|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
48-372 |
2.64e-164 |
|
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: 482.22 E-value: 2.64e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 48 EEQLPQYKLRVDSLF-LYENQDWA--QSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 125 DLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 205 QGLLQLDMLHEKLRELEEENMALRSkvqfaslssnalwaalgdaEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSR 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRS-------------------EASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 285 MTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQE 364
Cdd:pfam04849 222 LSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQE 301
|
....*...
gi 1907070326 365 EIKELRSK 372
Cdd:pfam04849 302 ELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
433-584 |
1.41e-25 |
|
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: 104.29 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 433 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 495
Cdd:pfam12448 1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 496 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 571
Cdd:pfam12448 79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158
|
170
....*....|...
gi 1907070326 572 PEKLQIVKPLEGS 584
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-369 |
2.98e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 112 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 191
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 192 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEachiKTETFTYEEKEQ--QLVN 269
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE----RRLEDLEEQIEElsEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 270 DCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ 349
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
250 260
....*....|....*....|....
gi 1907070326 350 DRNMECLGMLHE----SQEEIKEL 369
Cdd:TIGR02168 936 VRIDNLQERLSEeyslTLEEAEAL 959
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-370 |
2.12e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 143 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEE 222
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 223 ENMALRSKVQFASLSSNAL---WAAL-----GDAEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSD 294
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAeaeIEELeaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 295 ELL----RYQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 363
Cdd:TIGR02168 842 DLEeqieELSEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
....*..
gi 1907070326 364 EEIKELR 370
Cdd:TIGR02168 922 EKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-417 |
1.90e-06 |
|
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: 51.99 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEesetdsscstplrf 197
Cdd:TIGR02169 210 AERYQALlkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK--RLEEIEQL-------------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 198 nesfslsqgllqLDMLHEKLRELEEENMaLRSKVQFASLSSNAlwAALGDAEAchiktetftyeEKEQQLvNDCVKELRE 277
Cdd:TIGR02169 274 ------------LEELNKKIKDLGEEEQ-LRVKEKIGELEAEI--ASLERSIA-----------EKEREL-EDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 278 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 357
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 358 MLHESQEEIKELRSKsgpsahlcfsqsygvftGESLAAEIEGTMRKKLSLDEESVSKQKA 417
Cdd:TIGR02169 407 ELDRLQEELQRLSEE-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
274-372 |
3.01e-06 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 48.66 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 274 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 353
Cdd:pfam06785 91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160
|
90
....*....|....*....
gi 1907070326 354 ECLGMLHESQEEIKELRSK 372
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-372 |
4.60e-06 |
|
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: 50.84 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 143 LSEQNEALEEQLGQAFDQVNQLQHELskkDELLRIVSIASEESETDSSCSTPL-----RFNESfsLSQGLLQLDMLHEKL 217
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRL---DELSQELSDASRKIGEIEKEIEQLeqeeeKLKER--LEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 218 RELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKEQQLVNDCVKE----LRETNAQMSRMTEELSGKS 293
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAELSKLEEEVSRiearLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070326 294 DELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-421 |
8.20e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 209 QLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiktetftYEEKEQQLVNDCVKELRETNAQMSRMTEE 288
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---------EVEQLEERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 289 LSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKE 368
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907070326 369 LRSKsgpsahlcfsqsygvftGESLAAEIE--GTMRKKLSLDEESVSKQKAQQKR 421
Cdd:TIGR02168 850 LSED-----------------IESLAAEIEelEELIEELESELEALLNERASLEE 887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-466 |
1.08e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 100 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRnhvLSEQNEALEEQLgqafdqvnqlQHELSKKDELLRIVS 179
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN---LERQLEELEAQL----------EELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 180 IASEESETDSSCSTplRFNESFSLSQGLLQldMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachikTETFT 259
Cdd:TIGR02168 341 ELEEKLEELKEELE--SLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASL-------------NNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 260 YEEKEQQLVNDCVKELRETNAQMSRMTEELsgksdELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQR 339
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 340 QLTMELHELQDRNMECLGML--HES-QEEIKEL-RSKSGPSAHL-CFSQSYGVFTGESLAAEI--EGTMRKKLSLDEESV 412
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVENLNAA 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070326 413 S------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG--SNRSSVIMTAKPFESGVQP 466
Cdd:TIGR02168 559 KkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKALSY 620
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
143-350 |
1.64e-05 |
|
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: 48.15 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 143 LSEQN-EALEEQLGQAFDQVNQLQHELSKkdELLRIVSIASEESETDSSCSTPLRFNESFSlsqgllqlDMLHEkLRELE 221
Cdd:pfam04108 109 IDEDSvEILRDALKELIDELQAAQESLDS--DLKRFDDDLRDLQKELESLSSPSESISLIP--------TLLKE-LESLE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 222 EEnMA--LRSKVQFASLSSNALWAALGDaeachiKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRY 299
Cdd:pfam04108 178 EE-MAslLESLTNHYDQCVTAVKLTEGG------RAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907070326 300 QEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQD 350
Cdd:pfam04108 251 IDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
153-372 |
2.08e-05 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 47.39 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 153 QLGQAFDQVNQ----LQHELSKKD--ELLRIVSIAsEESETDSSCSTPlrfneSFSLSQGLLQ-------LDMLHEKLRE 219
Cdd:pfam15294 64 LLRQLFSQAEKwhlkLQADISELEnrELLEQIAEF-EEREFTSSNKKP-----NFELNKPKLEplnegggSALLHMEIER 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 220 LEEENMALRSkvQFASLSSNALwAALGDAEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDEllrY 299
Cdd:pfam15294 138 LKEENEKLKE--RLKTLESQAT-QALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA---S 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 300 QEEISSLLSQIVDLQHKLkehviekeeLRLhlqaskdaQRQLTMELHELQD--------RNMEclGMLHESQEEIKELRS 371
Cdd:pfam15294 212 TALQKSLEEDLASTKHEL---------LKV--------QEQLEMAEKELEKkfqqtaayRNMK--EMLTKKNEQIKELRK 272
|
.
gi 1907070326 372 K 372
Cdd:pfam15294 273 R 273
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-309 |
4.00e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 86 VLAEETFRYMILGTDRV----EQMTKTYNDIDMVTHLLAERDRDLE-LAARIGQALLKRNHVLSEQnEALEEQLGQAFDQ 160
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEI-EELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 161 VNQLQHEL-SKKDELLRIVSIASEESEtdsscstplRFNESF-SLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSS 238
Cdd:TIGR02169 352 RDKLTEEYaELKEELEDLRAELEEVDK---------EFAETRdELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070326 239 NALWAALGDAEACHIKTETFT------YEEKEQQLvNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQ 309
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKedkaleIKKQEWKL-EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-371 |
6.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 197
Cdd:COG1196 212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 198 nesfslsqglLQLDMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachiktetftyEEKEQQLVndcvKELRE 277
Cdd:COG1196 281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRREL-------------------EERLEELE----EELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 278 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 357
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250
....*....|....
gi 1907070326 358 MLHESQEEIKELRS 371
Cdd:COG1196 408 AEEALLERLERLEE 421
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-410 |
1.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 96 ILGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELL 175
Cdd:PRK03918 154 ILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 176 RIVSIASEESEtdsscSTPLRFNESFSLSQGLLQ-LDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachik 254
Cdd:PRK03918 224 EKLEKEVKELE-----ELKEEIEELEKELESLEGsKRKLEEKIRELEERIEELKKEIE---------------------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 255 tetfTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLhlqas 334
Cdd:PRK03918 277 ----ELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEERL----- 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070326 335 kdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSLDEE 410
Cdd:PRK03918 341 ----EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-372 |
1.34e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 113 DMVTHLLAERDRDLE-LAARIGQALLKRNHVLSE----------QNEALEEQLGQAFDQVNQLQHEL--------SKKDE 173
Cdd:pfam15921 267 DRIEQLISEHEVEITgLTEKASSARSQANSIQSQleiiqeqarnQNSMYMRQLSDLESTVSQLRSELreakrmyeDKIEE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 174 LLRIVSIASEESeTDSSCSTPLRFNESFSLSQGLLQLDM-LHEKLREL---EEENMALRSKVQFASLSSNALWAALGDae 249
Cdd:pfam15921 347 LEKQLVLANSEL-TEARTERDQFSQESGNLDDQLQKLLAdLHKREKELsleKEQNKRLWDRDTGNSITIDHLRRELDD-- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 250 achiktetftyEEKEQQLVNDCVKELR-ETNAQMSRMTEELSGKSDELlryqEEISSLLSQIVDLQHKLKEHVIEKEELR 328
Cdd:pfam15921 424 -----------RNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907070326 329 LHLQASKDAQRQLTMELHElQDRNMEClgmlheSQEEIKELRSK 372
Cdd:pfam15921 489 MTLESSERTVSDLTASLQE-KERAIEA------TNAEITKLRSR 525
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
263-373 |
1.59e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 263 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 334
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070326 335 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 373
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-349 |
6.19e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 99 TDRVEQMTKTYNDIDMVTHLLAERDRDL--ELAARIGQALLKrnhvLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLR 176
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 177 IVSIASEESETDsscstplrfnesfsLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiKTE 256
Cdd:TIGR02169 333 KLLAEIEELERE--------------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 257 TFTYEEKEQQLVND-CVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK 335
Cdd:TIGR02169 396 KLKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
250
....*....|....
gi 1907070326 336 DAQRQLTMELHELQ 349
Cdd:TIGR02169 476 EEYDRVEKELSKLQ 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
254-372 |
7.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 254 KTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 333
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070326 334 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
262-372 |
1.30e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 262 EKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL 341
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110
....*....|....*....|....*....|.
gi 1907070326 342 TMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
247-372 |
1.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 247 DAEACHIKTETFTYeekeqqlvNDCVKELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQHKLKEHVIEKEE 326
Cdd:PHA02562 187 DMKIDHIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907070326 327 LRLHLQASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRSK 372
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDK 307
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
124-537 |
1.36e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 124 RDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSL 203
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE-----SEIIELKKSLSS 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 204 SQgLLQLDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachiKTETFTYEEKEQQLVNDCvKELRETNAQMS 283
Cdd:COG5022 918 DL-IENLEFKTELIARLKKLLNNIDLEEG---------------------PSIEYVKLPELNKLHEVE-SKLKETSEEYE 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 284 RM-------TEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK-----DAQRQLTMELHELQDR 351
Cdd:COG5022 975 DLlkkstilVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGL 1054
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 352 NMEclgMLHESQEEIKELRSKSgPSAHLCFSQSYGVFTGESLAAEIEgtMRKKLSLDEESVSKQKAQQKRVFDTVKVAND 431
Cdd:COG5022 1055 LLL---ENNQLQARYKALKLRR-ENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLL 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 432 TRgrsvtfpvllpIPGSNRSSVIMTAKPFESgvqpaEDKTLLSPGGSTEVPGNSQPTNPP---GSPEDSDLATALH---- 504
Cdd:COG5022 1129 QE-----------ISKFLSQLVNTLEPVFQK-----LSVLQLELDGLFWEANLEALPSPPpfaALSEKRLYQSALYdeks 1192
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907070326 505 RLSLRRQNYLSEK-----QFFAEEWERKIQILAEQEEE 537
Cdd:COG5022 1193 KLSSSEVNDLKNElialfSKIFSGWPRGDKLKKLISEG 1230
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-372 |
1.98e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 47 LEEQLPQYKLRVDSLfLYENQDWAQSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDRDL 126
Cdd:COG4717 137 LEAELAELPERLEEL-EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 127 ElaarigqallkrnhVLSEQNEALEEQLGQAFDQ--VNQLQHELSKKDELLRIVS-IASEESETDSSCSTPLRFNESFSL 203
Cdd:COG4717 216 E--------------EAQEELEELEEELEQLENEleAAALEERLKEARLLLLIAAaLLALLGLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 204 SQGLLQLDMLH------------------EKLRELEEEN-MALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKE 264
Cdd:COG4717 282 VLGLLALLFLLlarekaslgkeaeelqalPALEELEEEElEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 265 QQLvndcvkELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQrQLTME 344
Cdd:COG4717 361 EEL------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-ELEEE 433
|
330 340
....*....|....*....|....*...
gi 1907070326 345 LHELQDRnmeclgmLHESQEEIKELRSK 372
Cdd:COG4717 434 LEELEEE-------LEELEEELEELREE 454
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
209-351 |
2.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 209 QLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAeachiKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEE 288
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELN----EQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070326 289 LSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 351
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
130-411 |
3.04e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 130 ARIgQALLKRNHVLSEQnEALEEQlgqafdqVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQ 209
Cdd:PLN02939 150 ARL-QALEDLEKILTEK-EALQGK-------INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 210 LDMLHEKLRELEEENMALRSKVQFASlssnalwaalgdAEACHIK-TETFTYE-EKEQQLVNDCVKELRetnAQMSRMTE 287
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLK------------AELIEVAeTEERVFKlEKERSLLDASLRELE---SKFIVAQE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 288 ELSgKSDELlryqeEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNM--ECLGMLHESQEE 365
Cdd:PLN02939 286 DVS-KLSPL-----QYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskFSSYKVELLQQK 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907070326 366 IKELRSKSGPSAHLCFSQsygVFTGESLAAEIEGTMRKklsLDEES 411
Cdd:PLN02939 360 LKLLEERLQASDHEIHSY---IQLYQESIKEFQDTLSK---LKEES 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-369 |
3.74e-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: 41.21 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 176 RIVSIASEESETDSSC---STPLRFNESFSLSQgLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAch 252
Cdd:TIGR02169 640 RMVTLEGELFEKSGAMtggSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 253 iKTETFtyeEKEQQLVNDcvkELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ 332
Cdd:TIGR02169 717 -KIGEI---EKEIEQLEQ---EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907070326 333 ASKdaQRQLTMELHELQDRNMECLGMLHESQEEIKEL 369
Cdd:TIGR02169 790 HSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
119-388 |
3.95e-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: 40.52 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 119 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEESEtdsscstplrfn 198
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA--ELAELEKEIAE------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 199 esfslsqgllqldmLHEKLRELEEEnmaLRSKVQFASLSSNALWAALGdaeachIKTETFTYEEKEQQLVNDCVKELRET 278
Cdd:COG4942 95 --------------LRAELEAQKEE---LAELLRALYRLGRQPPLALL------LSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 279 NAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGM 358
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEAL 228
|
250 260 270
....*....|....*....|....*....|
gi 1907070326 359 LHESQEEIKELRSKSGPSAhlcFSQSYGVF 388
Cdd:COG4942 229 IARLEAEAAAAAERTPAAG---FAALKGKL 255
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-372 |
4.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 229 SKVQFASLSSNALWAALGDAEAC---HIKTETFTYEEKEQQLvNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISS 305
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAAlseQLRKALFELDKLQEEL-EQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070326 306 LLSQIVDLQHKLKEHV-------IEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG4372 85 LNEQLQAAQAELAQAQeeleslqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-349 |
6.01e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 104 QMTKTYNDIDMVTHLLAERDRDLELAARigQA-LLKRNHVLSEQNEALEEQLgqafdQVNQLQHELSKKDELLRIVSIAS 182
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLER--QAeKAERYKELKAELRELELAL-----LVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 183 EESETDSScstplrfnesfslsqgllQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTetftYEE 262
Cdd:TIGR02168 253 EELEELTA------------------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-QKQI----LRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 263 KEQQLVNDcVKELRETNAQMSRMTEELSgksDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLT 342
Cdd:TIGR02168 310 RLANLERQ-LEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
....*..
gi 1907070326 343 MELHELQ 349
Cdd:TIGR02168 386 SKVAQLE 392
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
100-372 |
6.15e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 100 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVS 179
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 180 iaseesetdsscstplRFNESFSLSQGLLQLD-MLHEKLRELEEENMALRSKVQFASLSS-NALWAALGDAEAC-----H 252
Cdd:PRK01156 253 ----------------RYESEIKTAESDLSMElEKNNYYKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKkqilsN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 253 IKTETFTYEEKEQQLVNdcVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ 332
Cdd:PRK01156 317 IDAEINKYHAIIKKLSV--LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907070326 333 ASKDAQR----QLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:PRK01156 395 EILKIQEidpdAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-372 |
7.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 139 RNHVLsEQNEALE--EQLGQAFDQVNQLQHELSK----KDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDM 212
Cdd:COG4913 214 REYML-EEPDTFEaaDALVEHFDDLERAHEALEDareqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 213 LHEKLRELEEENMALRSKVQFASlssnalwAALGDAEAchiktetfTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGK 292
Cdd:COG4913 293 LEAELEELRAELARLEAELERLE-------ARLDALRE--------ELDELEAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 293 SDELLRYQEEISSLLSQIVDLQHKLKEHvieKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
248-369 |
7.51e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 248 AEACHIKtETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKS---DELLRYQEEISSLLSQIVDLQHKLKEHV--I 322
Cdd:PRK04778 331 EEIDRVK-QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQLEEIEKEQEKLSEMLqgL 409
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907070326 323 EKEELRLHlQASKDAQRQLTMELHELQDRNM-----ECLGMLHESQEEIKEL 369
Cdd:PRK04778 410 RKDELEAR-EKLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEAL 460
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
208-372 |
7.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 208 LQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiktetfTYEEKEQqlvndcvkELRETNAQMSRMTE 287
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK--------EIKRLEL--------EIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070326 288 ELSG--KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGmlhESQEE 365
Cdd:COG1579 81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAE 157
|
....*..
gi 1907070326 366 IKELRSK 372
Cdd:COG1579 158 LEELEAE 164
|
|
| |
