|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
904-1212 |
5.73e-66 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 224.91 E-value: 5.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 904 EGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVST-SYIKVWDIRDSaK 980
Cdd:cd00200 6 KGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDLETG-E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 981 CIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGKLTGHIGPVMCLT 1059
Cdd:cd00200 85 CVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1060 VTQTasqHDLVVTGSKDHYVKMFELGecvtgTIGPTHNFEPpHYDGIECLAIQGD--ILFSGSRDNGIKKWDLDQQELIQ 1137
Cdd:cd00200 143 FSPD---GTFVASSSQDGTIKLWDLR-----TGKCVATLTG-HTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 1138 QIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDCRVKLWN 1212
Cdd:cd00200 214 TLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
893-1212 |
4.44e-48 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 177.41 E-value: 4.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 893 RTAPLQCVSMAEGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYcSHSG-LVFSVSTSY 969
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF-SPDGkLLASGSDDG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 970 -IKVWDIrDSAKCIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGK 1047
Cdd:COG2319 185 tVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLLRT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1048 LTGHIGPVMCLTVTqtasqHD--LVVTGSKDHYVKMFELGecvTGTIGPTHnfePPHYDGIECLAI--QGDILFSGSRDN 1123
Cdd:COG2319 242 LTGHSGSVRSVAFS-----PDgrLLASGSADGTVRLWDLA---TGELLRTL---TGHSGGVNSVAFspDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1124 GIKKWDLDQQELIQQIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAICTNA--KHIFT 1201
Cdd:COG2319 311 TVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPdgRTLAS 389
|
330
....*....|.
gi 2462506429 1202 ASSDCRVKLWN 1212
Cdd:COG2319 390 GSADGTVRLWD 400
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
528-609 |
3.72e-42 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.
Pssm-ID: 410203 [Multi-domain] Cd Length: 82 Bit Score: 148.80 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 528 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 607
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 2462506429 608 TK 609
Cdd:cd22262 81 TK 82
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
904-1175 |
3.82e-40 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 153.91 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 904 EGHTKPILCL--DATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVST-SYIKVWDIrDSAK 980
Cdd:COG2319 159 TGHSGAVTSVafSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSAdGTVRLWDL-ATGK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 981 CIRTLTSSGqvisgdacaatstraitsaqgeHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGKLTGHIGPVMCLT 1059
Cdd:COG2319 238 LLRTLTGHS----------------------GSVRSVAFSPDGRLLASGSAdGTVRLWDLATGELLRTLTGHSGGVNSVA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1060 VTQTAsqhDLVVTGSKDHYVKMFELGecvTGTIGPTHnfePPHYDGIECLAI--QGDILFSGSRDNGIKKWDLDQQELIQ 1137
Cdd:COG2319 296 FSPDG---KLLASGSDDGTVRLWDLA---TGKLLRTL---TGHTGAVRSVAFspDGKTLASGSDDGTVRLWDLATGELLR 366
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462506429 1138 QIpNAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDN 1175
Cdd:COG2319 367 TL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
528-609 |
1.08e-27 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 107.32 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 528 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 607
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 2462506429 608 TK 609
Cdd:cd22263 81 AK 82
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
528-609 |
2.74e-26 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 103.44 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 528 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKgLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 607
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKDESV-LRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 2462506429 608 TK 609
Cdd:cd22248 80 SK 81
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1113-1216 |
1.35e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 80.34 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1113 GDILFSGSRDNGIKKWDLDQQELIQQiPNAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAI 1192
Cdd:COG2319 90 GRLLASASADGTVRLWDLATGLLLRT-LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSV 168
|
90 100
....*....|....*....|....*.
gi 2462506429 1193 CTNA--KHIFTASSDCRVKLWNYVPG 1216
Cdd:COG2319 169 AFSPdgKLLASGSDDGTVRLWDLATG 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-441 |
3.12e-13 |
|
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: 72.87 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 232 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV---LQNLSTMECYTEEKANKIKAD 308
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 309 YEKRLR---------------------EMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE 367
Cdd:COG4942 106 LAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506429 368 EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRlAKPMSERVAGRAGLKPP 441
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLPWP 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
241-684 |
2.35e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 241 EIEIKQKLIDELENSQRRLQTL---KHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANkikadyEKRLREMN 317
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL------EAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 318 RDLQKLQAAQKEHARLlknqsryERELKKLQAEVAEMKKAKVALMKQMREEqQRRRLVETKRNRE-----IAQLKKEQRR 392
Cdd:COG4717 146 ERLEELEERLEELREL-------EEELEELEAELAELQEELEELLEQLSLA-TEEELQDLAEELEelqqrLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 393 QEFQIRALESQKRQ--QEMVLRRKTQEVSALRRLAKPMSERVAG--------------------RAGLKPPMLDSGAEVS 450
Cdd:COG4717 218 AQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALlglggsllsliltiagvlflVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 451 ASTTSSEAESGARSVSSIVRQwnRKINHFLGDHPAPTVNGTRPARKKFQ-----KKGASQSFSKAARLKWQSLERRIIDI 525
Cdd:COG4717 298 ASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDrieelQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 526 VmqRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQ-----ELAEEIEVLAANIDYINDGITDCQA 600
Cdd:COG4717 376 L--AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 601 TIVQLEETKEELDSTDTsvvisscsLAEARllldnflkasidkgLQVAQKEAQIRLLEGRLRQTDMAGSsqnhlLLDALR 680
Cdd:COG4717 454 ELAELEAELEQLEEDGE--------LAELL--------------QELEELKAELRELAEEWAALKLALE-----LLEEAR 506
|
....
gi 2462506429 681 EKAE 684
Cdd:COG4717 507 EEYR 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-448 |
1.35e-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: 62.77 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 232 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDtqLERDRVLQNlstmecyteEKANKIKADYEK 311
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR--LEQQKQILR---------ERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 312 RLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetKRNREIAQLKKEQR 391
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----TLRSKVAQLELQIA 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506429 392 RQEFQIRALESQKRQQEMVLRRKTQEVSAL-RRLAKPMSERVAGRAGLKPPMLDSGAE 448
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQE 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
300-691 |
5.87e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 300 EKANKIKADYEKR--------LREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKAKVALMKQMREEQQR 371
Cdd:COG1196 213 ERYRELKEELKELeaellllkLRELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 372 RRLVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSA 451
Cdd:COG1196 290 EYELL----AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 452 STTSSEAESGARsvSSIVRQWNRKinhflgdhpaptvngtrpARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMT 531
Cdd:COG1196 363 AEEALLEAEAEL--AEAEEELEEL------------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 532 IVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEE 611
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 612 LDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQA 691
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
231-692 |
6.29e-09 |
|
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: 60.52 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 231 FQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYE 310
Cdd:pfam15921 315 YMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----DQLQKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 311 KRLREMNrdLQKLQAaQKEHARLLKNQ---SRYERELKKLQAEVAEMKkakvALMKQMREEQQrrrlveTKRNREIAQLK 387
Cdd:pfam15921 388 KREKELS--LEKEQN-KRLWDRDTGNSitiDHLRRELDDRNMEVQRLE----ALLKAMKSECQ------GQMERQMAAIQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 388 KEQRRQEfQIRALESQKRQQEMVLRRKTQEVSAlRRLAKPMSERVAG-------------------------RAGLKPPM 442
Cdd:pfam15921 455 GKNESLE-KVSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVSdltaslqekeraieatnaeitklrsRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 443 L----DSGAEVSASTTSSEA----ESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFS-- 508
Cdd:pfam15921 533 LqhlkNEGDHLRNVQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKil 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 509 ---KAARLKwqSLERRIIDIVMQRMTIVNleADMERLIKKREelfllqeaLRRKRERLQAESPEEEKGLQELAEEIEVLA 585
Cdd:pfam15921 613 kdkKDAKIR--ELEARVSDLELEKVKLVN--AGSERLRAVKD--------IKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 586 ANIDYINDGI-TDCQATIVQLEETKEELDSTDTSVVISSCSLAEArllldnfLKASIDKGLQVAQKEAQIRLLEGRLRQT 664
Cdd:pfam15921 681 RNFRNKSEEMeTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA-------MKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
490 500 510
....*....|....*....|....*....|.
gi 2462506429 665 DMAGSSQN---HLLLDalrEKAEAHPELQAL 692
Cdd:pfam15921 754 EEAMTNANkekHFLKE---EKNKLSQELSTV 781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-614 |
6.87e-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: 60.46 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 301 KANKIKAdyEKRLREMNRDLQKLQAAQKEHARLLKN---QSRYERELKKLQAEVAEMKKAKVAL-MKQMREEQQRRRLVE 376
Cdd:TIGR02168 171 KERRKET--ERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELALLVLrLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 377 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA-GRAGLKPpmlDSGAEVSASTTS 455
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQiLRERLAN---LERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 456 SEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQsfskAARLKWQSLERRIIDIVMQ----RMT 531
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLELQiaslNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 532 IVNLEADMERLIKKREELFLLQEALRRK-----RERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLE 606
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
....*...
gi 2462506429 607 ETKEELDS 614
Cdd:TIGR02168 482 RELAQLQA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-663 |
7.77e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 142 RAKQDLERLKKKEVRQRRKspeKEAFKKRAKLQQEnseeTDENEAEEEEEERDESGC--------EEEEGREDEDEDSGS 213
Cdd:COG1196 216 RELKEELKELEAELLLLKL---RELEAELEELEAE----LEELEAELEELEAELAELeaeleelrLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 214 EESLVDSDSDPEEKEVNF-QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLS 292
Cdd:COG1196 289 EEYELLAELARLEQDIARlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 293 TMECYTEEKANKIKADYEKRLREMNR---DLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQ 369
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 370 QRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQ-QEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAE 448
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEElAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 449 V----SASTTSSEAESGARSVSSIVRQWNR--KINHFLGDHPAPTVN---GTRPARKKFQKKGASQSFSKAARLKWQSLE 519
Cdd:COG1196 529 LigveAAYEAALEAALAAALQNIVVEDDEVaaAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 520 R---------------RIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVL 584
Cdd:COG1196 609 ReadaryyvlgdtllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 585 AANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARL-----------LLDNFLKASIDKGLQVAQKEAQ 653
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREelleelleeeeLLEEEALEELPEPPDLEELERE 768
|
570
....*....|
gi 2462506429 654 IRLLEGRLRQ 663
Cdd:COG1196 769 LERLEREIEA 778
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
241-417 |
1.74e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.98 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 241 EIEIKQKLIDELEnsqrRLQTLKHQYEEKL---ILLQNKIRDTQLERDR-VLQNLSTMECYTEEKAN----KIKADYEKR 312
Cdd:pfam17380 369 EIAMEISRMRELE----RLQMERQQKNERVrqeLEAARKVKILEEERQRkIQQQKVEMEQIRAEQEEarqrEVRRLEEER 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 313 LREMNRDLQKLQAAQKEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQ----RRRLVETKRNREIAQLKK 388
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERL--RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKLLEKEM 522
|
170 180 190
....*....|....*....|....*....|....
gi 2462506429 389 EQRR----QEFQIRALESQKR-QQEMVLRRKTQE 417
Cdd:pfam17380 523 EERQkaiyEEERRREAEEERRkQQEMEERRRIQE 556
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
222-495 |
2.41e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 222 SDPEEKEVnfQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEklilLQNKIRDTQLERDRVLQNLSTmecyTEEK 301
Cdd:COG3883 14 ADPQIQAK--QKELSELQAEL---EAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAE----AEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 302 ANKIKADYEKRLREMNRD----------------------LQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 359
Cdd:COG3883 81 IEERREELGERARALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 360 ALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLK 439
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506429 440 PPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPAR 495
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-613 |
2.45e-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: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 232 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcYTEEKANKIKADYEK 311
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 312 RLREMNRDLQKLQAAQKEHarllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQR----RRLVETKRNReIAQLK 387
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEA----------EAEIEELEAQIEQLKEELKALREALDELRAEltllNEEAANLRER-LESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 388 KEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPpmldsgaevSASTTSSEAESGARSVSS 467
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------SLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 468 IVRQWNRKInhflgdhpaptvngtRPARKKFQKKGASQSfskAARLKWQSLERRIIDIVMQRMTIVNLEADMerLIKKRE 547
Cdd:TIGR02168 902 ELRELESKR---------------SELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEE--AEALEN 961
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506429 548 ELFLLQEALRRKRERLQAEspeeekgLQELA-------EEIEVLAANIDYINDGITDCQATIVQLEETKEELD 613
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENK-------IKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-693 |
2.47e-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: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 371 RRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVagraglkppmldSGAEVS 450
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI------------SALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 451 ASTTSSEAESGARSVSSIVRQWNRKINHFLGDHpaptvngtrparkkfQKKGASQSFSKAARLKWQSLERRIidivmQRM 530
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELE---------------ERLEEAEEELAEAEAEIEELEAQI-----EQL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 531 TIvNLEADMERLIKKREELFLLQEALRRKRER---LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQAtivQLEE 607
Cdd:TIGR02168 795 KE-ELKALREALDELRAELTLLNEEAANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE---LIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 608 TKEELDSTDTSVVISSCSLAEARLLLDNFlkasiDKGLQVAQKEAQiRLLEGRLRQTDMAGSSQNHL---------LLDA 678
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEEL-----SEELRELESKRS-ELRRELEELREKLAQLELRLeglevridnLQER 944
|
330
....*....|....*....
gi 2462506429 679 LREK----AEAHPELQALI 693
Cdd:TIGR02168 945 LSEEysltLEEAEALENKI 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-692 |
5.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 214 EESLVDSDSDPEEKEVNF---QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLE----RDR 286
Cdd:TIGR02168 322 EAQLEELESKLDELAEELaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 287 VLQNLSTMEcYTEEKANKIKADYEKRLREMNR-DLQKLQAAQKEHARLLKN----QSRYERELKKLQAEVAEMKKAKVAL 361
Cdd:TIGR02168 402 IERLEARLE-RLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEElqeeLERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 362 MKQMREEQQRRRLVETKRN------REIAQLKKEQRR---------------QEFQiRALES--QKRQQEMVLRRKTQEV 418
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQEnlegfsEGVKALLKNQSGlsgilgvlselisvdEGYE-AAIEAalGGRLQAVVVENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 419 SALRRLAKPMServaGRAGLKPPMLDSGAEVSASTTSS-EAESGARSVSSIVR----QWNRKINHFLGD-HPAPTV-NGT 491
Cdd:TIGR02168 560 KAIAFLKQNEL----GRVTFLPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVkfdpKLRKALSYLLGGvLVVDDLdNAL 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 492 RPARKK------FQKKG----ASQSFSKAARLKWQS-LERRI-IDIVMQRMT-----IVNLEADMERLIKKREELFLLQE 554
Cdd:TIGR02168 636 ELAKKLrpgyriVTLDGdlvrPGGVITGGSAKTNSSiLERRReIEELEEKIEeleekIAELEKALAELRKELEELEEELE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 555 ALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTdtsvvisscsLAEARLLLD 634
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE----------LAEAEAEIE 785
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 635 NfLKASIDKGL-QVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQAL 692
Cdd:TIGR02168 786 E-LEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-683 |
5.57e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLIDELEnsqRRLQTLKHQYEE----KLILLQNKIRDTQLERDRVLQNLSTME--CYT 298
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALR---EELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEalLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 299 -EEKANKIKADYEKRLREMNRDLQKLQ----AAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRR 373
Cdd:COG4913 371 lGLPLPASAEEFAALRAEAAALLEALEeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 374 LVETKRNREIA--------QLKKEQRRQEFQI-RALESQKRqqeMVLRRKTQEVSALRRL-AKPMSERVAGRaGLKPpml 443
Cdd:COG4913 449 LAEALGLDEAElpfvgeliEVRPEEERWRGAIeRVLGGFAL---TLLVPPEHYAAALRWVnRLHLRGRLVYE-RVRT--- 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 444 dsgAEVSASTTSSEAESGARSVS---SIVRQW-NRKINHF-----------LGDHP-APTVNG------TRpARKKFQKK 501
Cdd:COG4913 522 ---GLPDPERPRLDPDSLAGKLDfkpHPFRAWlEAELGRRfdyvcvdspeeLRRHPrAITRAGqvkgngTR-HEKDDRRR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 502 GASQS---FSKAARLKWqsLERRIidivmqrmtiVNLEADMERLIKKREELFLLQEALRRKRERLQ--AESPEEEKGLQE 576
Cdd:COG4913 598 IRSRYvlgFDNRAKLAA--LEAEL----------AELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVAS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 577 LAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDstdtsvvisscslaEARLLLDNFLKASIDKGLQVAQKEAQIRL 656
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELE--------------ELEEELDELKGEIGRLEKELEQAEEELDE 731
|
490 500
....*....|....*....|....*..
gi 2462506429 657 LEGRLRQTDMAGSSQNHLLLDALREKA 683
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAA 758
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-433 |
9.32e-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: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLER---DRVLQNLSTMECYTEEK 301
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeelEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 302 ANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRR--------- 372
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeslaaeiee 863
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462506429 373 -RLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 433
Cdd:TIGR02168 864 lEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-421 |
1.12e-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: 56.61 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 131 SSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKraKLQQEnseetdeneAEEEEEERDESGCEEEEGREDEDED 210
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS--SLEQE---------IENVKSELKELEARIEELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 211 SGSEESLVDSDSDPEEKEVnfQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDrvlqn 290
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK----- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 291 lstMECYTEEkankikaDYEKRLREMNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKkakvalmKQMREEQQ 370
Cdd:TIGR02169 851 ---SIEKEIE-------NLNGKKEELEEELEELEAALRD----------LESRLGDLKKERDELE-------AQLRELER 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 371 RRRLVETKRNRE---IAQLKKEQRRQEFQIRALESQKRQQE-------------MVLRRKTQEVSAL 421
Cdd:TIGR02169 904 KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEeipeeelsledvqAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-412 |
1.13e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 75 ALIQNYIREIEELRTKLLESEAMNESLRRSLsrasarspyslgaspaapafggspassmEDASEVIRRAKQDLERLKKKE 154
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKAL----------------------------AELRKELEELEEELEQLRKEL 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 155 VRQRRKSPEKEAFKKRAKLQQENseetdeneaeeEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQAD 234
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQ-----------LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 235 LADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcYTEEKANKIKADYEKRLR 314
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS-EDIESLAAEIEELEELIE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 315 EMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNreiaqlKKEQRRQE 394
Cdd:TIGR02168 870 ELESELEALLNERASLEEALA---LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE------GLEVRIDN 940
|
330
....*....|....*...
gi 2462506429 395 FQIRALESQKRQQEMVLR 412
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEA 958
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-437 |
2.46e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 232 QADLADLTCEIEIKQKLIDELENsqrRLQTLKHQYEEKLILLQNKIRDTQLE----RDRVLQNLSTMECYteekaNKIKA 307
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRA---ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYL-----KYLAP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 308 DYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLK 387
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-------AELAELQ 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462506429 388 KEQRRQEFQIRALESQKRQQEmvLRRKTQEVSALR-RLAKPMSERVAGRAG 437
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAA--ERTPAAGFAALKgKLPWPVSGRVVRRFG 268
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-433 |
3.42e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDtqLERDRVLQNLSTMECYTEeKANK 304
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELS-KLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 305 IKADYEKRLREMNRDLQKL----QAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRn 380
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL- 884
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462506429 381 reiAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 433
Cdd:TIGR02169 885 ---GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
307-440 |
3.98e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.48 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 307 ADYEKRLREMNRDLQKLQAaqkeHARLLKNQSR-YERELKKLQAEVAEMKKakvalmkQMREEQQRRRLVeTKRNREIAQ 385
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEA----EVEELEAELEeKDERIERLERELSEARS-------EERREIRKDREI-SRLDREIER 476
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 386 LKKEQRRQEFQIRALESQ----KRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKP 440
Cdd:COG2433 477 LERELEEERERIEELKRKlerlKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-704 |
7.83e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 301 KANKIKAdyEKRLREMNRDLQKLQAAQKEharlLKNQsryereLKKL--QAEVA--------EMKKAKVALM-KQMREEQ 369
Cdd:COG1196 171 KERKEEA--ERKLEATEENLERLEDILGE----LERQ------LEPLerQAEKAeryrelkeELKELEAELLlLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 370 QRRRLVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRrlakpmservagraglkppmldsGAEV 449
Cdd:COG1196 239 AELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-----------------------AEEY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 450 SASTTSSEAEsgarsvssivrqwnrkinhflgdhpaptvngtrpARKKFQKKGASQSFSKAARLKWQ--SLERRIIDIVM 527
Cdd:COG1196 292 ELLAELARLE----------------------------------QDIARLEERRRELEERLEELEEElaELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 528 QRMT----IVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIV 603
Cdd:COG1196 338 ELEEleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 604 QLEETKEELDStdtsvvisscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKA 683
Cdd:COG1196 418 RLEEELEELEE----------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
410 420
....*....|....*....|.
gi 2462506429 684 EAHPELQALIYNVQQENGYAS 704
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLE 508
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
269-658 |
1.16e-06 |
|
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: 52.59 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 269 KLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKAD---YEKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELK 345
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRVAELK---EELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 346 KLQAEVAEMKKAKVALMKQMREEQQRRRLVE----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKT 415
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 416 QEvsaLRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTS------SEAESGA-----RSVSSIVRQWNRKINhFLGDHP 484
Cdd:pfam07888 185 EE---LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEAlleelRSLQERLNASERKVE-GLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 485 APTVNgtrparkkfqKKGASQSFSKAARLKWQSLERRIIDIVMQ-----------RMTIV-NLEADMERLIKkreelflL 552
Cdd:pfam07888 261 SSMAA----------QRDRTQAELHQARLQAAQLTLQLADASLAlregrarwaqeRETLQqSAEADKDRIEK-------L 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 553 QEALRRKRERLQAESPEEEKGLQELAEEievlaanidyindgiTDCqaTIVQLEETKEELDStdtsvvisscslaearll 632
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEVELGRE---------------KDC--NRVQLSESRRELQE------------------ 368
|
410 420
....*....|....*....|....*.
gi 2462506429 633 ldnfLKASidkgLQVAQKEAQIRLLE 658
Cdd:pfam07888 369 ----LKAS----LRVAQKEKEQLQAE 386
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
241-423 |
1.26e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 241 EIEIKQKLIDELENSQRRLQTLKHQYEEKLILL-------QNKIRDTQLERDRVLQNLSTMECYTE-------------E 300
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeklniQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqiselkK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 301 KANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKR 379
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKE 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462506429 380 NREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRR 423
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-454 |
1.36e-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: 52.76 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLIDELEN-SQRRLQTL-------KHQYEEKLILLQNKIRDTQLERdrvlqnlstmec 296
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKrLEEIEQLLeelnkkiKDLGEEEQLRVKEKIGELEAEI------------ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 297 yteEKANKIKADYEKRLREMNRDLQKLQAaqkEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVE 376
Cdd:TIGR02169 304 ---ASLERSIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506429 377 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTT 454
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
272-417 |
1.89e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 272 LLQNKIRDTQLERDRVLQNLST-MECYTEEK-------ANKIKADYEKRLREMNRDLQKLQAaqkehaRLLKNQSRYERE 343
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKeAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEK------RLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 344 LKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR------EIAQLKKEQRRQEfQIRALESQKRQQEMVLRRKTQE 417
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqeleRISGLTAEEAKEI-LLEKVEEEARHEAAVLIKEIEE 180
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-582 |
2.50e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 138 EVIRRAKqdlERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESL 217
Cdd:PTZ00121 1215 EEARKAE---DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 218 VDSDSDPEEKEvnfQADLADLTCEIEIK-QKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV--------L 288
Cdd:PTZ00121 1292 ADEAKKAEEKK---KADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeA 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 289 QNLSTMECYTEEKANKIKADYEKRLREMNR---------DLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 359
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKkaeedkkkaDELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 360 ALMK--QMREEQQRRRLVETKRNREIAQLKKEQRRQ--EFQIRALESQKRQQEmvLRRKTQEVSALRRLAKPMSERVAGR 435
Cdd:PTZ00121 1449 AKKKaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADE 1526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 436 A-----GLKPPMLDSGAEVSASTTSSEAES--GARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPAR-KKFQKKGASQSF 507
Cdd:PTZ00121 1527 AkkaeeAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARiEEVMKLYEEEKK 1606
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 508 SKAARLKWQSLERRIIDIVMQ----RMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIE 582
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-430 |
2.91e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 36 RVKAMQEAIDAINNRVTQLMSQEANLllakagdgNEAIGALIQNYiREIEELRTKLLESEAMNESLRRSLSRASARspys 115
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPEL--------REELEKLEKEV-KELEELKEEIEELEKELESLEGSKRKLEEK---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 116 lgaspaapafggspassMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENseetdeneaeeeeeerde 195
Cdd:PRK03918 261 -----------------IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY------------------ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 196 sgceeeegredededsgseeslvdsdsdpEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLqN 275
Cdd:PRK03918 306 -----------------------------LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-E 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 276 KIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLqaaQKEHARLLKNQSRYERELKKLQAEVAEMK 355
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI---EEEISKITARIGELKKEIKELKKAIEELK 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 356 KAK--VALMKQMREEQQRRRLVEtKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLrRKTQEVSALRRLAKPMSE 430
Cdd:PRK03918 433 KAKgkCPVCGRELTEEHRKELLE-EYTAELKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKELAEQLKE 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
323-623 |
4.49e-06 |
|
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: 50.53 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 323 LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRRLVETkrNREIAQLKKEQRRQEFQIRALES 402
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAAL--ARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 403 QKRQQEMVLRRKTQEVSalRRLakpmseRVAGRAGLKPPMLdsgaevsasttsseaesgarsvssivrqwnrkinhFLgd 482
Cdd:COG4942 91 EIAELRAELEAQKEELA--ELL------RALYRLGRQPPLA-----------------------------------LL-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 483 hpaptvngtrparkkFQKKGASQSFSKAARLKwQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRER 562
Cdd:COG4942 126 ---------------LSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506429 563 LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISS 623
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
249-403 |
4.51e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 249 IDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKaDYEKRLrEMNRDLQKLQAAQK 328
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQL-GNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506429 329 EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQ 403
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
243-409 |
4.63e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 49.00 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 243 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnkirdTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQK 322
Cdd:pfam14988 22 KLWNQYVQECEEIERRRQELASRYTQQTAELQ-----TQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 323 LQAA-----QKEHARLLKNQSRYERELKKLQA-EVAEMKKAKVALMKQMREEQQRRRLVETKRN--REIAQLKKEQRRQE 394
Cdd:pfam14988 97 VRAEtaekdREAHLQFLKEKALLEKQLQELRIlELGERATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQLI 176
|
170
....*....|....*
gi 2462506429 395 FQIRALESQKRQQEM 409
Cdd:pfam14988 177 QETQALEAIKSKLEN 191
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
242-430 |
5.98e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 50.06 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 242 IEIKQ---KLIDELENSQRRLQTLKHQyeeklillQNKIRDTQLERDRVLQNLSTMECYTE----EKANKIKADyEKRLr 314
Cdd:pfam15742 62 AELKQaqqKLLDSTKMCSSLTAEWKHC--------QQKIRELELEVLKQAQSIKSQNSLQEklaqEKSRVADAE-EKIL- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 315 emnrDLQKlqaaQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETK-----------RNREi 383
Cdd:pfam15742 132 ----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNvnelqqqvrslQDKE- 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462506429 384 AQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSE 430
Cdd:pfam15742 203 AQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSS 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
81-583 |
6.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 81 IREIEELR-----TKLLESEAMNESLRRSlsrASARSPYSLGASPAAPAFGGSPASSMEDASEV-----IRRA--KQDLE 148
Cdd:PTZ00121 1229 VKKAEEAKkdaeeAKKAEEERNNEEIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKkkadeAKKAeeKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 149 RLKKKEVRQRRKSPEK---EAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPE 225
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 226 EKEVNFQADLADLTCEiEIKQKlIDEL---ENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTmECYTEEKA 302
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAE-EDKKK-ADELkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 303 NKiKADYEKRLREMnrdlqKLQAAQKEHARLLKNQSRyERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNRE 382
Cdd:PTZ00121 1463 KK-KAEEAKKADEA-----KKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 383 IAQLKK-EQRRQEFQIRALESQKRQQEM--VLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAE 459
Cdd:PTZ00121 1536 ADEAKKaEEKKKADELKKAEELKKAEEKkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 460 SGARSVSSIVRQWN--RKINHFLGDHPAPTVNGTRPARK--KFQKKGASQSFSKAARLKWQSLERRiidivmqrmtivnl 535
Cdd:PTZ00121 1616 EEAKIKAEELKKAEeeKKKVEQLKKKEAEEKKKAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAK-------------- 1681
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2462506429 536 EADMERliKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEV 583
Cdd:PTZ00121 1682 KAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-432 |
6.95e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 249 IDELENSQRRLQTLKHQY-----EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKL 323
Cdd:COG4913 264 YAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 324 QA----AQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQrrrlvetkrnrEIAQLKKEQRRQEFQIRA 399
Cdd:COG4913 344 EReierLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE-----------ALEEELEALEEALAEAEA 412
|
170 180 190
....*....|....*....|....*....|...
gi 2462506429 400 LESQKRQQemvLRRKTQEVSALRRLAKPMSERV 432
Cdd:COG4913 413 ALRDLRRE---LRELEAEIASLERRKSNIPARL 442
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
510-711 |
8.05e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 510 AARLKWQSLERRIIDivmQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANID 589
Cdd:COG1196 229 LLLLKLRELEAELEE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 590 YINDGITDCQATIVQLEETKEELDSTDTSVVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGS 669
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462506429 670 SQNHLLLDALREKAEAHPELQALIynvQQENGYASTDEEISE 711
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEE 421
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
251-431 |
1.09e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 251 ELENSQRRLQTLKhqyEEKLILLQNKIRDT---QLER----DRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKL 323
Cdd:pfam17380 354 RQEERKRELERIR---QEEIAMEISRMRELerlQMERqqknERVRQEL--------EAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 324 QA--AQKEHAR---LLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKEQRRqefQIR 398
Cdd:pfam17380 423 EQirAEQEEARqreVRRLEEERAREMERVRLEEQE-RQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQRR---KIL 497
|
170 180 190
....*....|....*....|....*....|...
gi 2462506429 399 ALESQKRQQEMVlrrktQEVSALRRLAKPMSER 431
Cdd:pfam17380 498 EKELEERKQAMI-----EEERKRKLLEKEMEER 525
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
255-436 |
1.11e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 255 SQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQK--EHAR 332
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERkrELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 333 LLKNQSRYE----RELKKLQ-----------AEVAEMKKAKV-------------ALMKQMREEQqrrrlvETKRNREIA 384
Cdd:pfam17380 365 IRQEEIAMEisrmRELERLQmerqqknervrQELEAARKVKIleeerqrkiqqqkVEMEQIRAEQ------EEARQREVR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462506429 385 QLKKEQRRQEFQIRaLESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRA 436
Cdd:pfam17380 439 RLEEERAREMERVR-LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-661 |
1.12e-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: 50.06 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 340 YERELKKLQAEVAEM--------KKAKVALMKQMREEQQRRRLVETKR--NREIAQLKKEQRRQEFQIRALESQKRQQEM 409
Cdd:TIGR02168 675 RRREIEELEEKIEELeekiaeleKALAELRKELEELEEELEQLRKELEelSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 410 VLRRKT-QEVSALRRLAKPMSERVAG---RAGLKPPMLDSGAEVSASttsseaESGARSVSSIVRQWNRKINhflgdhpa 485
Cdd:TIGR02168 755 ELTELEaEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKAL------REALDELRAELTLLNEEAA-------- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 486 ptvngtrparkkfqkkgasqsfskAARLKWQSLERRIID----IVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRE 561
Cdd:TIGR02168 821 ------------------------NLRERLESLERRIAAterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 562 RLQAESPEEE-------KGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSvvISSCSLAEARLLLD 634
Cdd:TIGR02168 877 ALLNERASLEealallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN--LQERLSEEYSLTLE 954
|
330 340
....*....|....*....|....*..
gi 2462506429 635 NFLKASIDKGLQVAQKEAQIRLLEGRL 661
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-431 |
1.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 311 KRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK--AKVALMKQMREEQQRRRLVETKRNREIAQLKK 388
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462506429 389 EQRRQEfQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 431
Cdd:COG4717 151 LEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1175-1212 |
1.43e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.07 E-value: 1.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2462506429 1175 NFTPIGEIKGHDSPINAIC--TNAKHIFTASSDCRVKLWN 1212
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
313-429 |
1.67e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 313 LREMNRDLQKLQAAQkehARLLKNQSRYERELKKLQAEVAEMKK-------------AKVALMKQMREEQQRRRLvetkr 379
Cdd:COG1842 32 IRDMEEDLVEARQAL---AQVIANQKRLERQLEELEAEAEKWEEkarlalekgredlAREALERKAELEAQAEAL----- 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462506429 380 NREIAQLKKEQRRQEFQIRALESQ----KRQQEMVL-RRKTQEvsALRRLAKPMS 429
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKleelKAKKDTLKaRAKAAK--AQEKVNEALS 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
273-426 |
1.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 273 LQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKAdYEKRLREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVA 352
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQ-LEEELEELNEQLQAAQAELAQAQEELE---SLQEEAEELQEELE 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 353 EMKKAKVALM---KQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALEsqKRQQEMVLRRKTQEVSALRRLAK 426
Cdd:COG4372 119 ELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE--QELQALSEAEAEQALDELLKEAN 193
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
82-628 |
2.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 82 REIEELRTKLLESEAMNESLRRSLSRASArspyslgASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKS 161
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKK-------AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 162 PEK---EAFKKRA----KLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQAD 234
Cdd:PTZ00121 1388 EEKkkaDEAKKKAeedkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 235 LADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQL---ERDRVLQNLSTMEcyTEEKANKIKADYEK 311
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAE--EAKKADEAKKAEEK 1545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 312 RLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVA-EMKKAKVALMKQMREEQQRRRLVETKRNREiAQLKKEQ 390
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 391 RRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAglkppmldSGAEVSASTTSSEAESGARSVSSIVR 470
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA--------EEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 471 QwnrkinhflgdhpaptvngTRPARKKFQ-KKGASQSFSKAARLKWQSLERRIidivmqrmTIVNLEADMERLIKKREEL 549
Cdd:PTZ00121 1697 E-------------------AEEAKKAEElKKKEAEEKKKAEELKKAEEENKI--------KAEEAKKEAEEDKKKAEEA 1749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 550 FLLQE-----ALRRKRERLQAESPEEEKGL---QELAEEIEVLAANIDYINDGITDCQATIVQ--------LEETKEELD 613
Cdd:PTZ00121 1750 KKDEEekkkiAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFANIIEggkegnlvINDSKEMED 1829
|
570
....*....|....*
gi 2462506429 614 STDTSVVISSCSLAE 628
Cdd:PTZ00121 1830 SAIKEVADSKNMQLE 1844
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
245-433 |
3.19e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 245 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLsTMECYTEEKANKIKADYEKRlREMNRDLQKLQ 324
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL-YQEEQERKERQKEREEAEKK-ARQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 325 AAQKEHARLLKnqsryerelkklQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQefqiraLESQK 404
Cdd:pfam13868 242 EEQIELKERRL------------AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ------IEERE 303
|
170 180
....*....|....*....|....*....
gi 2462506429 405 RQQEMVLRRKTQEVSALRRLAKPMSERVA 433
Cdd:pfam13868 304 EQRAAEREEELEEGERLREEEAERRERIE 332
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
225-426 |
4.87e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLID---------ELENSQRRLQTLKHQ-------------YEEKLILLQNKIRDTQL 282
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNleelekkaeEYEKLKEKLIKLKGEikslkkelekleeLKKKLAELEKKLDELEE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 283 ERDRVLQNLstmecytEEKANKIKADYEKRLREMN---RDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 359
Cdd:PRK03918 571 ELAELLKEL-------EELGFESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 360 ALMKQMrEEQQRRRLVETKRN--REIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAK 426
Cdd:PRK03918 644 ELRKEL-EELEKKYSEEEYEElrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
316-426 |
7.14e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 44.10 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 316 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLKKE-QRRQE 394
Cdd:pfam03938 7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKE-------QELQKKEQElQQLQQ 79
|
90 100 110
....*....|....*....|....*....|..
gi 2462506429 395 FQIRALesQKRQQEMVLRRKTQEVSALRRLAK 426
Cdd:pfam03938 80 KAQQEL--QKKQQELLQPIQDKINKAIKEVAK 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-404 |
7.43e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 230 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEE-KANKIKAD 308
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 309 YEKRLREMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreeqqrrrlveTKRNREIAQLKK 388
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----------SSLEKELEKAKK 624
|
170
....*....|....*.
gi 2462506429 389 EQRRQEFQIRALESQK 404
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKK 640
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
318-683 |
7.81e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 318 RDLQKLQAAQKEHARLLKNQSRYErELKKLQAEVAEMKKAKVALMKQMREEQQRRrlvetkrnreiaqlKKEQRRQEFQI 397
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFN-TLESAELRLSHLHFGYKSDETLIASRQEER--------------QETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 398 RALESQKRQqemVLRRKTQEVSALR-RLAKPMSERVAGRAGLKPpMLDSGAEvsasTTSSEAESgARSVSSIVRQWNRKI 476
Cdd:pfam12128 293 RTLDDQWKE---KRDELNGELSAADaAVAKDRSELEALEDQHGA-FLDADIE----TAAADQEQ-LPSWQSELENLEERL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 477 NHFLGDHpaptvNGTRPARKKFQKKGASQSFSKAARLKwQSLERriidivmQRMTIVNLEADMERLIKKreelflLQEAL 556
Cdd:pfam12128 364 KALTGKH-----QDVTAKYNRRRSKIKEQNNRDIAGIK-DKLAK-------IREARDRQLAVAEDDLQA------LESEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 557 RRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNF 636
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQA 504
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462506429 637 LkasidkglqVAQKEAQIRLLE--GRLRQTDMAGSSQNHLLLDALREKA 683
Cdd:pfam12128 505 S---------EALRQASRRLEErqSALDELELQLFPQAGTLLHFLRKEA 544
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1176-1212 |
9.54e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.79 E-value: 9.54e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2462506429 1176 FTPIGEIKGHDSPINAIC--TNAKHIFTASSDCRVKLWN 1212
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
230-435 |
9.63e-05 |
|
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: 46.64 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 230 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNK---IRDTQLErdrvLQNLSTMECYTEEKANKIK 306
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeIHDLEIQ----LTAIKTSEEHYLKEVEDLK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 307 ADYEK-RLR--EMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvETKRNREI 383
Cdd:pfam05483 478 TELEKeKLKniELTAHCDKLLLENKE---LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----EMNLRDEL 550
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506429 384 AQLKKE--QRRQEFQIRALESQK--RQQEMVLRRKTQEVSALRRLAKPMSERVAGR 435
Cdd:pfam05483 551 ESVREEfiQKGDEVKCKLDKSEEnaRSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
225-417 |
9.86e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstMECYTEEKANK 304
Cdd:pfam13868 41 EERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV--ERIQEEDQAEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 305 IKADYEKR-----LREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRl 374
Cdd:pfam13868 119 EEKLEKQRqlreeIDEFNEEQAEWKELEKeeereEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ- 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462506429 375 vETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQE 417
Cdd:pfam13868 198 -DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQ 239
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
898-933 |
1.02e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.79 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2462506429 898 QCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 933
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-477 |
1.16e-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: 46.65 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 243 EIKQ---KLIDELENSQRRLQTLKHQYE----------EKLILLQNK----IRDTQLERDRVLQNLSTMECyTEEKANKI 305
Cdd:pfam15921 650 DIKQerdQLLNEVKTSRNELNSLSEDYEvlkrnfrnksEEMETTTNKlkmqLKSAQSELEQTRNTLKSMEG-SDGHAMKV 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 306 KADYEKRLREMNRDLQKLQA-----------AQKEHARLLKNQSRYERELkklqAEVAEMKKAKVALMKQMReeQQRRRL 374
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSkiqfleeamtnANKEKHFLKEEKNKLSQEL----STVATEKNKMAGELEVLR--SQERRL 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 375 VETKRNREIAQLKKEQRRQEFQiralESQKRQQEMVLRRKTQEVSALRRLAKPmseRVAGRAGLKPPMLdsgaEVSASTT 454
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQ----DIIQRQEQESVRLKLQHTLDVKELQGP---GYTSNSSMKPRLL----QPASFTR 871
|
250 260
....*....|....*....|...
gi 2462506429 455 SSEAESGARSVSSIVRQWNRKIN 477
Cdd:pfam15921 872 THSNVPSSQSTASFLSHHSRKTN 894
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
270-422 |
1.25e-04 |
|
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: 46.27 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 270 LILLQNKIRDTQLERDRVLQNLstmecytEEKANKIKADYE---KRLREMNRDLQKLQaaQKEHARLLKNQSRYERELKK 346
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDresDRNQELQKRIRLLE--KREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 347 LQAEVAEMKKAKvalmKQMREEQQRRRLVETKRNrEIAQLKKEQRRQEFQIRALESQK---RQQEMVLRRKTQEVSALR 422
Cdd:pfam05557 82 KKYLEALNKKLN----EKESQLADAREVISCLKN-ELSELRRQIQRAELELQSTNSELeelQERLDLLKAKASEAEQLR 155
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
250-397 |
1.31e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 250 DELENSQRRLQTLKHQYEEKLILLQNKIRDTqlerDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK-LQAAQK 328
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEA----EKLKEEL-------EEKKEKLQEEEDKLLEEAEKEAQQaIKEAKK 584
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 329 EHARLLknqsryeRELKKLQAEVAEMKKAKVAlmkqmreEQQRRRLVETKRNREIAQLKKEQRRQEFQI 397
Cdd:PRK00409 585 EADEII-------KELRQLQKGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1141-1172 |
1.33e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 40.37 E-value: 1.33e-04
10 20 30
....*....|....*....|....*....|..
gi 2462506429 1141 NAHKDWVCALAFIPGRPMLLSACRAGVIKVWN 1172
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
253-417 |
1.44e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 253 ENSQRRLQTLkHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyTE-EKANKIKADYEKRLREMNRDLQKLQAAQKEHA 331
Cdd:COG1579 3 PEDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALE--ARlEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 332 RLLkNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-----EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQ 406
Cdd:COG1579 80 EQL-GNVRNNKEYEALQKEIESLKRRISDLEDEILElmeriEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 2462506429 407 QEMVLRRKTQE 417
Cdd:COG1579 159 EELEAEREELA 169
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
896-933 |
2.09e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.99 E-value: 2.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2462506429 896 PLQCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 933
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-424 |
2.50e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 250 DELENSQRRLQTLKhqyeeklilLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYEKRLREMNRDLQKLQAAQKE 329
Cdd:COG3206 189 KELEEAEAALEEFR---------QKNGLVDLSEEAKLLLQQLSELE----SQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 330 HARLLKNQ--SRYERELKKLQAEVAEMK-------------KAKVA-LMKQMREEQQrRRLVETKRNREIAQLKK---EQ 390
Cdd:COG3206 256 LPELLQSPviQQLRAQLAELEAELAELSarytpnhpdvialRAQIAaLRAQLQQEAQ-RILASLEAELEALQAREaslQA 334
|
170 180 190
....*....|....*....|....*....|....
gi 2462506429 391 RRQEFQIRALESQKRQQEmvLRRKTQEVSALRRL 424
Cdd:COG3206 335 QLAQLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
314-418 |
2.51e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 314 REMNRDL-QKLQAAQKEHARLLKNQSRYER-ELKKLQAEVAEMKKakvalmkQMREE----QQRR----RLVETKRNREI 383
Cdd:pfam15709 328 REQEKASrDRLRAERAEMRRLEVERKRREQeEQRRLQQEQLERAE-------KMREEleleQQRRfeeiRLRKQRLEEER 400
|
90 100 110
....*....|....*....|....*....|....*
gi 2462506429 384 AQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEV 418
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL 435
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
244-387 |
2.65e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 244 IKQKLIDELENSQRRLQTLKhQYEEKL--ILLQNKIRDTQLERD-RVLQNLstmecytEEKANKIKADYEKRLREmnrdl 320
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLM-KELELLnsIKPKLRDRKDALEEElRQLKQL-------EDELEDCDPTELDRAKE----- 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 321 qKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLK 387
Cdd:smart00787 212 -KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLK 277
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-659 |
3.51e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1 MNEGKRVIGEDGAeGYSDLFREnamlqKENGALRLRVKAMQEA-----IDAINNRVTQLMSQEANLL-----LAKAGDGN 70
Cdd:pfam02463 150 MKPERRLEIEEEA-AGSRLKRK-----KKEALKKLIEETENLAeliidLEELKLQELKLKEQAKKALeyyqlKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 71 EAIGALIQNYIRE--IEELRTKLLESEAMNESLRRSLSRA---SARSPYSLGASPAAPAFGGSPASSMEDASEVIRRAKQ 145
Cdd:pfam02463 224 EYLLYLDYLKLNEerIDLLQELLRDEQEEIESSKQEIEKEeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 146 DLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSdpe 225
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 226 EKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKIRDTQLERDRVLQNLSTMECYTEEKANKI 305
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-EILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 306 KADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMR------EEQQRRRLVETKR 379
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriisAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 380 NREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAE 459
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 460 SGARSVSSIVRQWNRKINH-FLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKWQSLErRIIDIVMQRMTIVNLEAD 538
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE-LQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 539 ME----RLIKKREELFLLQEALRRK---RERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEE 611
Cdd:pfam02463 699 LEikkkEQREKEELKKLKLEAEELLadrVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2462506429 612 LDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEG 659
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
299-423 |
3.98e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 299 EEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK---AKVALMKQMREEQQRRRLV 375
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEqlqAAQAELAQAQEELESLQEE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462506429 376 ETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRR 423
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
300-422 |
3.98e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.44 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 300 EKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKakvalmKQMREEQQRRRLVETKR 379
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE---ELEEERRQAEEEAERLEQ------KRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462506429 380 NREiaqlkKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALR 422
Cdd:pfam20492 73 MEA-----EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-435 |
4.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLAdltceieikQKLIDELENSQRRLQTLKHQYEeklILLQnkIRDTQLERDRVLQNLSTmecyteekank 304
Cdd:COG4913 219 EEPDTFEAADAL---------VEHFDDLERAHEALEDAREQIE---LLEP--IRELAERYAAARERLAE----------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 305 ikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRR--RLvetkrNRE 382
Cdd:COG4913 274 --LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleQL-----ERE 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462506429 383 IAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGR 435
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1178-1216 |
4.98e-04 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 43.48 E-value: 4.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2462506429 1178 PIGEIKGHDSPINAICTNA--KHIFTASSDCRVKLWNYVPG 1216
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETG 41
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
316-426 |
5.46e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.13 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 316 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvetKRNREIAQLKKE--QRRQ 393
Cdd:COG2825 31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQ------KKERELQKKQQElqRKQQ 104
|
90 100 110
....*....|....*....|....*....|....*
gi 2462506429 394 EFQiRALesQKRQQEMV--LRRKTQEvsALRRLAK 426
Cdd:COG2825 105 EAQ-QDL--QKRQQELLqpILEKIQK--AIKEVAK 134
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
245-428 |
5.56e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 245 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNlstmecyTEEKANKIKADYEK---------RLR- 314
Cdd:pfam15709 321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQE-------QLERAEKMREELELeqqrrfeeiRLRk 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 315 -------------EMNRDLQkLQAAQkEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR 381
Cdd:pfam15709 394 qrleeerqrqeeeERKQRLQ-LQAAQ-ERARQ--QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLM 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462506429 382 EIAqlkkEQRRQEFQIRALESQ-KRQQEMVLRRKTQEVSALRRLAKPM 428
Cdd:pfam15709 470 EMA----EEERLEYQRQKQEAEeKARLEAEERRQKEEEAARLALEEAM 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
307-562 |
5.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 307 ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSR------YERELKKLQAEVAEMKKAKVALMK-QMREEQQRRRLVETKr 379
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDDLAAlEEQLEELEAELEELE- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 380 nREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVS-ALRRLAKPMSERVAGRAglkppmldSGAEVSASTTSSEA 458
Cdd:COG4913 706 -EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAALGDA--------VERELRENLEERID 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 459 ESGARsVSSIVRQWNRKINHFLGDHPAPTVNGTRparkkfqkkgasqsfSKAARLKWQSLERRIIDIVmqrmtIVNLEAD 538
Cdd:COG4913 777 ALRAR-LNRAEEELERAMRAFNREWPAETADLDA---------------DLESLPEYLALLDRLEEDG-----LPEYEER 835
|
250 260
....*....|....*....|....*.
gi 2462506429 539 MERLIKKREELFL--LQEALRRKRER 562
Cdd:COG4913 836 FKELLNENSIEFVadLLSKLRRAIRE 861
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
243-408 |
7.97e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 43.67 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 243 EIKQKLIDELENSQRRLQTL--KHQY-EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKI--KADYEKRLRemn 317
Cdd:pfam15066 318 EVLQKLKHTNRKQQMQIQDLqcSNLYlEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVIleKNDINKTLQ--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 318 rDLQKLQAAQKEHARllknQSRYERELkkLQAEVAEMKKAKVALMKQ-MREEQQRRRLVE---------TKRNREIAQLK 387
Cdd:pfam15066 395 -NLQEILANTQKHLQ----ESRKEKET--LQLELKKIKVNYVHLQERyITEMQQKNKSVSqclemdktlSKKEEEVERLQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462506429 388 --------------------KEQRRQEFQIRALESQKRQQE 408
Cdd:pfam15066 468 qlkgelekattsaldllkreKETREQEFLSLQEEFQKHEKE 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
299-421 |
9.29e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 299 EEKANKIKADYEKRLREMNRDlqKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKaKValmkQMREEQQRRRLVE-T 377
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKE--ALLEAKEE---IHKLRNEFEKELRERRNELQKLEK-RL----LQKEENLDRKLELlE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462506429 378 KRNREIAQLKK--EQRRQEFQIRALESQKRQQEMvlRRKTQEVSAL 421
Cdd:PRK12704 107 KREEELEKKEKelEQKQQELEKKEEELEELIEEQ--LQELERISGL 150
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
142-709 |
1.02e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 142 RAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEE--EEEERDESGCEEEEGREDEDedsgSEESLVD 219
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKklQEEELKLLAKEEEELKSELL----KLERRKV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 220 SDSDPEEKEVNfqadladltcEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTE 299
Cdd:pfam02463 311 DDEEKLKESEK----------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 300 EKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKR 379
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 380 NREIAQLKKEqRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSAST--TSSE 457
Cdd:pfam02463 461 LKDELELKKS-EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlgVAVE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 458 AESGARSVSSIVRQWNRKINHFLGDHpapTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQrmtiVNLEA 537
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQK---LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ----LDKAT 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 538 DMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDT 617
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 618 SVVISSCSLAEARL---LLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSsqnhLLLDALREKAEAHPELQALIY 694
Cdd:pfam02463 693 EILRRQLEIKKKEQrekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE----EEEEEEKSRLKKEEKEEEKSE 768
|
570
....*....|....*
gi 2462506429 695 NVQQENGYASTDEEI 709
Cdd:pfam02463 769 LSLKEKELAEEREKT 783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
134-395 |
1.11e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 134 EDASEVIRRAKQDLERLKKKEV---RQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDED 210
Cdd:pfam02463 778 EEREKTEKLKVEEEKEEKLKAQeeeLRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 211 SGSEESLVDSDSDpEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIrdtQLERDRVLQN 290
Cdd:pfam02463 858 RLEEEITKEELLQ-ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI---KEEAEILLKY 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 291 LStmECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKvalMKQMREEQQ 370
Cdd:pfam02463 934 EE--EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER---LEEEKKKLI 1008
|
250 260
....*....|....*....|....*
gi 2462506429 371 RRRLVETKRNREIAQLKKEQRRQEF 395
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSINKGW 1033
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1141-1172 |
1.33e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.33e-03
10 20 30
....*....|....*....|....*....|..
gi 2462506429 1141 NAHKDWVCALAFIPGRPMLLSACRAGVIKVWN 1172
Cdd:pfam00400 8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
242-413 |
1.40e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 40.27 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 242 IEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteekankikadyekRLREMNRDLQ 321
Cdd:COG2882 11 LDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAA----------------QLRNYQQFIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 322 KLQAAQKEHARLLKN-QSRYERELKKLQaevaemkkakvalmkqmrEEQQRRRLVETKRNREIAQLKKEQRRQEfqiral 400
Cdd:COG2882 75 RLDEAIEQQQQQVAQaEQQVEQARQAWL------------------EARQERKALEKLKERRREEERQEENRRE------ 130
|
170
....*....|...
gi 2462506429 401 esQKRQQEMVLRR 413
Cdd:COG2882 131 --QKELDELASRR 141
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
232-401 |
1.50e-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: 42.57 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 232 QADLADLTCEIEIKQKLIDELENSQ---RRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIkAD 308
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLeelRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL-AD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 309 YEKRLREMNRDLQK-----LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQ-----MREEQQRRRLVETK 378
Cdd:pfam07888 291 ASLALREGRARWAQeretlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELK 370
|
170 180
....*....|....*....|....*...
gi 2462506429 379 RNREIAQLKKEQRRQEFQ-----IRALE 401
Cdd:pfam07888 371 ASLRVAQKEKEQLQAEKQelleyIRQLE 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-426 |
1.62e-03 |
|
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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 223 DPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEeklillqnKIRDTQLERDRVLQnlstmecyTEEKA 302
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVAS--------AEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 303 nkikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAkvalMKQMREEQQR-RRLVETKRNR 381
Cdd:COG4913 671 ----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDElQDRLEAAEDL 742
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462506429 382 EIAQLKK--EQRRQEFQIRALESQKRQQemVLRRKTQEVSALRRLAK 426
Cdd:COG4913 743 ARLELRAllEERFAAALGDAVERELREN--LEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
225-582 |
1.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 225 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLqNKIRDTQLERDRVLQNLSTME-------CY 297
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELErlkkrltGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 298 TEEKANKIKADYEKRLREMNRDLQKLQAA----QKEHARLLKN--------------------------QSRYERELKKL 347
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAieelkkakgkcpvcgrelteehrkelLEEYTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 348 QAEVAEMKKAKVALMKQMRE-EQQRRRLVETKRNREIA-QLKK-EQRRQEFQIRALESQKRQQEMVLRRKTQ---EVSAL 421
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRElEKVLKKESELIKLKELAeQLKElEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgEIKSL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 422 RRLAKPMSERVAGRAGLKPPmLDSGAEVSASTTSSEAESGARS---VSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKF 498
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKK-LDELEEELAELLKELEELGFESveeLEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 499 QKKGASQSFSKAARLKwQSLERriidiVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQA--ESPEE-EKGLQ 575
Cdd:PRK03918 624 LEEELDKAFEELAETE-KRLEE-----LRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEEleKRREEiKKTLE 697
|
....*..
gi 2462506429 576 ELAEEIE 582
Cdd:PRK03918 698 KLKEELE 704
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
241-412 |
1.94e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 241 EIEIKQKLIDElensQRRLQTLKHQYEEKL----------ILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYE 310
Cdd:pfam15709 349 EVERKRREQEE----QRRLQQEQLERAEKMreeleleqqrRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 311 KRlrEMNRDLQKLQaaQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnreiAQLKKEQ 390
Cdd:pfam15709 425 QE--EFRRKLQELQ--RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK----ARLEAEE 496
|
170 180
....*....|....*....|....*
gi 2462506429 391 RRQ--EFQIR-ALESQKRQQEMVLR 412
Cdd:pfam15709 497 RRQkeEEAARlALEEAMKQAQEQAR 521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-408 |
2.04e-03 |
|
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: 42.31 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 235 LADLTCEIEIKQKLIDELENS----QRRLQTLKHQYEEKLILL--------QNKIRDTQLERDRVLQNLSTMEcyteEKA 302
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQlnqlKSEISDLNNQKEQDWNKElkselknqEKKLEEIQNQISQNNKIISQLN----EQI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 303 NKIK-------ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLV 375
Cdd:TIGR04523 345 SQLKkeltnseSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462506429 376 E----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQE 408
Cdd:TIGR04523 425 EkeierlketiIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
310-433 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 310 EKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKE 389
Cdd:COG1579 23 EHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEA-RIKKYEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462506429 390 QRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 433
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
307-435 |
2.29e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 307 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEVAEM-KKAKVALMKQmrEEQQRRRLVETKRNRE-- 382
Cdd:pfam04012 21 EDPEKMLEQAIRDMQSeLVKARQALAQTIARQKQLERRLEQQTEQAKKLeEKAQAALTKG--NEELAREALAEKKSLEkq 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506429 383 --------------IAQLKKEQRRQEFQIRALESQKR-----------QQEMVLRRKTQEVSALRRLAKPMSERVAGR 435
Cdd:pfam04012 99 aealetqlaqqrsaVEQLRKQLAALETKIQQLKAKKNllkarlkaakaQEAVQTSLGSLSTSSATDSFERIEEKIEER 176
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
366-715 |
2.58e-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: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 366 REEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKppMLDS 445
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER--QLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 446 GAEVSASTTSSEAESGARSVS--SIVRQWNRKINHFLGDHPAptvngtrparkKFQKKGASQSfSKAARLkwqsleRRII 523
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEieQLLEELNKKIKDLGEEEQL-----------RVKEKIGELE-AEIASL------ERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 524 DIVMQRM-----TIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDC 598
Cdd:TIGR02169 311 AEKERELedaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 599 QATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQ----KEAQIRLLEGRLRQT--DMAGSSQN 672
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEekedKALEIKKQEWKLEQLaaDLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462506429 673 HL------------LLDALREKAEAHPELQALiynVQQENGYASTDEEISEFSEG 715
Cdd:TIGR02169 471 LYdlkeeydrvekeLSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQG 522
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
313-441 |
2.73e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 313 LREMNRDLQKLQAaQKEHARLLKNQSRYEReLKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnREIAQLKKEQRR 392
Cdd:COG0542 413 LDELERRLEQLEI-EKEALKKEQDEASFER-LAELRDELAELEEELEALKARWEAEKELIEEIQELK-EELEQRYGKIPE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 393 QEFQIRALESQKRQQEMVLR-------------RKT---------QEVSALRRLAKPMSERVAG---------------R 435
Cdd:COG0542 490 LEKELAELEEELAELAPLLReevteediaevvsRWTgipvgklleGEREKLLNLEEELHERVIGqdeaveavadairrsR 569
|
....*.
gi 2462506429 436 AGLKPP 441
Cdd:COG0542 570 AGLKDP 575
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
241-571 |
2.88e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 241 EIEIKQKLIDELENSQRRLQTLKHQYEEKLIL----LQNKIRdtqLERDRV-LQNLSTMECYTEEKANKIKADY------ 309
Cdd:pfam07111 54 ELEGSQALSQQAELISRQLQELRRLEEEVRLLretsLQQKMR---LEAQAMeLDALAVAEKAGQAEAEGLRAALagaemv 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 310 EKRLREMN-RDLQKLQAAQKEHARLLKNQsrYERELKKLQAEVAEMKKAKVALmkQMREEQQRRRLVETKRNREI--AQL 386
Cdd:pfam07111 131 RKNLEEGSqRELEEIQRLHQEQLSSLTQA--HEEALSSLTSKAEGLEKSLNSL--ETKRAGEAKQLAEAQKEAELlrKQL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 387 KKEQRRQEFQIRALES-QKRQQEMVLRRKTQEVSALRR--LAKPMSERVAGRAGLKPPMLDSGAEVSAST--TSSEAESG 461
Cdd:pfam07111 207 SKTQEELEAQVTLVESlRKYVGEQVPPEVHSQTWELERqeLLDTMQHLQEDRADLQATVELLQVRVQSLThmLALQEEEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 462 ARSVS--------------SIVRQWNRKINHFLGDHPAP------TVNGTRPARKKFQKKGASQSFSKAarLKWQSLERR 521
Cdd:pfam07111 287 TRKIQpsdslepefpkkcrSLLNRWREKVFALMVQLKAQdlehrdSVKQLRGQVAELQEQVTSQSQEQA--ILQRALQDK 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2462506429 522 IIDIVMQRMTIVNLEADMERLikkreelfllQEAlrRKRERLQAESPEEE 571
Cdd:pfam07111 365 AAEVEVERMSAKGLQMELSRA----------QEA--RRRQQQQTASAEEQ 402
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
275-431 |
3.05e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 275 NKIRDTQLERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRyERELKKLQAEVAEM 354
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEE--ERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 355 KKakvalmKQMREEQQRRRLVETKRNREiaqlKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 431
Cdd:pfam13868 98 QE------REQMDEIVERIQEEDQAEAE----EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1-418 |
3.50e-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: 41.63 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 1 MNEGKRVIGEDgaegySDLFRENAMLQKENGALRlrvKAMQEAIDAINNRVTQLMSQEANLLLAKAGDgneaigaliQNY 80
Cdd:pfam05483 407 LEELKKILAED-----EKLLDEKKQFEKIAEELK---GKEQELIFLLQAREKEIHDLEIQLTAIKTSE---------EHY 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 81 IREIEELRTKLLESEAMNESLRRSLSRASarspyslgaspaapafggspassMEDASEVIRRAKQDLERLKKKEVRQRRK 160
Cdd:pfam05483 470 LKEVEDLKTELEKEKLKNIELTAHCDKLL-----------------------LENKELTQEASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 161 SPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLvdsdsDPEEKEVNFQADLADLTC 240
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVL-----KKEKQMKILENKCNNLKK 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 241 EIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMeCYTEEKANKIKADYEKRLREmnrDL 320
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-IDNYQKEIEDKKISEEKLLE---EV 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 321 QKLQAAQKEHARLLKNQSryerelKKLQAEVAEMkkakVALMKqmREEQQRRRLVEtKRNREIAQLKKEQRRQEFQIRAL 400
Cdd:pfam05483 678 EKAKAIADEAVKLQKEID------KRCQHKIAEM----VALME--KHKHQYDKIIE-ERDSELGLYKNKEQEQSSAKAAL 744
|
410 420
....*....|....*....|
gi 2462506429 401 ESQ--KRQQEMVLRRKTQEV 418
Cdd:pfam05483 745 EIElsNIKAELLSLKKQLEI 764
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
224-416 |
3.52e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 224 PEEKEVNFQADLADLTCEIEIKQKL-IDELENSQRRLQTLKhQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA 302
Cdd:PRK11281 36 PTEADVQAQLDALNKQKLLEAEDKLvQQDLEQTLALLDKID-RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 303 NKIKADY-----EKRLREMNRDLQKLQAAQKE-HARLLKNQSRYERelkkLQAEVAEMkkakvalmkQMREEQQRRRLVE 376
Cdd:PRK11281 115 RETLSTLslrqlESRLAQTLDQLQNAQNDLAEyNSQLVSLQTQPER----AQAALYAN---------SQRLQQIRNLLKG 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462506429 377 TKRNREiaQLKKEQRRQ-EFQIRALESQKRQQEMVLRRKTQ 416
Cdd:PRK11281 182 GKVGGK--ALRPSQRVLlQAEQALLNAQNDLQRKSLEGNTQ 220
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
518-620 |
3.89e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 518 LERRIIDIVMQRMTIVNL--EADMERLIKKREELFLLQEALRRKRERLQAEspeeekglQELAEEIEVLAANIDYINDGI 595
Cdd:COG0542 416 LERRLEQLEIEKEALKKEqdEASFERLAELRDELAELEEELEALKARWEAE--------KELIEEIQELKEELEQRYGKI 487
|
90 100
....*....|....*....|....*
gi 2462506429 596 TDCQATIVQLEETKEELDSTDTSVV 620
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREEV 512
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
243-431 |
4.26e-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: 41.49 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 243 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKIRDTQLERDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK 322
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR-ELETHIEEYDREFNEI-------ENASSSLGSDLAAREDALNQSLKE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 323 LQAAQKEHARLLKNqsryERELKKLQAEVAEMKKAKVALMKQmrEEQQRRRLVETkRNREIAQLKKE---QRRQEFQIRA 399
Cdd:TIGR00618 748 LMHQARTVLKARTE----AHFNNNEEVTAALQTGAELSHLAA--EIQFFNRLREE-DTHLLKTLEAEigqEIPSDEDILN 820
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462506429 400 LESQKRQQEM-----VLRRKTQEVSALRRLAKPMSER 431
Cdd:TIGR00618 821 LQCETLVQEEeqflsRLEEKSATLGEITHQLLKYEEC 857
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
316-409 |
4.68e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 316 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQqrrrlvETKRNREIAQLKKEQRRQEF 395
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA------REKKEKELQKKVQEFQRKQQ 79
|
90
....*....|....
gi 2462506429 396 QIRALESQKRQQEM 409
Cdd:smart00935 80 KLQQDLQKRQQEEL 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
517-699 |
4.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 517 SLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEAL--------RRKRERLQAESPEEEKGLQELAEEIEVLAANI 588
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 589 DYINDGITDCQATI-----VQLEETKEELDSTDTSvvisscsLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 663
Cdd:COG4913 319 DALREELDELEAQIrgnggDRLEQLEREIERLERE-------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462506429 664 TDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQE 699
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1042-1083 |
5.08e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 5.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2462506429 1042 FQPVGKLTGHIGPVMCLTVTQTasqHDLVVTGSKDHYVKMFE 1083
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPD---GKLLASGSDDGTVKVWD 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
300-471 |
5.68e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 300 EKANKIKADYEKRLREMNRDLQKLQAAQK--EHARLLKNQSRYERELK-------KLQAEVAEMKKAKVALMKQMREEQQ 370
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKakqaaeaKAKAEAEAERKAKEEAAKQAEEEAK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 371 RRRLVETKRNREIAQLKKEQ------------RRQEFQIRALESQKRQQEMVLRRKTQEVSALRRL---AKPMSERVAGR 435
Cdd:TIGR02794 158 AKAAAEAKKKAEEAKKKAEAeakakaeaeakaKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAeaeRKADEAELGDI 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462506429 436 AGLkppMLDSGAEVSASTTSSEAESGARSVSSIVRQ 471
Cdd:TIGR02794 238 FGL---ASGSNAEKQGGARGAAAGSEVDKYAAIIQQ 270
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
243-372 |
6.10e-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: 40.96 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 243 EIKQKLIDELENSQRRLQTLKH-QYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA---NKIKADYEKRLRE-MN 317
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghlTNLRAERRKQLEEiLE 708
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506429 318 RDLQKLQAAQKEH----ARLLKNQSRYerelKKLQAEVAEMKKAKVALMKQMREEQQRR 372
Cdd:pfam10174 709 MKQEALLAAISEKdaniALLELSSSKK----KKTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
311-441 |
6.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 311 KRLREMNRDLQKLQAAQKEHARL--LKNQSRY---ERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVEtkrnREIAQ 385
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELeyLRAALRLwfaQRRLELLEAELEELRAELARLEAELERLEARLDALR----EELDE 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506429 386 LKKEQRRQEFQ-IRALESQKRQQEMVLRRKTQEVSALRRLAKpmservagRAGLKPP 441
Cdd:COG4913 328 LEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLA--------ALGLPLP 376
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
299-546 |
6.36e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.79 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 299 EEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETK 378
Cdd:COG3064 54 EEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 379 RN-----REIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSAST 453
Cdd:COG3064 134 KRkaeeeRKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 454 TSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIV 533
Cdd:COG3064 214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
250
....*....|...
gi 2462506429 534 NLEADMERLIKKR 546
Cdd:COG3064 294 GLVLDDSAALAAE 306
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
134-446 |
6.55e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 134 EDASEVIRRAKQDLERLKKKE-----VRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDED 208
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEepsgqVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 209 EDSGSEESLVDSDSDPEEKEVNFQADLADLT---------CEIEIKQKLIDELENSQRRLQTLKHQYEEKLillqNKIRD 279
Cdd:pfam02029 86 QKEFDPTIADEKESVAERKENNEEEENSSWEkeekrdsrlGRYKEEETEIREKEYQENKWSTEVRQAEEEG----EEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 280 TQLERDRVLQNLSTMECYTEEKANKIKADYEKRL----REMNRDLQKLQAAQ--------KEHARLLKNQSRYERELKKL 347
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKvfldQKRGHPEVKSQNGEeevtklkvTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 348 QAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR--EIAQLKK--EQRRqefQIRALESQKRQQEMvLRRKTQEVSALRR 423
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAelELEELKKkrEERR---KLLEEEEQRRKQEE-AERKLREEEEKRR 317
|
330 340
....*....|....*....|...
gi 2462506429 424 LAKPMSERVAGRAGLKPPMLDSG 446
Cdd:pfam02029 318 MKEEIERRRAEAAEKRQKLPEDS 340
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
307-593 |
7.33e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 307 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEvaeMKKAKVALmKQMREEQqrRRLVETKRNreiaq 385
Cdd:pfam12128 596 AASEEELRERLDKAEEaLQSAREKQAAAEEQLVQANGELEKASRE---ETFARTAL-KNARLDL--RRLFDEKQS----- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 386 lkkEQRRQEfqiRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRA-GLKPPMLDSGAEVSASTTSSEA------ 458
Cdd:pfam12128 665 ---EKDKKN---KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKrEARTEKQAYWQVVEGALDAQLAllkaai 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 459 ---ESGARSVSSIVRQWNRKinhflgDHPAPTVNGTRPARKKFQKKGASQSFSKAAR-----LKWQSLERRIIDIVMQRM 530
Cdd:pfam12128 739 aarRSGAKAELKALETWYKR------DLASLGVDPDVIAKLKREIRTLERKIERIAVrrqevLRYFDWYQETWLQRRPRL 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506429 531 --TIVNLEADMERLikkREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYIND 593
Cdd:pfam12128 813 atQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
245-514 |
8.82e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.41 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 245 KQKLIDELENSQRRLQT----LKHQYEEKLILlqNKIRDTQLERDRVLQNLSTMECYTEEKANKIKA------------- 307
Cdd:PTZ00108 997 KEYLLGKLERELARLSNkvrfIKHVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAeeeegaeeddead 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 308 ------------DYEKRLR--------EMNRDLQK-LQAAQKEHARLLKN--QSRYERELKKLQAEVAEMKKAKVALMKQ 364
Cdd:PTZ00108 1075 deddeeelgaavSYDYLLSmpiwsltkEKVEKLNAeLEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAK 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 365 MREEQQRRRLVETKRNREIAQLKKEQRRQefqirALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLD 444
Cdd:PTZ00108 1155 EQRLKSKTKGKASKLRKPKLKKKEKKKKK-----SSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDE 1229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506429 445 SGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFSKAARLK 514
Cdd:PTZ00108 1230 EQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGkpknAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
321-407 |
9.22e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 38.76 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506429 321 QKLQAAQKEHARL-LKN---QSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRR--------------------LVE 376
Cdd:pfam06391 68 KKIEQYEKENKDLiLKNkmkLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKekakqelidelmtsnkdaeeIIA 147
|
90 100 110
....*....|....*....|....*....|.
gi 2462506429 377 TKRNReIAQLKKEQRRQEFQIRALESQKRQQ 407
Cdd:pfam06391 148 QHKKT-AKKRKSERRRKLEELNRVLEQKPTQ 177
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1042-1083 |
9.42e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 35.37 E-value: 9.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2462506429 1042 FQPVGKLTGHIGPVMCLTVTQTasqHDLVVTGSKDHYVKMFE 1083
Cdd:smart00320 2 GELLKTLKGHTGPVTSVAFSPD---GKYLASGSDDGTIKLWD 40
|
|
| |
