|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
48-353 |
7.24e-168 |
|
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: 490.69 E-value: 7.24e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 48 EEQLPQYKLRVDSLF-LYENQDWA--QSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 125 DLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 205 QGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEI 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070332 285 SSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
414-565 |
1.57e-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: 103.90 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 414 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 476
Cdd:pfam12448 1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 477 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 552
Cdd:pfam12448 79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158
|
170
....*....|...
gi 1907070332 553 PEKLQIVKPLEGS 565
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-351 |
2.34e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 112 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 191
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 192 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKAcHIKTETftyEEKEQQLVNDCVKELRETNAQMSRMteels 271
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRER---LESLERRIAATERRLEDLEEQIEEL----- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 272 gksdellryQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 344
Cdd:TIGR02168 851 ---------SEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
....*..
gi 1907070332 345 EEIKELR 351
Cdd:TIGR02168 922 EKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-398 |
2.20e-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: 55.07 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEesetdsscstplrf 197
Cdd:TIGR02169 210 AERYQALlkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK--RLEEIEQL-------------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 198 nesfslsqgllqLDMLHEKLREL-EEENMALRSKACHIKTETF----TYEEKEQQLvNDCVKELRETNAQMSRMTEELSG 272
Cdd:TIGR02169 274 ------------LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 273 KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 352
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907070332 353 KsgpsahlcfsqsygvftGESLAAEIEGTMRKKLSLDEESVSKQKA 398
Cdd:TIGR02169 421 E-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-391 |
1.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 96 ILGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELL 175
Cdd:PRK03918 154 ILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 176 RIVSIASEESEtdsscSTPLRFNESfslsqgLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvndcvKE 255
Cdd:PRK03918 224 EKLEKEVKELE-----ELKEEIEEL------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 256 LRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLhlqaskdaqRQLTMELHELQDRNME 335
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEERL---------EELKKKLKELEKRLEE 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070332 336 clgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSLDEE 391
Cdd:PRK03918 357 ----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
255-353 |
3.02e-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: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 255 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 334
Cdd:pfam06785 91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160
|
90
....*....|....*....
gi 1907070332 335 ECLGMLHESQEEIKELRSK 353
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-447 |
3.76e-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: 50.83 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 102 VEQMTKTYNDIDMVTHLLAE-RDRDLELAARIgQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSI 180
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEElRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 181 ASEESETDSSCSTplrfNESFSLSQgllQLDMLHEKLRELEEENMALRSKachiktetftYEEKEQQL------VNDCVK 254
Cdd:TIGR02168 331 KLDELAEELAELE----EKLEELKE---ELESLEAELEELEAELEELESR----------LEELEEQLetlrskVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 255 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQ-------------------IVDLQHKLKEHVIEKEELRLHLQAS 315
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelqaeleeleeeLEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 316 KDAQRQLTMELHELQDRNMECLGML--HES-QEEIKEL-RSKSGPSAHL-CFSQSYGVFTGESLAAEI--EGTMRKKLSL 388
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVE 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070332 389 DEESVS------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG--SNRSSVIMTAKPFESGVQP 447
Cdd:TIGR02168 554 NLNAAKkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKALSY 620
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-353 |
5.88e-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: 50.45 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 143 LSEQNEALEEQLGQAFDQVNQLQHELSKK--DELLRIVS-IASEESETdSSCSTPLRFNESfslsqgllQLDMLHEKLRE 219
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEkIGELEAEI-ASLERSIAEKER--------ELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 220 LEEENMALRSKACHIKTETFTYEEKEQQLVNDcVKELRETNAQMSRMTEELSGKS----DELLRYQEEISsllsqivDLQ 295
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEE-YAELKEELEDLRAELEEVDKEFaetrDELKDYREKLE-------KLK 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070332 296 HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 353
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-352 |
1.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 197
Cdd:COG1196 212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 198 nesfslsqglLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEELSGKSDEL 277
Cdd:COG1196 281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070332 278 LRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 352
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-330 |
2.58e-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: 48.13 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 104 QMTKTYNDIDMVTHLLAERDRD---LELAARIGQALLKRN--------HVLSEQNEALEEQLGQAFDQVNQLQHELSKKD 172
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQlksLERQAEKAERYKELKaelrelelALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 173 ELLRIVSIASEESEtdsscstpLRFNEsfslsqgllqldmLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDc 252
Cdd:TIGR02168 260 AELQELEEKLEELR--------LEVSE-------------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ- 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070332 253 VKELRETNAQMSRMTEELSgksDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ 330
Cdd:TIGR02168 318 LEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
216-353 |
2.77e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 216 KLRELEEENMALRSKACHIKTETFTYeekeqqlvNDCVKELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQ 295
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELT 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070332 296 HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRSK 353
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDK 307
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
124-518 |
7.65e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 124 RDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSL 203
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE-----SEIIELKKSLSS 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 204 SQgLLQLDMLHEKLRELEEENMALRSKAchIKTETFTYEEKEQQLVNDCvKELRETNAQMSRM-------TEELSGKSDE 276
Cdd:COG5022 918 DL-IENLEFKTELIARLKKLLNNIDLEE--GPSIEYVKLPELNKLHEVE-SKLKETSEEYEDLlkkstilVREGNKANSE 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 277 LLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK-----DAQRQLTMELHELQDRNMEclgMLHESQEEIKELR 351
Cdd:COG5022 994 LKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGLLLL---ENNQLQARYKALK 1070
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 352 SKSgPSAHLCFSQSYGVFTGESLAAEIEgtMRKKLSLDEESVSKQKAQQKRVFDTVKVANDTRgrsvtfpvllpIPGSNR 431
Cdd:COG5022 1071 LRR-ENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQE-----------ISKFLS 1136
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 432 SSVIMTAKPFESgvqpaEDKTLLSPGGSTEVPGNSQPTNPP---GSPEDSDLATALH----RLSLRRQNYLSEK-----Q 499
Cdd:COG5022 1137 QLVNTLEPVFQK-----LSVLQLELDGLFWEANLEALPSPPpfaALSEKRLYQSALYdeksKLSSSEVNDLKNElialfS 1211
|
410
....*....|....*....
gi 1907070332 500 FFAEEWERKIQILAEQEEE 518
Cdd:COG5022 1212 KIFSGWPRGDKLKKLISEG 1230
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
143-331 |
8.55e-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: 45.84 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 143 LSEQN-EALEEQLGQAFDQVNQLQHELSK-----KDELLRIVS-IASEESETDSSCSTPLRFNESFSLSQGLLQL----- 210
Cdd:pfam04108 109 IDEDSvEILRDALKELIDELQAAQESLDSdlkrfDDDLRDLQKeLESLSSPSESISLIPTLLKELESLEEEMASLleslt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 211 ---DMLHEKLRELEEEnmalrskachiKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSL 287
Cdd:pfam04108 189 nhyDQCVTAVKLTEGG-----------RAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSA 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907070332 288 LSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQD 331
Cdd:pfam04108 258 LQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
207-353 |
8.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 207 LLQLDMLHEKLRELEEEnmalrskachiktetftyEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISS 286
Cdd:COG1196 231 LLKLRELEAELEELEAE------------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070332 287 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 353
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-322 |
1.05e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 118 LLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSscstplrf 197
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 198 nesfslsqgllQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDEL 277
Cdd:COG4717 140 -----------ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907070332 278 LRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLHLQASKDAQRQL 322
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLL 251
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
211-350 |
1.07e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 211 DMLHEKLRELEEENMALRSKACHIKtETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKS---DELLRYQEEISSL 287
Cdd:PRK04778 313 DTLPDFLEHAKEQNKELKEEIDRVK-QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQ 391
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 288 LSQIVDLQHKLKEHV--IEKEELRLHlQASKDAQRQLTMELHELQDRNM-----ECLGMLHESQEEIKEL 350
Cdd:PRK04778 392 LEEIEKEQEKLSEMLqgLRKDELEAR-EKLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEAL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-340 |
1.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 118 LLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLgqafDQVNQLQHELSKKDEllRIVSIASEESETDsscstplrf 197
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEE--ELEELEAELEELR--------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 198 NESFSLSQgLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvNDCVKELRETNAQMSRMTEELS-GKSDE 276
Cdd:COG4717 116 EELEKLEK-LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL-EELEAELAELQEELEELLEQLSlATEEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070332 277 LLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRlhlqaSKDAQRQLTMELHELQDRNMECLGML 340
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELE-----EELEQLENELEAAALEERLKEARLLL 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
202-332 |
1.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 202 SLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMTEELSGKSDELL 278
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907070332 279 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 332
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-402 |
1.25e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 143 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETdsscstplrfnesfslsqgllQLDMLHEKLRELEE 222
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR---------------------QISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 223 EnmalrskachiktetftyEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHV 302
Cdd:TIGR02168 741 E------------------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 303 IEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKsgpsahlcfsqsygvftGESLAAEIE--G 380
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-----------------IESLAAEIEelE 865
|
250 260
....*....|....*....|..
gi 1907070332 381 TMRKKLSLDEESVSKQKAQQKR 402
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEE 887
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
153-353 |
1.41e-04 |
|
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: 44.70 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 153 QLGQAFDQVNQ----LQHELSKKD--ELLRIVSIAsEESETDSSCSTPlrfneSFSLSQGLLQ-------LDMLHEKLRE 219
Cdd:pfam15294 64 LLRQLFSQAEKwhlkLQADISELEnrELLEQIAEF-EEREFTSSNKKP-----NFELNKPKLEplnegggSALLHMEIER 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 220 LEEENMALRSKachikteTFTYEEKeqqlVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEeISSLLSQI----VDLQ 295
Cdd:pfam15294 138 LKEENEKLKER-------LKTLESQ----ATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKE-ISDLEEKMaalkSDLE 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 296 HKLKEHVIEKEELRLHLQASK----DAQRQLTMELHELQD--------RNMEclGMLHESQEEIKELRSK 353
Cdd:pfam15294 206 KTLNASTALQKSLEEDLASTKhellKVQEQLEMAEKELEKkfqqtaayRNMK--EMLTKKNEQIKELRKR 273
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-353 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 113 DMVTHLLAERDRDLE-LAARIGQALLKRNHVLSE----------QNEALEEQLGQAFDQVNQLQHEL--------SKKDE 173
Cdd:pfam15921 267 DRIEQLISEHEVEITgLTEKASSARSQANSIQSQleiiqeqarnQNSMYMRQLSDLESTVSQLRSELreakrmyeDKIEE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 174 LLRIVSIASEESeTDSSCSTPLRFNESFSLSQGLLQLDM-LHEKLREL---EEENMAL--RSKACHIKTETFTYE----E 243
Cdd:pfam15921 347 LEKQLVLANSEL-TEARTERDQFSQESGNLDDQLQKLLAdLHKREKELsleKEQNKRLwdRDTGNSITIDHLRRElddrN 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 244 KEQQLVNDCVKELR-ETNAQMSRMTEELSGKSDELlryqEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL 322
Cdd:pfam15921 426 MEVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL 501
|
250 260 270
....*....|....*....|....*....|.
gi 1907070332 323 TMELHElQDRNMEClgmlheSQEEIKELRSK 353
Cdd:pfam15921 502 TASLQE-KERAIEA------TNAEITKLRSR 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-330 |
1.58e-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: 45.83 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 86 VLAEETFRYMILGTDRV----EQMTKTYNDIDMVTHLLAERDRDLE-LAARIGQALLKRNHVLSEQnEALEEQLGQAFDQ 160
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEI-EELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 161 VNQLQHEL-SKKDELLRIVSIASEESEtdsscstplRFNESF-SLSQGLLQLDMLHEKLRELEEENMALrskachiktet 238
Cdd:TIGR02169 352 RDKLTEEYaELKEELEDLRAELEEVDK---------EFAETRdELKDYREKLEKLKREINELKRELDRL----------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 239 ftyeekeqqlvndcVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDA 318
Cdd:TIGR02169 412 --------------QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250
....*....|..
gi 1907070332 319 QRQLTMELHELQ 330
Cdd:TIGR02169 478 YDRVEKELSKLQ 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-353 |
1.65e-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: 45.44 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 119 LAERDRDLELAARIG--QALL-----KRNHVLSEQNEAL------EEQLGQAFDQVNQLQHELSKKDELLrivsiasEES 185
Cdd:TIGR02169 670 RSEPAELQRLRERLEglKRELsslqsELRRIENRLDELSqelsdaSRKIGEIEKEIEQLEQEEEKLKERL-------EEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 186 ETD-SSCSTPLRFNESfSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYE-EKEQQLVNDCVKELRETNAQM 263
Cdd:TIGR02169 743 EEDlSSLEQEIENVKS-ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 264 SRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHES 343
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250
....*....|
gi 1907070332 344 QEEIKELRSK 353
Cdd:TIGR02169 902 ERKIEELEAQ 911
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
244-354 |
1.71e-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: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 244 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 315
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070332 316 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 354
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-353 |
7.39e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 235 KTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 314
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070332 315 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 353
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-355 |
1.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 119 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSK-KDELLRIVSIASEESETdsscstpLRF 197
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKEKAEEY-------IKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 198 NEsfslsqgllQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDEL 277
Cdd:PRK03918 299 SE---------FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070332 278 lryqEEISSLLSQIVDLQHKLKEHviEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKSG 355
Cdd:PRK03918 365 ----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
101-350 |
1.14e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.15 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 101 RVEQ-MTKTYNDIDMVTHLLAERDRdlelaaRIG---------QALLKRNHVLSEQNEALEEQLGQAFDQVNQL---QHE 167
Cdd:pfam03148 82 RLEKaLEALEEPLHIAQECLTLREK------RQGidlvhdeveKELLKEVELIEGIQELLQRTLEQAWEQLRLLraaRHK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 168 LSK----KDELLRIVSIASEESETDSSCS---TPLRFNESFSLSQGLLQL--DMLHEKLRELeEENMALRSKACHIKTET 238
Cdd:pfam03148 156 LEKdlsdKKEALEIDEKCLSLNNTSPNISykpGPTRIPPNSSTPEEWEKFtqDNIERAEKER-AASAQLRELIDSILEQT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 239 FTYEEKEQQLVNDcvkELRETNAQMSRMTEELsgkSDELLRYQEEISSLLSQIVDLQHKL--KEHVIEKEELRLHLQAS- 315
Cdd:pfam03148 235 ANDLRAQADAVNF---ALRKRIEETEDAKNKL---EWQLKKTLQEIAELEKNIEALEKAIrdKEAPLKLAQTRLENRTYr 308
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907070332 316 ------KD-AQRQLTMELHELQDrNMECL-GMLHESQEEIKEL 350
Cdd:pfam03148 309 pnvelcRDeAQYGLVDEVKELEE-TIEALkQKLAEAEASLQAL 350
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
130-392 |
1.32e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 130 ARIgQALLKRNHVLSEQnEALEEQlgqafdqVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQ 209
Cdd:PLN02939 150 ARL-QALEDLEKILTEK-EALQGK-------INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 210 LDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVndcvkELRETNAQMSRMTEELSGKsdeLLRYQEEISSLLS 289
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVF-----KLEKERSLLDASLRELESK---FIVAQEDVSKLSP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 290 QIVD--------LQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNM--ECLGMLHESQEEIKELRSKSGPSAH 359
Cdd:PLN02939 293 LQYDcwwekvenLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskFSSYKVELLQQKLKLLEERLQASDH 372
|
250 260 270
....*....|....*....|....*....|...
gi 1907070332 360 LCFSQsygVFTGESLAAEIEGTMRKklsLDEES 392
Cdd:PLN02939 373 EIHSY---IQLYQESIKEFQDTLSK---LKEES 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-353 |
1.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 116 THLLAERDrdleLAARIGQAL-----LKRNH----VLSEQNEALEeQLGQAFDQVNQLQHELSKKDELLRIVsiaseese 186
Cdd:COG4913 215 EYMLEEPD----TFEAADALVehfddLERAHealeDAREQIELLE-PIRELAERYAAARERLAELEYLRAAL-------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 187 tdsscstPLRFNEsfsLSQGLLQ--LDMLHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLVNDCVKELRETNAQMS 264
Cdd:COG4913 282 -------RLWFAQ---RRLELLEaeLEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 265 RMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHvieKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 344
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
....*....
gi 1907070332 345 EEIKELRSK 353
Cdd:COG4913 426 AEIASLERR 434
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
215-350 |
1.49e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.34 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 215 EKLRELEEENMALRSKAcHIKTETftYEE---KEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQI 291
Cdd:pfam10168 575 QELQSLEEERKSLSERA-EKLAEK--YEEikdKQEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAI 651
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070332 292 VDLQHKlkehvieKEELRLHLQASKDAQRQLTMELHELQDRNMEclGMLHESQEEIKEL 350
Cdd:pfam10168 652 KQAKKK-------MNYQRYQIAKSQSIRKKSSLSLSEKQRKTIK--EILKQLGSEIDEL 701
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
27-351 |
1.65e-03 |
|
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: 42.40 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 27 ESITDVCSNEDLPEVELVNLLEEqlpqyklrvDSLFLYENQDWAQSSHQQQDAPETLSPVLA--EETFRYMILGTDRVEQ 104
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAE---------DEKLLDEKKQFEKIAEELKGKEQELIFLLQarEKEIHDLEIQLTAIKT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 105 MTKTYND--IDMVTHLLAERDRDLELAARIGQALLKRNHVLSE---------------------------QNEALEEQLG 155
Cdd:pfam05483 465 SEEHYLKevEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtlelkkhqediinckkqeermlkQIENLEEKEM 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 156 QAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGL----LQLDMLHEKLRELEEENMALRSKA 231
Cdd:pfam05483 545 NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCnnlkKQIENKNKNIEELHQENKALKKKG 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 232 CHIKTETFTYE--------------EKEQQLVNDCVKELRETNAQMSRMTEELSGK---SDELLRYQEEI----SSLLSQ 290
Cdd:pfam05483 625 SAENKQLNAYEikvnklelelasakQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAE 704
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070332 291 IVDLQHKLK---EHVIEKEELRLHLQASKDAQRQ-----LTMELHELQDRNMECLGMLHESQEEIKELR 351
Cdd:pfam05483 705 MVALMEKHKhqyDKIIEERDSELGLYKNKEQEQSsakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLK 773
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
119-353 |
1.84e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 119 LAERDRDLELAARIGQALLKRnhvlseqneaLEEQLGQAFDQVNQLQHELSK-KDELLRIVSIASEESETDSSCSTPLRF 197
Cdd:pfam05667 231 LASRLTPEEYRKRKRTKLLKR----------IAEQLRSAALAGTEATSGASRsAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 198 NESfslsqgllqldmlhEKLRELEEENMALRSKACHIKTETFTYEEKE------QQLVNDCVKELRETNAQMSRMTEELS 271
Cdd:pfam05667 301 THT--------------EKLQFTNEAPAATSSPPTKVETEEELQQQREeeleelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 272 GKSDELLRYQEEISSLLSQIvdlqhKLKEHVIE--------KEELRLHLQASKD-----------AQRQLTMELHELQDR 332
Cdd:pfam05667 367 QVEEELEELKEQNEELEKQY-----KVKKKTLDllpdaeenIAKLQALVDASAQrlvelagqwekHRVPLIEEYRALKEA 441
|
250 260
....*....|....*....|....
gi 1907070332 333 NMEclgMLHESQ---EEIKELRSK 353
Cdd:pfam05667 442 KSN---KEDESQrklEEIKELREK 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-351 |
1.98e-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: 41.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 209 QLDMLH------EKLRELEEEnmaLRSKACHIKTETFTYEEKEQQLVNdcvKELRETNAQMSRMTEELSGKSDELLRYQE 282
Cdd:TIGR02168 201 QLKSLErqaekaERYKELKAE---LRELELALLVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070332 283 EISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL-------TMELHELQDRNMECLGMLHESQEEIKELR 351
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLerqleelEAQLEELESKLDELAEELAELEEKLEELK 350
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
119-369 |
2.90e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 119 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSScstplrfn 198
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 199 esfSLSQGLLQLDMLHEKLRELEEENMALRSkachiktETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELL 278
Cdd:COG4942 101 ---AQKEELAELLRALYRLGRQPPLALLLSP-------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 279 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGMLHESQEEIKELRSKSGPSA 358
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
250
....*....|.
gi 1907070332 359 hlcFSQSYGVF 369
Cdd:COG4942 248 ---FAALKGKL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-353 |
3.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 119 LAERDRDLElAARIGQALLKRNHVLSEQNEALEEQLGQaFDQvnqlqHELSKKDELLRIVSIASEESETDSScstplRFN 198
Cdd:PRK03918 478 LRKELRELE-KVLKKESELIKLKELAEQLKELEEKLKK-YNL-----EELEKKAEEYEKLKEKLIKLKGEIK-----SLK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 199 ESFSLSQGLL-QLDMLHEKLRELEEENMALRSKACHIKTETFT-YEEKEQQL---------VNDCVKELRETNAQMSRMT 267
Cdd:PRK03918 546 KELEKLEELKkKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAEKELEREEKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 268 EELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHviEKEELR-LHLQASKDAQRqLTMELHELQDRNMECLGMLHESQEE 346
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELReEYLELSRELAG-LRAELEELEKRREEIKKTLEKLKEE 702
|
....*..
gi 1907070332 347 IKELRSK 353
Cdd:PRK03918 703 LEEREKA 709
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
213-353 |
4.68e-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: 39.52 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 213 LHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLvNDCVKELRETNAQMSRMTEELSG--KSDELLRYQEEISSLLSQ 290
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTE---LEDLEKEI-KRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070332 291 IVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGmlhESQEEIKELRSK 353
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAE 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
208-352 |
4.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 208 LQLDMLHEKLRELEEENMALRSKAchIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMT-EELSGKSDELLRYQEEISS 286
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKEL--RELEKVLKKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070332 287 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMEClgmLHESQEEIKELRS 352
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEP 599
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-352 |
5.95e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 197 FNESFSLSQGLLQLD-MLHEK-LRELEEENMALRSKACHIKTETftyeEKEQQLVNDCVKELRETNAQMSRMTEELSGKS 274
Cdd:PRK04863 259 FKHLITESTNYVAADyMRHANeRRVHLEEALELRRELYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYQAAS 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 275 DEL------LRYQEEISSLLSQIVDLQHKLKEhviekeelrlhlqaskdaQRQLTMELHELQDRNMECLGmlhESQEEIK 348
Cdd:PRK04863 335 DHLnlvqtaLRQQEKIERYQADLEELEERLEE------------------QNEVVEEADEQQEENEARAE---AAEEEVD 393
|
....
gi 1907070332 349 ELRS 352
Cdd:PRK04863 394 ELKS 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
122-353 |
5.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 122 RDRDLELAARIGQALLKRNHVLSEQNEAleEQLGQAFDQVNQLQhelSKKDELLRIVSIASEESETDSscstplrfnesf 201
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERA--EDLVEAEDRIERLE---ERREDLEELIAERRETIEEKR------------ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 202 slsqglLQLDMLHEKLRELEEENMALRSKAchikTETFTYEEKEQQLVNDCVKELRETNAQMSRMtEELSGKSDELLRYQ 281
Cdd:PRK02224 537 ------ERAEELRERAAELEAEAEEKREAA----AEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 282 EEISSL---LSQIVDLQHKLKEHVIEK----------------EELRLHLQASKDAQRQLTMELHELQDRNMECL---GM 339
Cdd:PRK02224 606 DEIERLrekREALAELNDERRERLAEKrerkreleaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQaeiGA 685
|
250
....*....|....
gi 1907070332 340 LHESQEEIKELRSK 353
Cdd:PRK02224 686 VENELEELEELRER 699
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
205-328 |
7.91e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 205 QGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMTEELSGKSDELLRYQ 281
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheeMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907070332 282 EEISSLLSQIVDLQHKLKEhvIEKEELRLHLQASKDAQRQLTMELHE 328
Cdd:COG1340 230 EEIIELQKELRELRKELKK--LRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-333 |
8.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 137 LKRNHVLSEQN----EALEEQLGQAFDQVNQLQHELSKKDELLRIVsiaseeSETDSSCSTPLRFNESfslsqgLLQLDM 212
Cdd:COG4913 598 IRSRYVLGFDNraklAALEAELAELEEELAEAEERLEALEAELDAL------QERREALQRLAEYSWD------EIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 213 LHEKLRELEEENMALRSKACHIktetftyEEKEQQLvNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIV 292
Cdd:COG4913 666 AEREIAELEAELERLDASSDDL-------AALEEQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907070332 293 DLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRN 333
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
213-318 |
8.91e-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: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070332 213 LHEKLRELEEENMALRSKachiktetftyeekeqqlvndcVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIV 292
Cdd:COG2433 418 LEEQVERLEAEVEELEAE----------------------LEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100
....*....|....*....|....*.
gi 1907070332 293 DLQHKLKEHVIEKEELRLHLQASKDA 318
Cdd:COG2433 476 RLERELEEERERIEELKRKLERLKEL 501
|
|
| |
