|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
24-288 |
1.27e-149 |
|
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: 441.77 E-value: 1.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 24 RDSESITVLGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHEL 103
Cdd:pfam04849 45 RETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 104 SKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL 183
Cdd:pfam04849 125 SKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 184 VNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHE 263
Cdd:pfam04849 205 MSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQE 284
|
250 260
....*....|....*....|....*
gi 1907070339 264 LQDRNMECLGMLHESQEEIKELRSK 288
Cdd:pfam04849 285 LQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
349-500 |
2.89e-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: 103.13 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 349 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 411
Cdd:pfam12448 1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 412 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 487
Cdd:pfam12448 79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158
|
170
....*....|...
gi 1907070339 488 PEKLQIVKPLEGS 500
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-286 |
1.69e-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: 58.53 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 47 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 126
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 127 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKAcHIKTETftyEEKEQQLVNDCVKELRETNAQMSRMteels 206
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRER---LESLERRIAATERRLEDLEEQIEEL----- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 207 gksdellryQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 279
Cdd:TIGR02168 851 ---------SEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
....*..
gi 1907070339 280 EEIKELR 286
Cdd:TIGR02168 922 EKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-333 |
1.55e-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: 55.46 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEesetdsscstplrf 132
Cdd:TIGR02169 210 AERYQALlkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK--RLEEIEQL-------------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 133 nesfslsqgllqLDMLHEKLREL-EEENMALRSKACHIKTETF----TYEEKEQQLvNDCVKELRETNAQMSRMTEELSG 207
Cdd:TIGR02169 274 ------------LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 208 KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 287
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907070339 288 KsgpsahlcfsqsygvftGESLAAEIEGTMRKKLSLDEESVSKQKA 333
Cdd:TIGR02169 421 E-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-326 |
3.81e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 6 NAIFkSRTGEAN--LMSSNHRDSESITVLGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNE 83
Cdd:PRK03918 128 NAIY-IRQGEIDaiLESDESREKVVRQILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 84 ALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESfslsqgLLQLDMLHEKLRELEEENMALR 163
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEEL------EKELESLEGSKRKLEEKIRELE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 164 SKACHIKTETFTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEEL 243
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 244 RLhlqaskdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSL 323
Cdd:PRK03918 339 RL---------EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEI 403
|
...
gi 1907070339 324 DEE 326
Cdd:PRK03918 404 EEE 406
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
190-288 |
1.69e-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: 49.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 190 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 269
Cdd:pfam06785 91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160
|
90
....*....|....*....
gi 1907070339 270 ECLGMLHESQEEIKELRSK 288
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-382 |
2.34e-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: 51.60 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 37 VEQMTKTYNDIDMVTHLLAE-RDRDLELAARIgQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSI 115
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEElRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 116 ASEESETDSSCSTplrfNESFSLSQgllQLDMLHEKLRELEEENMALRSKachiktetftYEEKEQQL------VNDCVK 189
Cdd:TIGR02168 331 KLDELAEELAELE----EKLEELKE---ELESLEAELEELEAELEELESR----------LEELEEQLetlrskVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 190 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQ-------------------IVDLQHKLKEHVIEKEELRLHLQAS 250
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelqaeleeleeeLEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 251 KDAQRQLTMELHELQDRNMECLGML--HES-QEEIKEL-RSKSGPSAHL-CFSQSYGVFTGESLAAEI--EGTMRKKLSL 323
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVE 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070339 324 DEESVS------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG--SNRSSVIMTAKPFESGVQP 382
Cdd:TIGR02168 554 NLNAAKkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKALSY 620
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-288 |
4.02e-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: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 78 LSEQNEALEEQLGQAFDQVNQLQHELSKK--DELLRIVS-IASEESETdSSCSTPLRFNESfslsqgllQLDMLHEKLRE 154
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEkIGELEAEI-ASLERSIAEKER--------ELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 155 LEEENMALRSKACHIKTETFTYEEKEQQLVNDcVKELRETNAQMSRMTEELSGKS----DELLRYQEEISsllsqivDLQ 230
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEE-YAELKEELEDLRAELEEVDKEFaetrDELKDYREKLE-------KLK 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070339 231 HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 288
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-287 |
8.52e-06 |
|
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: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 132
Cdd:COG1196 212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 133 nesfslsqglLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEELSGKSDEL 212
Cdd:COG1196 281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070339 213 LRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 287
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-265 |
1.88e-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: 48.51 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 39 QMTKTYNDIDMVTHLLAERDRD---LELAARIGQALLKRN--------HVLSEQNEALEEQLGQAFDQVNQLQHELSKKD 107
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQlksLERQAEKAERYKELKaelrelelALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 108 ELLRIVSIASEESEtdsscstpLRFNEsfslsqgllqldmLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDc 187
Cdd:TIGR02168 260 AELQELEEKLEELR--------LEVSE-------------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ- 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070339 188 VKELRETNAQMSRMTEELSgksDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ 265
Cdd:TIGR02168 318 LEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-288 |
2.35e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 151 KLRELEEENMALRSKACHIKTETFTYeekeqqlvNDCVKELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQ 230
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELT 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070339 231 HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRSK 288
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDK 307
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
78-266 |
4.69e-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: 46.61 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 78 LSEQN-EALEEQLGQAFDQVNQLQHELSK-----KDELLRIVS-IASEESETDSSCSTPLRFNESFSLSQGLLQL----- 145
Cdd:pfam04108 109 IDEDSvEILRDALKELIDELQAAQESLDSdlkrfDDDLRDLQKeLESLSSPSESISLIPTLLKELESLEEEMASLleslt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 146 ---DMLHEKLRELEEEnmalrskachiKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSL 222
Cdd:pfam04108 189 nhyDQCVTAVKLTEGG-----------RAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSA 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907070339 223 LSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQD 266
Cdd:pfam04108 258 LQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-275 |
5.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 53 LLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLgqafDQVNQLQHELSKKDEllRIVSIASEESETDsscstplrf 132
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEE--ELEELEAELEELR--------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 133 NESFSLSQgLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvNDCVKELRETNAQMSRMTEELS-GKSDE 211
Cdd:COG4717 116 EELEKLEK-LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL-EELEAELAELQEELEELLEQLSlATEEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070339 212 LLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRlhlqaSKDAQRQLTMELHELQDRNMECLGML 275
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELE-----EELEQLENELEAAALEERLKEARLLL 252
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
59-453 |
6.23e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 59 RDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSL 138
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE-----SEIIELKKSLSS 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 139 SQgLLQLDMLHEKLRELEEENMALRSKAchIKTETFTYEEKEQQLVNDCvKELRETNAQMSRM-------TEELSGKSDE 211
Cdd:COG5022 918 DL-IENLEFKTELIARLKKLLNNIDLEE--GPSIEYVKLPELNKLHEVE-SKLKETSEEYEDLlkkstilVREGNKANSE 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 212 LLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK-----DAQRQLTMELHELQDRNMEclgMLHESQEEIKELR 286
Cdd:COG5022 994 LKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGLLLL---ENNQLQARYKALK 1070
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 287 SKSgPSAHLCFSQSYGVFTGESLAAEIEgtMRKKLSLDEESVSKQKAQQKRVFDTVKVANDTRgrsvtfpvllpIPGSNR 366
Cdd:COG5022 1071 LRR-ENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQE-----------ISKFLS 1136
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 367 SSVIMTAKPFESgvqpaEDKTLLSPGGSTEVPGNSQPTNPP---GSPEDSDLATALH----RLSLRRQNYLSEK-----Q 434
Cdd:COG5022 1137 QLVNTLEPVFQK-----LSVLQLELDGLFWEANLEALPSPPpfaALSEKRLYQSALYdeksKLSSSEVNDLKNElialfS 1211
|
410
....*....|....*....
gi 1907070339 435 FFAEEWERKIQILAEQEEE 453
Cdd:COG5022 1212 KIFSGWPRGDKLKKLISEG 1230
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
146-285 |
6.59e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 146 DMLHEKLRELEEENMALRSKACHIKtETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKS---DELLRYQEEISSL 222
Cdd:PRK04778 313 DTLPDFLEHAKEQNKELKEEIDRVK-QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQ 391
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 223 LSQIVDLQHKLKEHV--IEKEELRLHlQASKDAQRQLTMELHELQDRNM-----ECLGMLHESQEEIKEL 285
Cdd:PRK04778 392 LEEIEKEQEKLSEMLqgLRKDELEAR-EKLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEAL 460
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
137-267 |
7.01e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 137 SLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMTEELSGKSDELL 213
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907070339 214 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 267
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-288 |
7.45e-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: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 142 LLQLDMLHEKLRELEEEnmalrskachiktetftyEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISS 221
Cdd:COG1196 231 LLKLRELEAELEELEAE------------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070339 222 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 288
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-337 |
8.80e-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: 46.20 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 78 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETdsscstplrfnesfslsqgllQLDMLHEKLRELEE 157
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR---------------------QISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 158 EnmalrskachiktetftyEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHV 237
Cdd:TIGR02168 741 E------------------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 238 IEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKsgpsahlcfsqsygvftGESLAAEIE--G 315
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-----------------IESLAAEIEelE 865
|
250 260
....*....|....*....|..
gi 1907070339 316 TMRKKLSLDEESVSKQKAQQKR 337
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEE 887
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
88-288 |
9.06e-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: 45.08 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 88 QLGQAFDQVNQ----LQHELSKKD--ELLRIVSIAsEESETDSSCSTPlrfneSFSLSQGLLQ-------LDMLHEKLRE 154
Cdd:pfam15294 64 LLRQLFSQAEKwhlkLQADISELEnrELLEQIAEF-EEREFTSSNKKP-----NFELNKPKLEplnegggSALLHMEIER 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 155 LEEENMALRSKachikteTFTYEEKeqqlVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEeISSLLSQI----VDLQ 230
Cdd:pfam15294 138 LKEENEKLKER-------LKTLESQ----ATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKE-ISDLEEKMaalkSDLE 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 231 HKLKEHVIEKEELRLHLQASK----DAQRQLTMELHEL--------QDRNMEclGMLHESQEEIKELRSK 288
Cdd:pfam15294 206 KTLNASTALQKSLEEDLASTKhellKVQEQLEMAEKELekkfqqtaAYRNMK--EMLTKKNEQIKELRKR 273
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
179-289 |
1.17e-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: 45.01 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 179 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 250
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070339 251 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 289
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-288 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 54 LAERDRDLELAARIG--QALL-----KRNHVLSEQNEAL------EEQLGQAFDQVNQLQHELSKKDELLrivsiasEES 120
Cdd:TIGR02169 670 RSEPAELQRLRERLEglKRELsslqsELRRIENRLDELSqelsdaSRKIGEIEKEIEQLEQEEEKLKERL-------EEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 121 ETD-SSCSTPLRFNESfSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYE-EKEQQLVNDCVKELRETNAQM 198
Cdd:TIGR02169 743 EEDlSSLEQEIENVKS-ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 199 SRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHES 278
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250
....*....|
gi 1907070339 279 QEEIKELRSK 288
Cdd:TIGR02169 902 ERKIEELEAQ 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
48-288 |
1.33e-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: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 48 DMVTHLLAERDRDLE-LAARIGQALLKRNHVLSE----------QNEALEEQLGQAFDQVNQLQHEL--------SKKDE 108
Cdd:pfam15921 267 DRIEQLISEHEVEITgLTEKASSARSQANSIQSQleiiqeqarnQNSMYMRQLSDLESTVSQLRSELreakrmyeDKIEE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 109 LLRIVSIASEESeTDSSCSTPLRFNESFSLSQGLLQLDM-LHEKLREL---EEENMAL--RSKACHIKTETFTYE----E 178
Cdd:pfam15921 347 LEKQLVLANSEL-TEARTERDQFSQESGNLDDQLQKLLAdLHKREKELsleKEQNKRLwdRDTGNSITIDHLRRElddrN 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 179 KEQQLVNDCVKELR-ETNAQMSRMTEELSGKSDELlryqEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL 257
Cdd:pfam15921 426 MEVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL 501
|
250 260 270
....*....|....*....|....*....|.
gi 1907070339 258 TMELHElQDRNMEClgmlheSQEEIKELRSK 288
Cdd:pfam15921 502 TASLQE-KERAIEA------TNAEITKLRSR 525
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
170-288 |
4.41e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 170 KTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 249
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907070339 250 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 288
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
36-285 |
6.58e-04 |
|
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: 42.92 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 36 RVEQ-MTKTYNDIDMVTHLLAERDRdlelaaRIG---------QALLKRNHVLSEQNEALEEQLGQAFDQVNQL---QHE 102
Cdd:pfam03148 82 RLEKaLEALEEPLHIAQECLTLREK------RQGidlvhdeveKELLKEVELIEGIQELLQRTLEQAWEQLRLLraaRHK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 103 LSK----KDELLRIVSIASEESETDSSCS---TPLRFNESFSLSQGLLQL--DMLHEKLRELeEENMALRSKACHIKTET 173
Cdd:pfam03148 156 LEKdlsdKKEALEIDEKCLSLNNTSPNISykpGPTRIPPNSSTPEEWEKFtqDNIERAEKER-AASAQLRELIDSILEQT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 174 FTYEEKEQQLVNDcvkELRETNAQMSRMTEELsgkSDELLRYQEEISSLLSQIVDLQHKL--KEHVIEKEELRLHLQAS- 250
Cdd:pfam03148 235 ANDLRAQADAVNF---ALRKRIEETEDAKNKL---EWQLKKTLQEIAELEKNIEALEKAIrdKEAPLKLAQTRLENRTYr 308
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907070339 251 ------KD-AQRQLTMELHELQDrNMECL-GMLHESQEEIKEL 285
Cdd:pfam03148 309 pnvelcRDeAQYGLVDEVKELEE-TIEALkQKLAEAEASLQAL 350
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
10-327 |
7.42e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 10 KSRTGEANLMSSNHRDSESITVLGTDRVEQMtKTYNDI------DMVTHLL-AERDRDLELAARIgQALLKRNHVLSEQn 82
Cdd:PLN02939 89 KSTSSDDDHNRASMQRDEAIAAIDNEQQTNS-KDGEQLsdfqleDLVGMIQnAEKNILLLNQARL-QALEDLEKILTEK- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 83 EALEEQlgqafdqVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMAL 162
Cdd:PLN02939 166 EALQGK-------INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 163 RSKACHIKTETFTYEEKEQQLVndcvkELRETNAQMSRMTEELSGKsdeLLRYQEEISSLLSQIVD--------LQHKLK 234
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERVF-----KLEKERSLLDASLRELESK---FIVAQEDVSKLSPLQYDcwwekvenLQDLLD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 235 EHVIEKEELRLHLQASKDAQRQLTMELHELQDRNM--ECLGMLHESQEEIKELRSKSGPSAHLCFSQsygVFTGESLAAE 312
Cdd:PLN02939 311 RATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSY---IQLYQESIKE 387
|
330
....*....|....*
gi 1907070339 313 IEGTMRKklsLDEES 327
Cdd:PLN02939 388 FQDTLSK---LKEES 399
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-290 |
8.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 54 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSK-KDELLRIVSIASEESETdsscstpLRF 132
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKEKAEEY-------IKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 133 NEsfslsqgllQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDEL 212
Cdd:PRK03918 299 SE---------FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070339 213 lryqEEISSLLSQIVDLQHKLKEHviEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKSG 290
Cdd:PRK03918 365 ----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
51-288 |
9.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 51 THLLAERDrdleLAARIGQAL-----LKRNH----VLSEQNEALEeQLGQAFDQVNQLQHELSKKDELLRIVsiaseese 121
Cdd:COG4913 215 EYMLEEPD----TFEAADALVehfddLERAHealeDAREQIELLE-PIRELAERYAAARERLAELEYLRAAL-------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 122 tdsscstPLRFNEsfsLSQGLLQ--LDMLHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLVNDCVKELRETNAQMS 199
Cdd:COG4913 282 -------RLWFAQ---RRLELLEaeLEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 200 RMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHvieKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 279
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
....*....
gi 1907070339 280 EEIKELRSK 288
Cdd:COG4913 426 AEIASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-265 |
9.46e-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: 43.13 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 54 LAERDRDLE-LAARIGQALLKRNHVLSEQnEALEEQLGQAFDQVNQLQHEL-SKKDELLRIVSIASEESEtdsscstplR 131
Cdd:TIGR02169 310 IAEKERELEdAEERLAKLEAEIDKLLAEI-EELEREIEEERKRRDKLTEEYaELKEELEDLRAELEEVDK---------E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 132 FNESF-SLSQGLLQLDMLHEKLRELEEENMALrskachiktetftyeekeqqlvndcVKELRETNAQMSRMTEELSGKSD 210
Cdd:TIGR02169 380 FAETRdELKDYREKLEKLKREINELKRELDRL-------------------------QEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907070339 211 ELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ 265
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
150-285 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 150 EKLRELEEENMALRSKAcHIKTETftYEE---KEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQI 226
Cdd:pfam10168 575 QELQSLEEERKSLSERA-EKLAEK--YEEikdKQEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAI 651
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070339 227 VDLQHKlkehvieKEELRLHLQASKDAQRQLTMELHELQDRNMEclGMLHESQEEIKEL 285
Cdd:pfam10168 652 KQAKKK-------MNYQRYQIAKSQSIRKKSSLSLSEKQRKTIK--EILKQLGSEIDEL 701
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
54-288 |
1.44e-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: 42.32 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 54 LAERDRDLELAARIGQALLKRnhvlseqneaLEEQLGQAFDQVNQLQHELSK-KDELLRIVSIASEESETDSSCSTPLRF 132
Cdd:pfam05667 231 LASRLTPEEYRKRKRTKLLKR----------IAEQLRSAALAGTEATSGASRsAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 133 NESfslsqgllqldmlhEKLRELEEENMALRSKACHIKTETFTYEEKE------QQLVNDCVKELRETNAQMSRMTEELS 206
Cdd:pfam05667 301 THT--------------EKLQFTNEAPAATSSPPTKVETEEELQQQREeeleelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 207 GKSDELLRYQEEISSLLSQIvdlqhKLKEHVIE--------KEELRLHLQASKD-----------AQRQLTMELHELQDR 267
Cdd:pfam05667 367 QVEEELEELKEQNEELEKQY-----KVKKKTLDllpdaeenIAKLQALVDASAQrlvelagqwekHRVPLIEEYRALKEA 441
|
250 260
....*....|....*....|....
gi 1907070339 268 NMEclgMLHESQ---EEIKELRSK 288
Cdd:pfam05667 442 KSN---KEDESQrklEEIKELREK 462
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
73-289 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 73 KRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGL----LQLDML 148
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCnnlkKQIENK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 149 HEKLRELEEENMALRSKACHIKTETFTYE--------------EKEQQLVNDCVKELRETNAQMSRMTEELSGK---SDE 211
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENKQLNAYEikvnklelelasakQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiADE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 212 LLRYQEEI----SSLLSQIVDLQHKLK---EHVIEKEELRLHLQASKDAQRQ-----LTMELHELQDRNMECLGMLHESQ 279
Cdd:pfam05483 687 AVKLQKEIdkrcQHKIAEMVALMEKHKhqyDKIIEERDSELGLYKNKEQEQSsakaaLEIELSNIKAELLSLKKQLEIEK 766
|
250
....*....|
gi 1907070339 280 EEIKELRSKS 289
Cdd:pfam05483 767 EEKEKLKMEA 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-286 |
1.63e-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: 42.35 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 144 QLDMLH------EKLRELEEEnmaLRSKACHIKTETFTYEEKEQQLVNdcvKELRETNAQMSRMTEELSGKSDELLRYQE 217
Cdd:TIGR02168 201 QLKSLErqaekaERYKELKAE---LRELELALLVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070339 218 EISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL-------TMELHELQDRNMECLGMLHESQEEIKELR 286
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLerqleelEAQLEELESKLDELAEELAELEEKLEELK 350
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-302 |
2.43e-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: 41.29 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 54 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSScstplrfn 133
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 134 esfSLSQGLLQLDMLHEKLRELEEENMALRSkachiktETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELL 213
Cdd:COG4942 101 ---AQKEELAELLRALYRLGRQPPLALLLSP-------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 214 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGMLHESQEEIKELRSKSGPSA 293
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*....
gi 1907070339 294 hlcFSQSYG 302
Cdd:COG4942 248 ---FAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-288 |
2.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 54 LAERDRDLElAARIGQALLKRNHVLSEQNEALEEQLGQaFDQvnqlqHELSKKDELLRIVSIASEESETDSScstplRFN 133
Cdd:PRK03918 478 LRKELRELE-KVLKKESELIKLKELAEQLKELEEKLKK-YNL-----EELEKKAEEYEKLKEKLIKLKGEIK-----SLK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 134 ESFSLSQGLL-QLDMLHEKLRELEEENMALRSKACHIKTETFT-YEEKEQQL---------VNDCVKELRETNAQMSRMT 202
Cdd:PRK03918 546 KELEKLEELKkKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAEKELEREEKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 203 EELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHviEKEELR-LHLQASKDAQRqLTMELHELQDRNMECLGMLHESQEE 281
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELReEYLELSRELAG-LRAELEELEKRREEIKKTLEKLKEE 702
|
....*..
gi 1907070339 282 IKELRSK 288
Cdd:PRK03918 703 LEEREKA 709
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-243 |
3.37e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 6 NAIFKSRTGEANlmssnhRDSESITVLgTDRVEQMTKTYND-IDMVTHLLAER--------DRDLELAARIGQALLKRNH 76
Cdd:PHA02562 169 DKLNKDKIRELN------QQIQTLDMK-IDHIQQQIKTYNKnIEEQRKKNGENiarkqnkyDELVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 77 VLSEQNEALEEQLGqAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLR---------FNESFSLSQGLLQLDM 147
Cdd:PHA02562 242 ELLNLVMDIEDPSA-ALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISegpdritkiKDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 148 LHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLVNdCVKELRETNAQMSRMteelsgkSDELLRYQEEISSLLSQIV 227
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKKLLELKNK---ISTNKQSLIT-LVDKAKKVKAAIEEL-------QAEFVDNAEELAKLQDELD 389
|
250
....*....|....*.
gi 1907070339 228 DLQHKLKEHVIEKEEL 243
Cdd:PHA02562 390 KIVKTKSELVKEKYHR 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-288 |
3.68e-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: 39.91 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 148 LHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLvNDCVKELRETNAQMSRMTEELSG--KSDELLRYQEEISSLLSQ 225
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTE---LEDLEKEI-KRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070339 226 IVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGmlhESQEEIKELRSK 288
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAE 164
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
57-288 |
3.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 57 RDRDLELAARIGQALLKRNHVLSEQNEAleEQLGQAFDQVNQLQhelSKKDELLRIVSIASEESETDSscstplrfnesf 136
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERA--EDLVEAEDRIERLE---ERREDLEELIAERRETIEEKR------------ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 137 slsqglLQLDMLHEKLRELEEENMALRSKAchikTETFTYEEKEQQLVNDCVKELRETNAQMSRMtEELSGKSDELLRYQ 216
Cdd:PRK02224 537 ------ERAEELRERAAELEAEAEEKREAA----AEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 217 EEISSL---LSQIVDLQHKLKEHVIEK----------------EELRLHLQASKDAQRQLTMELHELQDRNMECL---GM 274
Cdd:PRK02224 606 DEIERLrekREALAELNDERRERLAEKrerkreleaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQaeiGA 685
|
250
....*....|....
gi 1907070339 275 LHESQEEIKELRSK 288
Cdd:PRK02224 686 VENELEELEELRER 699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-287 |
4.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 143 LQLDMLHEKLRELEEENMALRSKAchIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMT-EELSGKSDELLRYQEEISS 221
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKEL--RELEKVLKKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070339 222 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMEClgmLHESQEEIKELRS 287
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEP 599
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
132-287 |
4.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 132 FNESFSLSQGLLQLD-MLHEK-LRELEEENMALRSKACHIKTETftyeEKEQQLVNDCVKELRETNAQMSRMTEELSGKS 209
Cdd:PRK04863 259 FKHLITESTNYVAADyMRHANeRRVHLEEALELRRELYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYQAAS 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 210 DEL------LRYQEEISSLLSQIVDLQHKLKEhviekeelrlhlqaskdaQRQLTMELHELQDRNMECLGmlhESQEEIK 283
Cdd:PRK04863 335 DHLnlvqtaLRQQEKIERYQADLEELEERLEE------------------QNEVVEEADEQQEENEARAE---AAEEEVD 393
|
....
gi 1907070339 284 ELRS 287
Cdd:PRK04863 394 ELKS 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-268 |
5.73e-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: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 72 LKRNHVLSEQN----EALEEQLGQAFDQVNQLQHELSKKDELLRIVsiaseeSETDSSCSTPLRFNESfslsqgLLQLDM 147
Cdd:COG4913 598 IRSRYVLGFDNraklAALEAELAELEEELAEAEERLEALEAELDAL------QERREALQRLAEYSWD------EIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 148 LHEKLRELEEENMALRSKACHIktetftyEEKEQQLvNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIV 227
Cdd:COG4913 666 AEREIAELEAELERLDASSDDL-------AALEEQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907070339 228 DLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRN 268
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
78-270 |
5.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 78 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVS--IASEESETDSSCSTPLRFNEsfSLSQGLLQLDMLHEKLREL 155
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEeeLEQARSELEQLEEELEELNE--QLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 156 EEENMALRSKACHIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQivDLQHK 232
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLeaqIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQA 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907070339 233 LKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNME 270
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
140-263 |
6.01e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 140 QGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMTEELSGKSDELLRYQ 216
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheeMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907070339 217 EEISSLLSQIVDLQHKLKEhvIEKEELRLHLQASKDAQRQLTMELHE 263
Cdd:COG1340 230 EEIIELQKELRELRKELKK--LRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| DUF4456 |
pfam14644 |
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, ... |
176-292 |
7.25e-03 |
|
Domain of unknown function (DUF4456); This domain family is found in bacteria and eukaryotes, and is approximately 210 amino acids in length. There is a single completely conserved residue E that may be functionally important.
Pssm-ID: 464232 Cd Length: 209 Bit Score: 38.81 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 176 YEEKEQQLVNDCVKELREtnaQMSRMTEELSGKS----DELL-RYQEEISSLLSQIVD-LQHKLKEHVIEKE----ELRL 245
Cdd:pfam14644 41 YQEQADEYHNSCLQELRN---QVERLEELLPSVPelifESLLkRHLQKLERAMKNIAAeFSQKQKQLEQLKQqheqQLRP 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907070339 246 HLQASKDAQrqltmELHEL----QDRNMECLGMLHESQEEIKELRSKSGPS 292
Cdd:pfam14644 118 TLGHPQNAQ-----ELEQLcdreEDRQKEHIELIQAHREALLEAVDKVAST 163
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
148-253 |
8.27e-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: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 148 LHEKLRELEEENMALRSKachiktetftyeekeqqlvndcVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIV 227
Cdd:COG2433 418 LEEQVERLEAEVEELEAE----------------------LEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100
....*....|....*....|....*.
gi 1907070339 228 DLQHKLKEHVIEKEELRLHLQASKDA 253
Cdd:COG2433 476 RLERELEEERERIEELKRKLERLKEL 501
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
144-288 |
8.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070339 144 QLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNdcvkELRETNAQMSRMTEELSGKSDELLRYQEEISSLL 223
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE----EAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070339 224 SQIVDLQHKLKE--------HVIEK--EELRLHLQA---SKDAQRQLTMELHELQDRnMECLGMLHESQEEIKELRSK 288
Cdd:COG1340 92 EELDELRKELAElnkaggsiDKLRKeiERLEWRQQTevlSPEEEKELVEKIKELEKE-LEKAKKALEKNEKLKELRAE 168
|
|
| |
