|
Name |
Accession |
Description |
Interval |
E-value |
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
69-372 |
4.03e-163 |
|
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: 475.28 E-value: 4.03e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 69 SEGQPNYTLRADSVF-GYDNDDW-LHTPL-LPPTVVLGLTHEQIEETLKYFLLCSDRVGQVTKTYHDIKAVTHLLEEKER 145
Cdd:pfam04849 1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 146 DLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQFYAST-EEIENAESHS-PIKRNESCSSL 223
Cdd:pfam04849 81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDaEESETESSCStPLRRNESFSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 224 SNFVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMVCVEELSSVNKQVVDLSEELARKVEDSLRQQEEI 303
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675229582 304 SSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Milton |
pfam12448 |
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ... |
433-601 |
2.87e-54 |
|
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: 185.18 E-value: 2.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 433 RLRSRCHSPG-LPG---SSPPVSTRSSCTSTPRTSYYGSDNASLNLEDKPSPN---NAQKEDNSG--PKRLGQPGTPGGQ 503
Cdd:pfam12448 1 RQRSLTPSPMnIPGsnqSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSIlseTSSSQDSGYdrPKKPGTPGTPGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 504 DLEAALRSLSARQQNHSSERPFFDVERERKLHALA--VDCEEGEgSSGFLTPNDSLtsspaASTGTNYSngsSRHSCGSS 581
Cdd:pfam12448 81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAgtYNYDEGE-HGGSLTPNDSI-----MSLGSNHS---GSSSHSSG 151
|
170 180
....*....|....*....|
gi 1675229582 582 GGSRSYLPDRLQIVKPLEGS 601
Cdd:pfam12448 152 FSSRSYLPEKLQIVKPLEGS 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-372 |
9.75e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 155 QSLLKQNQE---LTARNEMLDEQLEIAKEEIAQLRHELT-MRDDLLQFYASTEEIE---NAESHSPIKRNESCSSLSNFV 227
Cdd:TIGR02168 670 SSILERRREieeLEEKIEELEEKIAELEKALAELRKELEeLEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 228 hyDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQEL----------MMVCVEELSSVNKQVVDLSEELARKVEDSL 297
Cdd:TIGR02168 750 --AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675229582 298 RQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-351 |
2.05e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAvthllEEKERDLELA--------ARIgQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLL 196
Cdd:COG1196 210 EKAERYRELKE-----ELKELEAELLllklreleAEL-EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 197 Q-----FYASTEEIENAEShspiKRNESCSSLSNfvhydfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMmvc 271
Cdd:COG1196 284 EeaqaeEYELLAELARLEQ----DIARLEERRRE------LEERLEELEEELAELEEELEELEEELEELEEELEEAE--- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 272 vEELSSVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDK 351
Cdd:COG1196 351 -EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-372 |
3.04e-10 |
|
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: 63.92 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAvthllEEKERDLELAARIGQSLLKQ----NQELTARNEMLDE---QLEIAKEEIAQLRHELTMRDDLLQ 197
Cdd:TIGR02168 210 EKAERYKELKA-----ELRELELALLVLRLEELREEleelQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 198 -----FYASTEEIENAESHSPIKRNESCSSLSNFVHYDF----LQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELM 268
Cdd:TIGR02168 285 elqkeLYALANEISRLEQQKQILRERLANLERQLEELEAqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 269 MVcVEELSSVNKQVVDLSEELARKVEDSLRQQE----EISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLK---- 340
Cdd:TIGR02168 365 AE-LEELESRLEELEEQLETLRSKVAQLELQIAslnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaele 443
|
250 260 270
....*....|....*....|....*....|...
gi 1675229582 341 -LKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:TIGR02168 444 eLEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
147-365 |
1.86e-09 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 60.21 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 147 LELAARIgQSLLKQNQELTARNEML---------DEQLEIAKEEIAQLRHELTMRDDllQFYASTEEIENAESHSPIKRN 217
Cdd:pfam15905 118 TSLSASV-ASLEKQLLELTRVNELLkakfsedgtQKKMSSLSMELMKLRNKLEAKMK--EVMAKQEGMEGKLQVTQKNLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 218 ESCSSLSNfvhydfLQQKLKGLEDENrklrleanelTTETSHYEEQEQelmmvCVEELSSVNKQV------VDLSEELAR 291
Cdd:pfam15905 195 HSKGKVAQ------LEEKLVSTEKEK----------IEEKSETEKLLE-----YITELSCVSEQVekykldIAQLEELLK 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675229582 292 KVED---SLRQ--QEEISSLLAQIVDLQARCKGLTHENEELnhnLSASRESQLKLKSELKDLQDKYSQCEDMLCEARED 365
Cdd:pfam15905 254 EKNDeieSLKQslEEKEQELSKQIKDLNEKCKLLESEKEEL---LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-372 |
2.28e-09 |
|
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: 61.24 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 159 KQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDdllqfyastEEIENAESHspIKRNEScsslsnfvhydflqqKLKG 238
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE---------QEIENVKSE--LKELEA---------------RIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 239 LEDENRKLRLEANELTTETSHYEEQE-QELMMVCVEELSSVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARC 317
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1675229582 318 KGLTHENEELNHNLSasresqlKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:TIGR02169 850 KSIEKEIENLNGKKE-------ELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-398 |
2.30e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 105 THEQIEETLKYFLLCSDRVGQVTKTYHDIKAvthLLEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQ 184
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALAN---EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 185 LRHELTMrddLLQFYASTEEiENAESHSPIKRNEScsslsnfvHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQE 264
Cdd:TIGR02168 342 LEEKLEE---LKEELESLEA-ELEELEAELEELES--------RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 265 QELMmvcveelSSVNKQVVDLSEELARKVE-DSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKS 343
Cdd:TIGR02168 410 ERLE-------DRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1675229582 344 ELKDLQDKYSQCEDMLCEAR---EDIKNL-RNKSLPNSTVQRYTALASVLPMDSLAAEI 398
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEgfsEGVKALlKNQSGLSGILGVLSELISVDEGYEAAIEA 541
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-372 |
8.46e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 139 LLEEKERDLELAARIGQSLLKQNQELTARNEMLDE---QLEIAKEEIAQLrhELTMRDDLLQFYASTEEIENAEShspIK 215
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEEL--EAQIEQLKEELKALREALDELRA---EL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 216 RNEScsslsnfVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQEL---MMVCVEELSSVNKQVVDLSEELARK 292
Cdd:TIGR02168 813 TLLN-------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 293 VEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDK---------------YSQCED 357
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltleeaealENKIED 965
|
250
....*....|....*
gi 1675229582 358 MLCEAREDIKNLRNK 372
Cdd:TIGR02168 966 DEEEARRRLKRLENK 980
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
159-362 |
1.09e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.60 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 159 KQNQELTARNEMLDEQLEIAKEeiaQLRHELTMRDDLLQFYASTEEIENAESHSPIKRNESCSSLSNFV-----HYDFLQ 233
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELselrrQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 234 QKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMVCvEELSSVNKQVVDLSEELARKVEDSLrQQEEISSLLAQIVDL 313
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ-SSLAEAEQRIKELEFEIQSQEQDSE-IVKNSKSELARIPEL 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1675229582 314 QARCKGLTHENEELNHNlsasRESQLKLKSELKDLQDKYSQCEDMLCEA 362
Cdd:pfam05557 203 EKELERLREHNKHLNEN----IENKLLLKEEVEDLKRKLEREEKYREEA 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-372 |
2.71e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIG--QSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQfyASTEEIENAESHSPIKRN 217
Cdd:TIGR02169 216 LLKEKREYEGYELLKekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE--ELNKKIKDLGEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 218 ESCSSLSnfVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMmvcvEELSSVNKQVVDLSEELA--RKVED 295
Cdd:TIGR02169 294 EKIGELE--AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE----REIEEERKRRDKLTEEYAelKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 296 SLRQQ-EEISSLLA----QIVDLQARCKGLTHENEELNHNLSA-------SRESQLKLKSELKDLQDKYSQCEDMLCEAR 363
Cdd:TIGR02169 368 DLRAElEEVDKEFAetrdELKDYREKLEKLKREINELKRELDRlqeelqrLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
....*....
gi 1675229582 364 EDIKNLRNK 372
Cdd:TIGR02169 448 LEIKKQEWK 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-399 |
3.96e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 133 IKAVTHLLEEKERDLELAARIGQSLLKQNQELTarnEMLDEQLEIAKEEIaQLRHELTMRDDLLQFYAST-EEIENAEsh 211
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELE---EVLREINEISSELP-ELREELEKLEKEVKELEELkEEIEELE-- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 212 spiKRNEScsslsnfvhydfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcvEELSSVNKQVVDLSEELAR 291
Cdd:PRK03918 245 ---KELES------------LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 292 KVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNhnlsasresqlKLKSELKDLQDKYSQCEDMLcEAREDIKNLRN 371
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-----------ELKKKLKELEKRLEELEERH-ELYEEAKAKKE 372
|
250 260
....*....|....*....|....*...
gi 1675229582 372 KslpnstVQRYTALASVLPMDSLAAEIE 399
Cdd:PRK03918 373 E------LERLKKRLTGLTPEKLEKELE 394
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-372 |
4.26e-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: 56.99 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 133 IKAVTHLLEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQFYASTEEIENAESHS 212
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 213 PIKRNEScsslsnfvhydfLQQKLKGLEDENRKLRLEANELTTEtshYEEQEQELMMVcVEELSSVNKQVVDLSEELARK 292
Cdd:TIGR02168 780 AEAEIEE------------LEAQIEQLKEELKALREALDELRAE---LTLLNEEAANL-RERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 293 VEDSLRQQEEISSLLAQIVDLQARCKGLT-----HENE---------ELNHNLSASRESQLKLKSELKDLQDKYSQCEDM 358
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELEseleaLLNErasleealaLLRSELEELSEELRELESKRSELRRELEELREK 923
|
250
....*....|....
gi 1675229582 359 LCEAREDIKNLRNK 372
Cdd:TIGR02168 924 LAQLELRLEGLEVR 937
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-368 |
6.79e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRheltmrddllqfyastEEIENAESHSPIKRNES 219
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD----------------EQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 cSSLSNFVhyDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMvcveELSSVNKQVVDLSEELARKVEdslrq 299
Cdd:TIGR04523 429 -ERLKETI--IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR----SINKIKQNLEQKQKELKSKEK----- 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675229582 300 qeEISSLLAQIVDLQARCKGLTHENEELNhnlsasrESQLKLKSELKDLQDKYSQCEDMLCEAREDIKN 368
Cdd:TIGR04523 497 --ELKKLNEEKKELEEKVKDLTKKISSLK-------EKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-366 |
6.92e-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: 56.60 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 120 SDRVGQVTKTYHDIKAVTHLLEEKERDLELAArigQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTmrddllQFY 199
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERL---ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE------ELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 200 ASTEEIENA-ESHSPIKRNESCSSLSNFVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMvcveELSSV 278
Cdd:TIGR02168 866 ELIEELESElEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV----RIDNL 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 279 NKQvvdLSEELARKVEDSLRQQEEISSLLAQivdLQARCKGLTHENEEL-NHNLSASRESQlKLKSELKDLQdkySQCED 357
Cdd:TIGR02168 942 QER---LSEEYSLTLEEAEALENKIEDDEEE---ARRRLKRLENKIKELgPVNLAAIEEYE-ELKERYDFLT---AQKED 1011
|
....*....
gi 1675229582 358 mLCEAREDI 366
Cdd:TIGR02168 1012 -LTEAKETL 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-316 |
9.23e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAarigQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQFYASTEEIENAESH--SPIKRN 217
Cdd:COG4717 73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 218 ESCssLSNFVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQElmmVCVEELSSVNKQVVDLSEELARKVEDSL 297
Cdd:COG4717 149 EEL--EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*....
gi 1675229582 298 RQQEEISSLLAQIVDLQAR 316
Cdd:COG4717 224 ELEEELEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-371 |
1.72e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIGQSLLKQNQELTARNEMLDeQLEIAKEEIAQLrheltmrdDLLQFYASTEEIENAESHSpIKRNES 219
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKY--------NLEELEKKAEEYEKLKEKL-IKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 CSSLSNFVhydflqQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMVCVEELSSVNKQV----------VDLSEEL 289
Cdd:PRK03918 541 IKSLKKEL------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELepfyneylelKDAEKEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 290 ARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSAS-----RESQLKLKSELKDLQDKYSQCEDMLCEARE 364
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeyeelREEYLELSRELAGLRAELEELEKRREEIKK 694
|
....*..
gi 1675229582 365 DIKNLRN 371
Cdd:PRK03918 695 TLEKLKE 701
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
125-374 |
3.45e-07 |
|
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: 53.96 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAVTHLLEE---KERDLELAARIGQSLLKQNQE----LTARNE--------------MLDEQLEIAKEEIA 183
Cdd:pfam05483 248 QITEKENKMKDLTFLLEEsrdKANQLEEKTKLQDENLKELIEkkdhLTKELEdikmslqrsmstqkALEEDLQIATKTIC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 184 QLRHELTmrddllqfyASTEEIENAES-HSPI--KRNESCSSLSNFVHYDflQQKLKGLEDENRKLRLEAN-------EL 253
Cdd:pfam05483 328 QLTEEKE---------AQMEELNKAKAaHSFVvtEFEATTCSLEELLRTE--QQRLEKNEDQLKIITMELQkksseleEM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 254 TTETSHYEEQEQELMMVCVEE--LSSVNKQVVDLSEELARKVEDSL----RQQEEISSLLAQI----------------- 310
Cdd:pfam05483 397 TKFKNNKEVELEELKKILAEDekLLDEKKQFEKIAEELKGKEQELIfllqAREKEIHDLEIQLtaiktseehylkevedl 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675229582 311 -----------VDLQARCKGLTHENEELNHNLSasrESQLKLKSELKDLQDKYSQCEDMLcearEDIKNLRNKSL 374
Cdd:pfam05483 477 ktelekeklknIELTAHCDKLLLENKELTQEAS---DMTLELKKHQEDIINCKKQEERML----KQIENLEEKEM 544
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
233-389 |
3.59e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 233 QQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMmvcvEELSSVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVD 312
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1675229582 313 LQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNKSLPNSTVQRYTALASVL 389
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-386 |
5.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 107 EQIEETLKYFLLcsdrvgqvtktyHDIKAVTHLLEE-KERDLELAARIG--QSLLKQNQELTARNEMLDEQLEIAKEEIA 183
Cdd:PRK03918 506 KELEEKLKKYNL------------EELEKKAEEYEKlKEKLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEEELA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 184 QLRHELTMRDdllqfYASTEEIEnaeshSPIKRNEScsslsnfVHYDFLQQK--LKGLEDENRKLRLEANELTTETSHYE 261
Cdd:PRK03918 574 ELLKELEELG-----FESVEELE-----ERLKELEP-------FYNEYLELKdaEKELEREEKELKKLEEELDKAFEELA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 262 EQEQELMMVcVEELSSVNKQVVDlsEELARKVEDSLRQQEEISSLLAQIvdlqarcKGLTHENEELNHNLSasresqlKL 341
Cdd:PRK03918 637 ETEKRLEEL-RKELEELEKKYSE--EEYEELREEYLELSRELAGLRAEL-------EELEKRREEIKKTLE-------KL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1675229582 342 KSELKDLQDKYSQCEDmLCEAREDIKNLRNKslpnstVQRYTALA 386
Cdd:PRK03918 700 KEELEEREKAKKELEK-LEKALERVEELREK------VKKYKALL 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
140-372 |
1.59e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQFYASTEEIENAESHSPIKRNES 219
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 -CSSLSNFV-----HYDFLQQKLKGLED----ENRKL--------RLEAnELTTETSHYEE------QEQELMMVCVEE- 274
Cdd:pfam05483 595 kCNNLKKQIenknkNIEELHQENKALKKkgsaENKQLnayeikvnKLEL-ELASAKQKFEEiidnyqKEIEDKKISEEKl 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 275 LSSVNKQVVDLSEELARKVEDSLRQQEEISSLLA----------QIVDLQARCKGLTHENEELNHNLSASRESQL-KLKS 343
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVAlmekhkhqydKIIEERDSELGLYKNKEQEQSSAKAALEIELsNIKA 753
|
250 260 270
....*....|....*....|....*....|...
gi 1675229582 344 EL----KDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:pfam05483 754 ELlslkKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-372 |
1.66e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 105 THEQIEETLKYFLLCSDRVGQVT------KTYHDIKAVTHLLEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIA 178
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 179 KEEIAQLRHELT-MRDDLLQFYASTEEIENAESHSPIKRNESCSSLSNfvHYDFLQQKLKGLEDENRKLRLEANELTTET 257
Cdd:PRK03918 344 KKKLKELEKRLEeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITARIGELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 258 SHY----------------------EEQEQELMMVCVEELSSVNKQVVDLSEEL------ARKVEDSLRQQEEISSL--- 306
Cdd:PRK03918 422 KELkkaieelkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKErklrkeLRELEKVLKKESELIKLkel 501
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1675229582 307 LAQIVDLQARCKGLTHEN-EELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
229-370 |
5.03e-06 |
|
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: 49.25 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 229 YDFLQQKLKGLEDenrKLRLEANELTTETSH---YEEQEQELMMVCVEELSSVNKQVVDL---SEELARKVEDSL-RQQE 301
Cdd:smart00787 135 YEWRMKLLEGLKE---GLDENLEGLKEDYKLlmkELELLNSIKPKLRDRKDALEEELRQLkqlEDELEDCDPTELdRAKE 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675229582 302 EISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMlceAREDIKNLR 370
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLK 277
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-392 |
5.83e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 137 THLLEEKErdleLAARIgQSLLKQNQELT-ARNEMLDeqleiAKEEIAQLRHELTMRDDLLQFYASTEEIENAESHSPIK 215
Cdd:COG4913 215 EYMLEEPD----TFEAA-DALVEHFDDLErAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 216 RNESCSSLsnfvhydfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcveeLSSVNKQVVDLSEELARKVED 295
Cdd:COG4913 285 FAQRRLEL--------LEAELEELRAELARLEAELERLEARLDALREELDEL-------EAQIRGNGGDRLEQLEREIER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 296 SLRQQEEISSLLAQivdLQARCKGLTHEN----EELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNL-- 369
Cdd:COG4913 350 LERELEERERRRAR---LEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELea 426
|
250 260 270
....*....|....*....|....*....|
gi 1675229582 370 -------RNKSLPNSTVQRYTALASVLPMD 392
Cdd:COG4913 427 eiaslerRKSNIPARLLALRDALAEALGLD 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-389 |
5.95e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 225 NFVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQEL--------MMVCVEELSSVNKQVVDLSEELA---RKV 293
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeelreeleKLEKLLQLLPLYQELEALEAELAelpERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 294 EDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLK--------LKSELKDLQDKYSQCEDMLCEARED 365
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaeeleeLQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....
gi 1675229582 366 IKNLRNKSLPNSTVQRYTALASVL 389
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLL 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
239-373 |
8.65e-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: 49.67 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 239 LEDENRKLRlEANELTTETSHYEEQEQELMMVCVEELSSVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARCK 318
Cdd:TIGR02168 234 LEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675229582 319 GLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQ-------CEDMLCEAREDIKNLRNKS 373
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelesLEAELEELEAELEELESRL 374
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
163-373 |
2.93e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 163 ELTARNEMLDEQLEIAKEEIAQLRHEltmRDDLlqfyasteeieNAESHSPI-KRNEscsslsnfvhydfLQQKLKGLED 241
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEK---RDEL-----------NEELKELAeKRDE-------------LNAQVKELRE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 242 ENRKLRLEANELTTETSHYEEQEQELmmvcVEELSSVNKQVVDLSEELARKVEDSlRQQEEISSLLAQIVD-LQARCKGL 320
Cdd:COG1340 58 EAQELREKRDELNEKVKELKEERDEL----NEKLNELREELDELRKELAELNKAG-GSIDKLRKEIERLEWrQQTEVLSP 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1675229582 321 THENE------ELNHNLSAsRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNKS 373
Cdd:COG1340 133 EEEKElvekikELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEA 190
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
232-381 |
9.76e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.77 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 232 LQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMVCV-----------EELSSVNK-------QVVDLSEELARKV 293
Cdd:pfam08614 12 LLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIqsleqllaqlrEELAELYRsrgelaqRLVDLNEELQELE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 294 EDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSAsresqlkLKSELKDLQDKYSQCEdmlcEAREDIKNlRNKS 373
Cdd:pfam08614 92 KKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQD-------LQDELVALQLQLNMAE----EKLRKLEK-ENRE 159
|
....*...
gi 1675229582 374 LpnstVQR 381
Cdd:pfam08614 160 L----VER 163
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
140-407 |
1.25e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLElaaRIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTmrddllqfyasteeiENAESHSPIKrnES 219
Cdd:pfam10174 445 LSEKERIIE---RLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT---------------EKESSLIDLK--EH 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 CSSL-SNFVHYDflqQKLKGLEDENRKLRLEANELttETSHYEEQEQELMMVCVEELSSvnkQVVDLSEELARKVEDSLR 298
Cdd:pfam10174 505 ASSLaSSGLKKD---SKLKSLEIAVEQKKEECSKL--ENQLKKAHNAEEAVRTNPEIND---RIRLLEQEVARYKEESGK 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 299 QQEEISSLLAQIVDLQARckglTHENEELNHNLSASRESQLKLKSeLKDLQDKYSQCEDMLCEAREDIKNLRNKSLPNST 378
Cdd:pfam10174 577 AQAEVERLLGILREVENE----KNDKDKKIAELESLTLRQMKEQN-KKVANIKHGQQEMKKKGAQLLEEARRREDNLADN 651
|
250 260
....*....|....*....|....*....
gi 1675229582 379 VQRYTalasvlpMDSLAAEIEGTfRKGLD 407
Cdd:pfam10174 652 SQQLQ-------LEELMGALEKT-RQELD 672
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
232-372 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 232 LQQKLKGLEDENRKLRleaneltTETSHYEEQeqelMMVCVEELSSVNKQVVDLSEELARKvEDSLRQQEEISSLLAQI- 310
Cdd:pfam15294 131 LHMEIERLKEENEKLK-------ERLKTLESQ----ATQALDEKSKLEKALKDLQKEQGAK-KDVKSNLKEISDLEEKMa 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675229582 311 ---VDLQARCKGLTHENEELNHNLSASRESQLKLKSEL----KDLQDKYSQC------EDMLCEAREDIKNLRNK 372
Cdd:pfam15294 199 alkSDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLemaeKELEKKFQQTaayrnmKEMLTKKNEQIKELRKR 273
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-381 |
1.52e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIGQSLLKQNQEL-TARNEMLDEQLEIaKEEIAQLRHELTmRDDLLQFyasteeieNAESHspIKRNE 218
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELeNELNLLEKEKLNI-QKNIDKIKNKLL-KLELLLS--------NLKKK--IQKNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 219 SCSS-LSNfvhydfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcVEELSSVNKQvvdlseeLARKVEDSL 297
Cdd:TIGR04523 215 SLESqISE------LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL----KDEQNKIKKQ-------LSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 298 RQQEEISSLLAQIVDLQARCKGLTHENEElnhNLSASRESQLK-LKSELKDLQDKYSQCEDMLCEAREDIKNLR----NK 372
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEQ---DWNKELKSELKnQEKKLEEIQNQISQNNKIISQLNEQISQLKkeltNS 354
|
....*....
gi 1675229582 373 SLPNSTVQR 381
Cdd:TIGR04523 355 ESENSEKQR 363
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-371 |
2.01e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 135 AVTHLLEEKERDLELAARigqsLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELT-----MRDDLLQFYASTEEIENAE 209
Cdd:PRK02224 336 AAQAHNEEAESLREDADD----LEERAEELREEAAELESELEEAREAVEDRREEIEeleeeIEELRERFGDAPVDLGNAE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 210 SHSpikrnESCSSLSNFVHYDF--LQQKLKGLED---ENRKLR-----------LEANELTTETSHYEEQEQELMmvcvE 273
Cdd:PRK02224 412 DFL-----EELREERDELREREaeLEATLRTARErveEAEALLeagkcpecgqpVEGSPHVETIEEDRERVEELE----A 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 274 ELSSVNKQVVDLSE---------ELARKVEDSLRQQEEISSLLAQ----IVDLQARCKGLTHENEELNHNLSASRESQLK 340
Cdd:PRK02224 483 ELEDLEEEVEEVEErleraedlvEAEDRIERLEERREDLEELIAErretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
250 260 270
....*....|....*....|....*....|.
gi 1675229582 341 LKSELKDLQDKYSQCEDMLCEAREDIKNLRN 371
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
139-318 |
2.52e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 139 LLEEKERDLELA--ARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDdllqfyastEEIENAESHspIKR 216
Cdd:COG1579 9 LLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE---------LEIEEVEAR--IKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 217 NES-CSSLSNFVHYDFLQQKLKGLEDENRKLrleanelttetshyEEQEQELMmvcvEELSSVNKQVVDLSEELARKVED 295
Cdd:COG1579 78 YEEqLGNVRNNKEYEALQKEIESLKRRISDL--------------EDEILELM----ERIEELEEELAELEAELAELEAE 139
|
170 180
....*....|....*....|...
gi 1675229582 296 SLRQQEEISSLLAQIVDLQARCK 318
Cdd:COG1579 140 LEEKKAELDEELAELEAELEELE 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
140-371 |
2.77e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAarigQSLLKQNQELTArnemLDEQLEIAKEEIAQLRHELTMRDDLLQFYaSTEEIENAESHSPIKRNES 219
Cdd:TIGR00618 368 REISCQQHTLT----QHIHTLQQQKTT----LTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKKQQELQQR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 CSSLSNFvhydFLQQKLKGLEDENRklrlEANELTTETSHYEEQEQELMMVC--VEELSSVNKQVVDLSEELARKVEDSL 297
Cdd:TIGR00618 439 YAELCAA----AITCTAQCEKLEKI----HLQESAQSLKEREQQLQTKEQIHlqETRKKAVVLARLLELQEEPCPLCGSC 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 298 RQQEEISSLLAQIVDLQARCKGLTHEN-------EELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLR 370
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYaqletseEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
.
gi 1675229582 371 N 371
Cdd:TIGR00618 591 N 591
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
125-348 |
2.87e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAVTHLLEEkerdlelaarigqsLLKQNQELTARNEMLDEQL-EIAK--------EEIAQLRHELTMRDDL 195
Cdd:COG0497 159 EYREAYRAWRALKKELEE--------------LRADEAERARELDLLRFQLeELEAaalqpgeeEELEEERRRLSNAEKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 196 LQFYASTEEIENAESHSPIKR-NESCSSLSNFVHYDflqQKLKGLEDENRKLRLEANELTTETSHYEEQ----EQELMMV 270
Cdd:COG0497 225 REALQEALEALSGGEGGALDLlGQALRALERLAEYD---PSLAELAERLESALIELEEAASELRRYLDSlefdPERLEEV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 271 cvEE-LSSVNKqvvdlseeLARK----VEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHN-------LSASRE-- 336
Cdd:COG0497 302 --EErLALLRR--------LARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAEAElleaaekLSAARKka 371
|
250
....*....|....*
gi 1675229582 337 -SQL--KLKSELKDL 348
Cdd:COG0497 372 aKKLekAVTAELADL 386
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-372 |
4.27e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLE-----IAKEEIAQLRHELtmrddllqfyastEEIENAESHSpi 214
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKL-------------EEIQNQISQN-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 215 krNESCSSLSNFVHYdfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMmvcvEELSSVNKQVVDLSEELARKVE 294
Cdd:TIGR04523 334 --NKIISQLNEQISQ--LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK----QEIKNLESQINDLESKIQNQEK 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675229582 295 DSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
125-372 |
5.30e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAVTHLLEEKERDLELAARIGQSLLKQNQELTAR-NEMLDEQLEIAKEeIAQLRHELTmrDDLLQFyasTE 203
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARkQNKYDELVEEAKT-IKAEIEELT--DELLNL---VM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 204 EIENAESHspikrnescsslsnfvhydflqqkLKGLEDENRKLRLEANELTTETSHYEEQEqeLMMVCVEELSSVNKQVV 283
Cdd:PHA02562 249 DIEDPSAA------------------------LNKLNTAAAKIKSKIEQFQKVIKMYEKGG--VCPTCTQQISEGPDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 284 DLSE---ELARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLC 360
Cdd:PHA02562 303 KIKDklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250
....*....|..
gi 1675229582 361 EAREDIKNLRNK 372
Cdd:PHA02562 383 KLQDELDKIVKT 394
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-348 |
6.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 141 EEKERDLELAARIGQSLLKQNQEL-TARNEM--LDEQLEIAKEEIAQLRHELTMRDDLLQfyASTEEIENAESHspIKRN 217
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELeQAREELeqLEEELEQARSELEQLEEELEELNEQLQ--AAQAELAQAQEE--LESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 218 EScsslsnfvHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcVEELSSVNKQVVDLSEELAR-KVEDS 296
Cdd:COG4372 107 QE--------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER----EEELKELEEQLESLQEELAAlEQELQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1675229582 297 LRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDL 348
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
132-340 |
6.72e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 132 DIKAVTHLLEEKERDL--------ELAARIGQsLLKQNQELTARNEMLDEQLEIAKEEIAQLRHEL-TMRDDLLQFYAST 202
Cdd:COG4942 35 EIAELEKELAALKKEEkallkqlaALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRAELeAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 203 EEIENAESHSPIKRNESCSSLSNFVHY-----DFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcVEELSS 277
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYlkylaPARREQAEELRADLAELAALRAELEAERAELEALLAEL----EEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675229582 278 VNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLK 340
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
140-399 |
7.45e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDllqfyasTEEIENAESHSPIKRNES 219
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE-------EEEERSQQLQNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 csslsnfvHYDFLQQKLKGLEDENRKLRLEanELTTEtSHYEEQEQELMMVcVEELSSVNKQVVDLSEELArKVEDSLRQ 299
Cdd:pfam01576 104 --------HIQDLEEQLDEEEAARQKLQLE--KVTTE-AKIKKLEEDILLL-EDQNSKLSKERKLLEERIS-EFTSNLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 300 QEEISSLL--------AQIVDLQARCKGLTHENEELNHNlsasresQLKLKSELKDLQDKYSQCEDMLCEAR-------E 364
Cdd:pfam01576 171 EEEKAKSLsklknkheAMISDLEERLKKEEKGRQELEKA-------KRKLEGESTDLQEQIAELQAQIAELRaqlakkeE 243
|
250 260 270
....*....|....*....|....*....|....*
gi 1675229582 365 DIKNLRNKsLPNSTVQRYTALASVLPMDSLAAEIE 399
Cdd:pfam01576 244 ELQAALAR-LEEETAQKNNALKKIRELEAQISELQ 277
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
153-368 |
7.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 153 IGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELtmrdDLLQfyasteeienaeshspiKRNESCSSLSNfvhYDFL 232
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL----DALQ-----------------ERREALQRLAE---YSWD 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 233 QQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmMVCVEELSSVNKQVVDLSEELARkVEDSLRQ-QEEISSLLAQIV 311
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAALEEQL-EELEAELEELEEELDELKGEIGR-LEKELEQaEEELDELQDRLE 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1675229582 312 DLQARCKGLTHEN--EELNHNLSASRESQLK--LKSELKDLQDKYSQCEDMLCEAREDIKN 368
Cdd:COG4913 738 AAEDLARLELRALleERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
142-361 |
1.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 142 EKERDlELAARIgQSLLKQNQEL-TARNEMLDE-QLEIAKEE-IAQLRHELTMRDDLLQfyastEEIENAESHSPIKRNE 218
Cdd:PRK02224 271 ERERE-ELAEEV-RDLRERLEELeEERDDLLAEaGLDDADAEaVEARREELEDRDEELR-----DRLEECRVAAQAHNEE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 219 ScsslsnfvhyDFLQQKLKGLEDENRKLRLEANELTTEtshyeeqeqelmmvcveeLSSVNKQVVDLSEELarkveDSLR 298
Cdd:PRK02224 344 A----------ESLREDADDLEERAEELREEAAELESE------------------LEEAREAVEDRREEI-----EELE 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675229582 299 qqEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCE 361
Cdd:PRK02224 391 --EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-354 |
1.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 148 ELAARIGQSLLK---------QNQELTARNEMLDEQLEIAKEEIAQLRHELT----------MRDDLLQFYASTEEIENA 208
Cdd:COG3206 148 ELAAAVANALAEayleqnlelRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvdLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 209 ESHSPIKRNESCSSlsnfvhYDFLQQKLKGLEDENRKLrLEANELTTETSHYEEQEQELmmvcvEELSSV----NKQVVD 284
Cdd:COG3206 228 LAEARAELAEAEAR------LAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAEL-----AELSARytpnHPDVIA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675229582 285 LSEELARkVEDSLRQQEE--ISSLLAQIVDLQARCKGLTHENEELNHNLS--ASRESQLK-LKSELKDLQDKYSQ 354
Cdd:COG3206 296 LRAQIAA-LRAQLQQEAQriLASLEAELEALQAREASLQAQLAQLEARLAelPELEAELRrLEREVEVARELYES 369
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-369 |
1.41e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 122 RVGQVTKTYHDIKAVTHLLEEKERDLElaARIGQSLLKQNQELTARNEMLDEQLEIaKEEIAQLRHELtmrDDLLQFYAS 201
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIE--QKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEI---ENLNGKKEE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 202 TEEIenaeshspIKRnescsslsnfvhydfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMVCVEELSSVNKQ 281
Cdd:TIGR02169 866 LEEE--------LEE---------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 282 VVDLS---EELArKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNH-NLSASRESQLKLKsELKDLQDKysqcED 357
Cdd:TIGR02169 923 KAKLEaleEELS-EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLK-RLDELKEK----RA 996
|
250
....*....|..
gi 1675229582 358 MLCEAREDIKNL 369
Cdd:TIGR02169 997 KLEEERKAILER 1008
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
232-382 |
1.49e-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: 41.06 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 232 LQQKLKGLEDENRKLRLEANELTTETSHYEeqeqelmmvcvEELSSVNKQVVDLSEELarkveDSLRQQEEISSLLAQIV 311
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLE-----------LEIEEVEARIKKYEEQL-----GNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 312 DLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRN----------KSLPNSTVQR 381
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEeleaereelaAKIPPELLAL 179
|
.
gi 1675229582 382 Y 382
Cdd:COG1579 180 Y 180
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-371 |
1.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 191 MRDDLLQFYASTEEIENA-ESHSPIKRNES--CSSLSNfVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQel 267
Cdd:PRK02224 154 MIDDLLQLGKLEEYRERAsDARLGVERVLSdqRGSLDQ-LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQRE-- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 268 mmvcveelssvnkQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSE--- 344
Cdd:PRK02224 231 -------------QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErdd 297
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1675229582 345 ------------------LKDLQDKYSQCEDMLCEAREDIKNLRN 371
Cdd:PRK02224 298 llaeaglddadaeavearREELEDRDEELRDRLEECRVAAQAHNE 342
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
125-342 |
1.71e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAVT-HLLEE--------KERDLELAARIGQSLLKQNqeLTARNEMLDEQLEIAKEEIAQLRHELT-MRDD 194
Cdd:TIGR00618 480 QIHLQETRKKAVVlARLLElqeepcplCGSCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDVYHQLTsERKQ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 195 LLQFYASTEEIENAESHSPIKRNESCSSLSNFVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELMMV---C 271
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqqC 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1675229582 272 VEELSSVNKQVVDLSEELAR-KVEDSLRQQEEISSLLAQIVD-----LQARCKGLTHENEELNHNLSASRESQLKLK 342
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQeRVREHALSIRVLPKELLASRQlalqkMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
239-371 |
2.27e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 239 LEDENRKLRLEANELTTETSHYEEQEQELMMVcveelssvNKQVVDLSEELARKVEDSLRQQEEissLLAQIVDLQARCK 318
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEK--------YKELSASSEELSEEKDALLAQRAA---HEARIRELEEDIK 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 319 GLTHENEELNHNLSASRESQLKL-------KSELKDLQDKYSQCEDMLCEAREDIKNLRN 371
Cdd:pfam07888 140 TLTQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKLQQTEEELRSLSKEFQELRN 199
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
178-381 |
3.60e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 178 AKEEIAQLRHELTMRDDLLQFYASTEEIENAESHSPIKRNESCSSLSNFV--HYDFLQQKLKGLEDENRKL-------RL 248
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGgkKYLLLQKQLEQLQEENFRLetarddyRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 249 EANELTTETSHYEEQEQELMMVCVEELS-----SVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHE 323
Cdd:pfam05622 88 KCEELEKEVLELQHRNEELTSLAEEAQAlkdemDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675229582 324 NEELNHNL---SASReSQLKL-KSELKDLQDKYSQcEDMLCEARE-DIKNLRNKslpNSTVQR 381
Cdd:pfam05622 168 TLQLEEELkkaNALR-GQLETyKRQVQELHGKLSE-ESKKADKLEfEYKKLEEK---LEALQK 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-401 |
3.63e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 273 EELSSVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKY 352
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1675229582 353 SQcedMLCEA-----REDIKNLRNKSLPNSTVQRYTALASVLP-MDSLAAEIEGT 401
Cdd:COG4942 107 AE---LLRALyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPaRREQAEELRAD 158
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
293-399 |
5.35e-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: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 293 VEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAREDIKNLRNK 372
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100
....*....|....*....|....*..
gi 1675229582 373 SLPNSTVQRYTALASVLpmDSLAAEIE 399
Cdd:COG1579 82 LGNVRNNKEYEALQKEI--ESLKRRIS 106
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
140-346 |
5.37e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 140 LEEKERDLELAARIgQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQFYASTEEIENAESHSPikrnes 219
Cdd:pfam05557 369 LTMSNYSPQLLERI-EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKE------ 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 csslsnfvHYDFLQQKLKGLEDENRKLRLEANELttetshyeeqEQELMMVCVEELSSVNK-QVVDLSEELARKVEDSLR 298
Cdd:pfam05557 442 --------EVDSLRRKLETLELERQRLREQKNEL----------EMELERRCLQGDYDPKKtKVLHLSMNPAAEAYQQRK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1675229582 299 QQEEisSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELK 346
Cdd:pfam05557 504 NQLE--KLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLR 549
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
139-373 |
6.26e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 139 LLEEKERDLeLAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLQFYASTEEIENAESHSPIKRNE 218
Cdd:pfam10174 200 LLDQKEKEN-IHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQME 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 219 SCSSlsnfvHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEqelmmvcveelsSVNKQVVD-LSEELARKVE--- 294
Cdd:pfam10174 279 VYKS-----HSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQN------------SDCKQHIEvLKESLTAKEQraa 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 295 ------DSLRQQ-EEISSLLA----QIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEAR 363
Cdd:pfam10174 342 ilqtevDALRLRlEEKESFLNkktkQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLK 421
|
250
....*....|
gi 1675229582 364 EDIKNLRNKS 373
Cdd:pfam10174 422 ERVKSLQTDS 431
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
249-337 |
7.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 249 EANELTTETSHYEEQEQELMmvcvEELSSVNKQVVDLSEELARKVEDSLRQQEEISSLLAQIVDLQARckgLTHENEELN 328
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
....*....
gi 1675229582 329 HNLSASRES 337
Cdd:COG3883 90 ERARALYRS 98
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
139-372 |
7.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 139 LLEEKERDLELAARIGQSLLKQNQELTARNEMLDEQLEIAKEEIAQLRHELTMRDDLLqfyastEEI-ENAEshspiKRN 217
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELN------EKVkELKE-----ERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 218 EscsslsnfvhydfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcvEEL------SSVN----KQVVDLSE 287
Cdd:COG1340 82 E-------------LNEKLNELREELDELRKELAELNKAGGSIDKLRKEI-----ERLewrqqtEVLSpeeeKELVEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 288 ELAR---KVEDSLRQQEEISSLLAQIVDLQARCKGLTHENEELNHNLSASRESQLKLKSELKDLQDKYSQCEDMLCEARE 364
Cdd:COG1340 144 ELEKeleKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
....*...
gi 1675229582 365 DIKNLRNK 372
Cdd:COG1340 224 KADELHEE 231
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
149-310 |
8.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 149 LAARIGQSLLKQNQELTAR---------NEMLDEQLEIAKEEIAQLRHELtmrddllqfyasteEIENAESHSPIKRNES 219
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRileeakkeaEAIKKEALLEAKEEIHKLRNEF--------------EKELRERRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 220 csslSNFVHYDFLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQELmmvcvEELssVNKQVVDL-------SEE---- 288
Cdd:PRK12704 90 ----RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-----EEL--IEEQLQELerisgltAEEakei 158
|
170 180
....*....|....*....|..
gi 1675229582 289 LARKVEDSLRqqEEISSLLAQI 310
Cdd:PRK12704 159 LLEKVEEEAR--HEAAVLIKEI 178
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-375 |
8.69e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 125 QVTKTYHDIKAVTHLLEEKERDLELAARIGQSLLKQNQELTARNEMLD--EQLEIAKEEIAQLRHELTMRDDLLQFYAst 202
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTRTQMEMLTK-- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 203 eeiENAESHSPIKRNESCSS---------------LSNFVHYdfLQQKLKGLEDENRKLRLEANELTTETSHYEEQEQEL 267
Cdd:TIGR00606 543 ---DKMDKDEQIRKIKSRHSdeltsllgyfpnkkqLEDWLHS--KSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675229582 268 mmvcVEELSSVNKQVVDLS---------EELARKVEDSLRQQEEI-------SSLLAQIVDLQARCKGLTH-------EN 324
Cdd:TIGR00606 618 ----EEQLSSYEDKLFDVCgsqdeesdlERLKEEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCQrvfqteaEL 693
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1675229582 325 EELNHNL-SASRESQLKLKSELKDLQDKYSQCEDML--CEAREDIKNLRNKSLP 375
Cdd:TIGR00606 694 QEFISDLqSKLRLAPDKLKSTESELKKKEKRRDEMLglAPGRQSIIDLKEKEIP 747
|
|
| |
