK04778 407 QGLRKDELEAREKLERYRNKLHEIKRY-----LEKsnlpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
250
....*....|.
gi 1154491805 270 QEELKNLRNKT 280
Cdd:PRK04778 482 TEDVETLEEET 492
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
74-279 |
2.80e-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: 44.65 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 74 ELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPL---------KRNESSSSVQNyfHLDSLQKKLK 144
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvfqteaELQEFISDLQS--KLRLAPDKLK 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 145 DLEEEnvvlRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEeithLLSQIVDLQKKA 224
Cdd:TIGR00606 713 STESE----LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET----LLGTIMPEEESA 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 225 KACAVENEELVQHLGAAKDAQR---QLTAELR--ELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERkiaQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-277 |
2.99e-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: 44.66 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAA 108
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeSLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 109 E-ESEPESVcstplkRNESSSSVQnyfHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvNDCVKELRDANV 187
Cdd:TIGR02168 870 ElESELEAL------LNERASLEE---ALALLRSELEELSEELRELESKRSELRRE---LEELREKL-AQLELRLEGLEV 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 188 QIASISEELAkktEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAkdaqrQLTA--ELRELEDKYAECMEM 265
Cdd:TIGR02168 937 RIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV-----NLAAieEYEELKERYDFLTAQ 1008
|
250
....*....|..
gi 1154491805 266 LHEAQEELKNLR 277
Cdd:TIGR02168 1009 KEDLTEAKETLE 1020
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
43-277 |
3.15e-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: 44.57 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 43 RLLEEKERDLELAArigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYtSAAEESEPESVCSTPLK 122
Cdd:TIGR00618 504 CPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL-KEQMQEIQQSFSILTQC 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 123 RNESSSSvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTED 202
Cdd:TIGR00618 579 DNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154491805 203 AARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLgaakdaQRQLTAELRELEdkyaECMEMLHEAQEELKNLR 277
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSE------KEQLTYWKEMLA----QCQTLLRELETHIEEYD 717
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
121-255 |
3.44e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.51 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 121 LKRNES-SSSVQNyfHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKK 199
Cdd:pfam10473 12 LKESERkADSLKD--KVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMA----QNLRDLELDLVTLRSEKENL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154491805 200 TEDAARQQEEITHLLSQIVDLQKKAKacaVENEELVQHLGAAKDAQRQLTAELREL 255
Cdd:pfam10473 86 TKELQKKQERVSELESLNSSLENLLE---EKEQEKVQMKEESKTAVEMLQTQLKEL 138
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
180-279 |
3.69e-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: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 180 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQH-------LGAAKDAqRQLTA-- 250
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqLGNVRNN-KEYEAlq 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 1154491805 251 --------ELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1579 96 keieslkrRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
39-273 |
3.81e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 39 DAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS-MKDELLQFYTSAAEesepesvc 117
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEaLEDQHGAFLDADIE-------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 118 stplkrnessSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLVNDCVKElrdanvqIASISEELA 197
Cdd:pfam12128 341 ----------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK---YNRRRSKIKEQNNRD-------IAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 198 KKTEDAARQQEEITHLL----SQIVDLQKKAKACAVENEE-LVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEE 272
Cdd:pfam12128 401 KIREARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYrLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREE 479
|
.
gi 1154491805 273 L 273
Cdd:pfam12128 480 Q 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-277 |
3.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 40 AVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRhelsmKDELLQFYTSAAEEsepesvcst 119
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-----IAALLAEAGVEDEE--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 120 plkrnESSSSVQNYFHLDSLQKKLKDLEEEnvvLRSEASQLKTETITYEEKEQQlvndcvKELRDANVQIASISEELAKK 199
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQ---LEELLGELEELLEALDEEELE------EELEELEEELEELEEELEEL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 200 TEDAARQQEEITHLlsqivdlqkkakacavENEELVQHLgaaKDAQRQLTAELRELEDKYAECM---EMLHEAQEELKNL 276
Cdd:COG4717 452 REELAELEAELEQL----------------EEDGELAEL---LQELEELKAELRELAEEWAALKlalELLEEAREEYREE 512
|
.
gi 1154491805 277 R 277
Cdd:COG4717 513 R 513
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
77-259 |
4.43e-04 |
|
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: 43.53 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 77 EEQVEHIREEVSQLRHEL-----SMKDELLQFYTSAAEesePESVCSTPLKRNESSSSVQNYFH-LDSLQKKLKDLEE-- 148
Cdd:pfam04108 111 EDSVEILRDALKELIDELqaaqeSLDSDLKRFDDDLRD---LQKELESLSSPSESISLIPTLLKeLESLEEEMASLLEsl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 149 ----ENVVLRSEASQ-LKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKK 223
Cdd:pfam04108 188 tnhyDQCVTAVKLTEgGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSR 267
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154491805 224 AKACAVENEELVQHLGAAKDAQRQLTAELRELEDKY 259
Cdd:pfam04108 268 LPEYLAALKEFEERWEEEKETIEDYLSELEDLREFY 303
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
53-276 |
5.17e-04 |
|
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: 44.01 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 53 ELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkDELLQFytsaaeesepesvcstplKRNESSssvqn 132
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT--EQLEQA------------------KRNKAN----- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 133 yfhldsLQKKLKDLEEENVVLRSEA---SQLKTETITYEEKEQQLVNDCVKELRDANVQiasiSEELAKKTEDAARQQEE 209
Cdd:pfam01576 375 ------LEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQ----RAELAEKLSKLQSELES 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 210 ITHLLSQI-VDLQKKAKACAVENEEL--VQHLGAAKDAQR-QLTAELRELEDKYAECMEMLHEAQEELKNL 276
Cdd:pfam01576 445 VSSLLNEAeGKNIKLSKDVSSLESQLqdTQELLQEETRQKlNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
30-322 |
5.70e-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: 43.81 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 30 QMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELL-QFYTSAA 108
Cdd:pfam02463 670 ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLkQKIDEEE 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 109 EESEPESVCSTPLKRNESSSSVQ--------NYFHLDSLQ----KKLKDLEEEN---------VVLRSEASQLKTE--TI 165
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKekelaeerEKTEKLKVEeekeEKLKAQEEELraleeelkeEAELLEEEQLLIEqeEK 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 166 TYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQE-EITHLLSQIVDLQKKAKACAVENEELVQhlgaaKDA 244
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELlLKEEELEEQKLKDELESKEEKEKEEKKE-----LEE 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154491805 245 QRQLTAELRELEDKYAECMEMlhEAQEELKNLRNKTMPNTTSRRyhSLGLFPMDSLAAEIEGTmRKELQLEEAESPDI 322
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIKE--EAEILLKYEEEPEELLLEEAD--EKEKEENNKEEEEERNK-RLLLAKEELGKVNL 977
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
133-281 |
5.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 133 YFHLDSLQKKLKDLEEENVVL----RSEASQLKTETIT-YEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQ 207
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154491805 208 EeithllsqivDLQKKakacaveNEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTM 281
Cdd:PRK12704 103 E----------LLEKR-------EEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
70-276 |
6.54e-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: 43.40 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 70 TERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTplkRNESSSSVQNYFHLDSLQKKL 143
Cdd:COG3096 843 QRRSELerelaqHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEEL---REELDAAQEAQAFIQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 144 KDLEEENVVLRSEASQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLlsqivd 219
Cdd:COG3096 920 AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--------RRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDL------ 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 220 lqkkakacaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECM--------------EMLHEAQEELKNL 276
Cdd:COG3096 986 -----------NEKLRARLEQAEEARREAREQLRQAQAQYSQYNqvlaslkssrdakqQTLQELEQELEEL 1045
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
43-279 |
7.47e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 43 RLLEEKERDL---ELAARIGQSLLKKNKTLTERNELLEEQ----VEHIREEVSQLRHELSMKDEL-LQFYTSAAEESEpe 114
Cdd:COG5022 833 RETEEVEFSLkaeVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVELAERQLQELKIDVKSISSLkLVNLELESEIIE-- 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 115 svcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEEN--VVLRSEASQLKTETITYEEKEQQLvNDCVKELRDANVQIASI 192
Cdd:COG5022 911 ------LKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKL-KETSEEYEDLLKKSTIL 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEElVQHLGAAKDAQRQLTAELR---ELEDKYAECMEMLHEA 269
Cdd:COG5022 984 VREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE-VAELQSASKIISSESTELSilkPLQKLKGLLLLENNQL 1062
|
250
....*....|
gi 1154491805 270 QEELKNLRNK 279
Cdd:COG5022 1063 QARYKALKLR 1072
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
39-316 |
7.58e-04 |
|
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: 43.02 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 39 DAVTRLLEEKErDLELAARIGQSLLKKNktLTERNELLEEQVEHIREEVSQLRHELSMKDELLQF--YTSAAEES-EPES 115
Cdd:COG5185 253 DKLEKLVEQNT-DLRLEKLGENAESSKR--LNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeeQLAAAEAEqELEE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 116 vcstplKRNESSSSVQNYFHldSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEqqlvndcvkELRDANVQIASISEE 195
Cdd:COG5185 330 ------SKRETETGIQNLTA--EIEQGQESLTENLEAIKEEIENIVGEVELSKSSE---------ELDSFKDTIESTKES 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 196 LAKKTEDAARQQEEIthllsqivdlqkkakacaveNEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 275
Cdd:COG5185 393 LDEIPQNQRGYAQEI--------------------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNK 452
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1154491805 276 LRNKTMPNTTSR-RYHSLGLFpmDSLAAEIEGTMRKELQLEE 316
Cdd:COG5185 453 VMREADEESQSRlEEAYDEIN--RSVRSKKEDLNEELTQIES 492
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-277 |
7.58e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 140 QKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLV------NDCVKELRDANVQIASISEELAKKTEDAARQQEEITHL 213
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 214 LSQIVDLQKKAKACAVENEELVQHLG-------AAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLR 277
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
136-279 |
7.60e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 136 LDSLQKKLKDLEEEnvvlRSEASQ---LKTEtitYEEKEQQLVndcVKELRDANVQIASISEELAKKTEDAARQQEEITH 212
Cdd:COG1196 195 LGELERQLEPLERQ----AEKAERyreLKEE---LKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154491805 213 LLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
190-282 |
9.26e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.44 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 190 ASISEELAKKTEDAArqqeEITHLLSQIVDLQKKAKACAveNEELVQHLGAAKD-AQRQLTAELRELEDKYAECMEMLHE 268
Cdd:PRK08476 41 ASIKNDLEKVKTNSS----DVSEIEHEIETILKNAREEA--NKIRQKAIAKAKEeAEKKIEAKKAELESKYEAFAKQLAN 114
|
90
....*....|....
gi 1154491805 269 AQEELKNLRNKTMP 282
Cdd:PRK08476 115 QKQELKEQLLSQMP 128
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-264 |
1.36e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 29 GQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHI-------REEVSQLRHELSM-KDEL 100
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKlKREI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 101 lqfytsaaeesepesvcsTPLKRNES---SSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVND 177
Cdd:TIGR02169 402 ------------------NELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 178 cvkelrdanvqIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAC---AVENEELVQHLGAAKDAQRQLTAELRE 254
Cdd:TIGR02169 464 -----------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeerVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
250
....*....|
gi 1154491805 255 LEDKYAECME 264
Cdd:TIGR02169 533 VGERYATAIE 542
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
44-277 |
1.77e-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: 42.08 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 44 LLEEKERDLELAARIGQsLLKKNKTLTERNELLEEQVEHIRE---EVSQLRHELSMK----DELLQFYTSAAEESEPESV 116
Cdd:pfam01576 14 LQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARkqelEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 117 CSTPLKRN------------ESSSSVQNYFHLD--SLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKE- 181
Cdd:pfam01576 93 QLQNEKKKmqqhiqdleeqlDEEEAARQKLQLEkvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 182 --------LRDANVQIASISEELAKKTEDAARQQE--------EITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQ 245
Cdd:pfam01576 173 ekakslskLKNKHEAMISDLEERLKKEEKGRQELEkakrklegESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
250 260 270
....*....|....*....|....*....|..
gi 1154491805 246 RQLTAELRELEDKYAECMEMLHEAQEELKNLR 277
Cdd:pfam01576 253 EEETAQKNNALKKIRELEAQISELQEDLESER 284
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
67-279 |
2.33e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 67 KTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNY--FH--LDSLQKK 142
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAktIKaeIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 143 LKDLEEENV-------VLRSEASQLKT--ETITYEEK---EQQLVNDCVKELRDANVQIASISE---ELAKKTEDAARQQ 207
Cdd:PHA02562 243 LLNLVMDIEdpsaalnKLNTAAAKIKSkiEQFQKVIKmyeKGGVCPTCTQQISEGPDRITKIKDklkELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154491805 208 EEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 279
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
181-279 |
3.74e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 181 ELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcAVE--NEELvqhlgaAKDA---QRQLTAELREL 255
Cdd:COG1842 31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEkgREDL------AREAlerKAELEAQAEAL 103
|
90 100
....*....|....*....|....
gi 1154491805 256 EDKYAECMEMLHEAQEELKNLRNK 279
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESK 127
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
168-276 |
4.20e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 39.35 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 168 EEKEQQLVNDCVKELRDANVQiASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKAcavENEELVQHLGAAKDAQRQ 247
Cdd:PRK14160 11 ENMEEDCCKENENKEEDKGKE-EDLEFEEIEKEEIIEDSEESNEVKIEELKDENNKLKE---ENKKLENELEALKDRLLR 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1154491805 248 LTAEL--------RELEDKYAE-CMEMLHEAQEELKNL 276
Cdd:PRK14160 87 TVAEYdnyrkrtaKEKEGIYSDaCEDVLKELLPVLDNL 124
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
37-261 |
5.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 37 DIDAVTRLLEEKerdLELAARIGQSLLKKNK-TLTERNELLEEQVEHIREEVSQLRhelSMKDELLQFytsaaeESEPES 115
Cdd:PHA02562 185 TLDMKIDHIQQQ---IKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIE---ELTDELLNL------VMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 116 VCSTPLKRNESSSSVQNyfHLDSLQKKLKdLEEENVVLRSEASQLKTETITYEEKEQQLVNdCVKELRDANVQIasisEE 195
Cdd:PHA02562 253 PSAALNKLNTAAAKIKS--KIEQFQKVIK-MYEKGGVCPTCTQQISEGPDRITKIKDKLKE-LQHSLEKLDTAI----DE 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154491805 196 LAKKTEDAARQQEEITHLLSQI-------VDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 261
Cdd:PHA02562 325 LEEIMDEFNEQSKKLLELKNKIstnkqslITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
36-261 |
5.78e-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: 40.13 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 36 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEs 115
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 116 vcstpLKRNESSSSVQnyfhLDSLQKkLKDLEEENVVLRSE-ASQLktetityeEKEQQLVNDCVKELRDANVQIASISE 194
Cdd:COG4942 99 -----LEAQKEELAEL----LRALYR-LGRQPPLALLLSPEdFLDA--------VRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154491805 195 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAEL----RELEDKYAE 261
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeaEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
36-261 |
5.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 36 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELsmKDELLQFYTSAAEESEPES 115
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 116 VcstpLkrneSSSSVQNYfhLDSLQKkLKDLEEENvvlRSEASQLKTETITYEEKEQQLVndcvKELRDANVQIAsiseE 195
Cdd:COG3883 108 L----L----GSESFSDF--LDRLSA-LSKIADAD---ADLLEELKADKAELEAKKAELE----AKLAELEALKA----E 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154491805 196 LAKKTEDAARQQEEITHLLSQIVDLQKKAKAcavENEELVQHLGAAKDAQRQLTAELRELEDKYAE 261
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEA---QLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
30-261 |
6.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 30 QMTKTYNDIDAVTRLLEEKERDLElaarigqsllKKNKTLTERNELL---EEQVEHIREEVSQLRHELSMKDELLQFYTS 106
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELE----------QLEEELEQARSELeqlEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 107 AAEESEPEsvcstplkrnessssvqnyfhLDSLQKKLKDLEEENVVLRSEASQLKTEtitYEEKEQQLvndcvKELRDan 186
Cdd:COG4372 109 EAEELQEE---------------------LEELQKERQDLEQQRKQLEAQIAELQSE---IAEREEEL-----KELEE-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154491805 187 vQIASISEELAKKTEDaaRQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAE 261
Cdd:COG4372 158 -QLESLQEELAALEQE--LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
38-162 |
7.34e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 38 IDAVTRLLEEKERDLEL--AARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYT---SAAEESE 112
Cdd:COG2433 378 IEEALEELIEKELPEEEpeAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLErelSEARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1154491805 113 PESVcstpLKRNESSSsvqnyfhLD----SLQKKLKDLEEENVVLRSEASQLKT 162
Cdd:COG2433 458 RREI----RKDREISR-------LDreieRLERELEEERERIEELKRKLERLKE 500
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
108-277 |
7.73e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 39.43 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 108 AEESEPESVCSTPLKRNESSSSVQNyfhldsLQKKLKDLEEENVVLRSEASQLKTETITYEEKEqqlvndcvKELRDANV 187
Cdd:pfam09755 1 ASESDTSSVDGGPTLAPPSPVTREQ------LQKRIESLQQENRVLKMELETYKLRCKALQEEN--------RALRQASV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 188 QIAS--------ISEELAKKTEDAARQQEEITHLLSQ-----IVDLQKKAKACAVENEELVQHLGaaKDAQRQLTAELRE 254
Cdd:pfam09755 67 NIQAkaeqeeefISNTLLKKIQALKKEKETLAMNYEQeeeflTNDLSRKLTQLRQEKVELEQTLE--QEQEYQVNKLMRK 144
|
170 180
....*....|....*....|...
gi 1154491805 255 LEDKYAEcmemLHEAQEELKNLR 277
Cdd:pfam09755 145 IEKLEAE----TLNKQTNLEQLR 163
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
44-256 |
7.76e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 44 LLEEKERDLELaarIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLR--HELSMKDELLQFYTSAAEESEPESVCSTPL 121
Cdd:pfam17045 50 TLERKHKEIGL---LRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKrsYEKLQRKQLKEAREEAKSREEDRSELSRLN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 122 KRNESsssvqnyFHLDSL---------QKKLKDLEEENVVLRSEASQLKTETityeEKEQQLVNDCVKELRDANVQiaSI 192
Cdd:pfam17045 127 GKLEE-------FRQKSLeweqqrlqyQQQVASLEAQRKALAEQSSLIQSAA----YQVQLEGRKQCLEASQSEIQ--RL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154491805 193 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELE 256
Cdd:pfam17045 194 RSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQVLQNELMELK 257
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
65-280 |
7.80e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 65 KNKTLTERNELLEEQVE----HIREEVSQLRHeLSMKDELLQFYTSaaeesepesvcstpLKR--NESSSSvqnyfHLDS 138
Cdd:PRK04778 24 RKRNYKRIDELEERKQElenlPVNDELEKVKK-LNLTGQSEEKFEE--------------WRQkwDEIVTN-----SLPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 139 LQKKLKDLEEENVVLR-SEASQLKTETityeekEQQLvndcvkelRDANVQIASISEELAKKTEDAARQQEEITHLLSQI 217
Cdd:PRK04778 84 IEEQLFEAEELNDKFRfRKAKHEINEI------ESLL--------DLIEEDIEQILEELQELLESEEKNREEVEQLKDLY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154491805 218 VDLQKKAKAcavENEElvqhLGaakDAQRQLTAELRELEDKYAEcMEML-----H-EAQEELKNLRNKT 280
Cdd:PRK04778 150 RELRKSLLA---NRFS----FG---PALDELEKQLENLEEEFSQ-FVELtesgdYvEAREILDQLEEEL 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
185-276 |
7.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491805 185 ANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAecme 264
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---- 82
|
90
....*....|..
gi 1154491805 265 mlhEAQEELKNL 276
Cdd:COG3883 83 ---ERREELGER 91
|
|
| |
