|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
17-120 |
8.23e-48 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 164.72 E-value: 8.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 17 VIFQNVAKSYLPNAHLECHYTLTPYIHPHSKDWVGIFKVGWSTARDYYTFLWSpmPEHYVEGSTVNCVLAFQGYYLPNDD 96
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 1244518170 97 GEFYQFCYVTHKGEIRGASTPFQF 120
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
125-460 |
1.96e-31 |
|
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: 129.24 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 125 PVEELLTME-----DEGNSDMLVVTTKAGLL------------------ELKIEKTLKEKEELLKLIAVLEKETAQLREQ 181
Cdd:pfam07888 2 PLDELVTLEeeshgEEGGTDMLLVVPRAELLqnrleeclqeraellqaqEAANRQREKEKERYKRDREQWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 182 VGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRK 261
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 262 AQHereqlecQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQscladkenlyraLLL 341
Cdd:pfam07888 162 AGA-------QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT------------QKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 342 TTSNKEDTLF--LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQ------ 413
Cdd:pfam07888 223 TTAHRKEAENeaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegrarw 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518170 414 -------LHAVKKDQEKTDTLEHELRREVEDL--------KLRLQMAADhyrekfKECQRLQ 460
Cdd:pfam07888 303 aqeretlQQSAEADKDRIEKLSAELQRLEERLqeermereKLEVELGRE------KDCNRVQ 358
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-468 |
3.76e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLR--KAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKlvseiQTLKNLDGNKESM---ITHFKEEISKL 325
Cdd:TIGR02168 797 ELKALREALDelRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-----EQIEELSEDIESLaaeIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 326 QSCLADKENLYRALLLTTSNKEDTLF-LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKtmadlhtARLENERVKKQ 404
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEeLSEELRELESKRSELRRELEELREKLAQLELRLEG-------LEVRIDNLQER 944
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 405 LADtLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQ-------MAADHYREKFKECQRLQKQINKLSD 468
Cdd:TIGR02168 945 LSE-EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-448 |
7.11e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIEntkLVSEIQTLKNLDGNKESMITHFKEEISKLQS 327
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 328 CLADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLhtaRLENERVKKQLAD 407
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL---EEEEEALLELLAE 467
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1244518170 408 TLAELQLHavkkdQEKTDTLEHELRREVEDLKLRLQMAADH 448
Cdd:COG1196 468 LLEEAALL-----EAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
753-779 |
2.99e-11 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 58.43 E-value: 2.99e-11
10 20
....*....|....*....|....*..
gi 1244518170 753 KKCPLCELMFPPNYDQTKFEEHVESHW 779
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-608 |
3.17e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQkgllEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKEL-------YKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISK 324
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 325 LQSCLADKENLYRALlltTSNKEDTlflKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQ 404
Cdd:PRK02224 354 LEERAEELREEAAEL---ESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 405 LADTLAELQ------------LHAVK--------KDQEKTDTLEH------ELRREVEDLKLRlQMAADHYREKFKECQR 458
Cdd:PRK02224 428 EAELEATLRtarerveeaealLEAGKcpecgqpvEGSPHVETIEEdrerveELEAELEDLEEE-VEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 459 LQKQINKLSDQA-ASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAEtgfdmstkdhvcEMTKEIAEKI 537
Cdd:PRK02224 507 AEDRIERLEERReDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE------------EEAEEAREEV 574
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 538 EKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKlELAEVEDNYKVQLAEKEKEINGLASYLE 608
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE-ALAELNDERRERLAEKRERKRELEAEFD 644
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
780-806 |
4.59e-11 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 57.95 E-value: 4.59e-11
10 20
....*....|....*....|....*..
gi 1244518170 780 KVCPMCSEQFPPDYDQQGFERHVQTHF 806
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
755-778 |
1.65e-10 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 56.27 E-value: 1.65e-10
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-488 |
1.33e-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: 62.00 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQvgrmerelsqekgrCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVsvthkaiEKET 250
Cdd:TIGR02168 244 LQEELKEAEEE--------------LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-------RLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLknteienTKLVSEIQTLKNldgNKESMithfKEEISKLQSCLA 330
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEEL-------AELEEKLEELKE---ELESL----EAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKENLYRAlllttsnkedtlfLKEQLRKAEEQVQATRQELIFLTKELSdaVNVRDKTMADLHTARLENERvkKQLADTLA 410
Cdd:TIGR02168 369 ELESRLEE-------------LEEQLETLRSKVAQLELQIASLNNEIE--RLEARLERLEDRRERLQQEI--EELLKKLE 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1244518170 411 ELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVN 488
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-623 |
3.34e-09 |
|
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: 60.51 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 175 TAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSvthkaieketdlds 254
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCS-------------- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 255 lkdklrkaqhereqLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESmithfkeEISKLQSCLADKEN 334
Cdd:pfam05483 361 --------------LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV-------ELEELKKILAEDEK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 335 LyralllttsnkedtLFLKEQLRKAEEQVQATRQELIFLtkelsdaVNVRDKTMADLH----TARLENERVKKQLADTLA 410
Cdd:pfam05483 420 L--------------LDEKKQFEKIAEELKGKEQELIFL-------LQAREKEIHDLEiqltAIKTSEEHYLKEVEDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 411 ELQLHAVKKDQEKTDT----LEH-ELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAS-TNSVFTKKMGSQ 484
Cdd:pfam05483 479 ELEKEKLKNIELTAHCdkllLENkELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNlRDELESVREEFI 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 485 QKVNDASINTDPAASTSASAvdvkpAASCAETGFDMSTKDHVCEMTKeiaEKIEKYNKCKQLLQDE----KTKCNKYAEE 560
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSI-----EYEVLKKEKQMKILENKCNNLK---KQIENKNKNIEELHQEnkalKKKGSAENKQ 630
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1244518170 561 LAKMELKWKEQVKIAENVKLELAEVEDNYkvqlaEKEKEINGLASylENLSREKELTKSLEDQ 623
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIIDNY-----QKEIEDKKISE--EKLLEEVEKAKAIADE 686
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-629 |
1.02e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLlevsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 248 KETDLDSLKDKLRKAQhEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNL---DGNKESMITHFKEEISK 324
Cdd:PRK03918 271 LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 325 LQ---SCLADKENLY---RALL---------LTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMA 389
Cdd:PRK03918 350 LEkrlEELEERHELYeeaKAKKeelerlkkrLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 390 DLHTAR---------LENERVKKQLADTLAELQlhAVKKDQEKTDTLEHELRREVEDLK---------LRLQMAADHYRE 451
Cdd:PRK03918 430 ELKKAKgkcpvcgreLTEEHRKELLEEYTAELK--RIEKELKEIEEKERKLRKELRELEkvlkkeselIKLKELAEQLKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 452 ---------------KFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDvkpaaSCAET 516
Cdd:PRK03918 508 leeklkkynleelekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK-----ELEEL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 517 GFdmSTKDHVCEMTKEIAEKIEKYNKCK---QLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQ- 592
Cdd:PRK03918 583 GF--ESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEe 660
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1244518170 593 -------LAEKEKEINGLASYLENL-SREKELTKSLEDQKGRKLE 629
Cdd:PRK03918 661 yeelreeYLELSRELAGLRAELEELeKRREEIKKTLEKLKEELEE 705
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
780-806 |
1.24e-08 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 51.11 E-value: 1.24e-08
10 20
....*....|....*....|....*..
gi 1244518170 780 KVCPMCSEQFPPDYDQQGFERHVQTHF 806
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-586 |
2.51e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 229 AKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLE--CQLQTEKDEKELYkVHLKNTEientKLVSEIQTLKN 306
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEGY-ELLKEKE----ALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 307 LDGNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNK--EDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVR 384
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 385 DKTMADLHTARLENERVKKQLADtlaelqlhaVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQIN 464
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEE---------ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 465 KLsdqaastnsvfTKKMGSQQKVNDASIntDPAASTSASAVDVKPAASCAE---TGFDMSTKDhvceMTKEIAEKIEKYN 541
Cdd:TIGR02169 396 KL-----------KREINELKRELDRLQ--EELQRLSEELADLNAAIAGIEakiNELEEEKED----KALEIKKQEWKLE 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1244518170 542 KCKQLLQDEKTKCNKYAEELAKMElkwKEQvkiaENVKLELAEVE 586
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVE---KEL----SKLQRELAEAE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-471 |
3.33e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQqleEDIVSVthkaiekET 250
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK---EKIGEL-------EA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQLECQLQteKDEKELYKVHLKNTEIEntklvSEIQTLKnldGNKESMITHFKEeisklqscLA 330
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLA--KLEAEIDKLLAEIEELE-----REIEEER---KRRDKLTEEYAE--------LK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKENLYRALLLTTSNKEDTLFlkeqlrkaEEQVQAtRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLA 410
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETR--------DELKDY-REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1244518170 411 EL-QLHAVKKD-QEKTDTLEHELRREVEDLKlrlqMAADHYREKFKECQRLQKQINKLSDQAA 471
Cdd:TIGR02169 435 KInELEEEKEDkALEIKKQEWKLEQLAADLS----KYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-610 |
4.97e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 288 KNTEIENtkLVSEIQTLknldgnkESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTL-FLKEQLRKAEEQVQAT 366
Cdd:TIGR02168 675 RRREIEE--LEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 367 RQELIFLTKELSDAVNVRDKTMADLHTARL---ENERVKKQLADTLAEL--QLHAVKKDQEKTDTLEHELRREVEDLKLR 441
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLkeELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 442 LQMAADHYREKFKECQRLQKQINKLSDQAASTNSVftkkmgsqqkVNDASINTDPAASTSASAVDVKPAASCAEtgfdMS 521
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAE----------IEELEELIEELESELEALLNERASLEEAL----AL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 522 TKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKE-QVKIAENVKLELAEVEDNYKV---QLAEKE 597
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKiedDEEEAR 971
|
330
....*....|...
gi 1244518170 598 KEINGLASYLENL 610
Cdd:TIGR02168 972 RRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-448 |
5.45e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSqekgRCEQLQAEQKGLL-EVSQSLRVENeefmKRYSDATAKVQQLEEDIVSVTHKAIEKE 249
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELS----SLQSELRRIENRLdELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 250 TDLDSLKDKLRKAQHEREQLECQLqtEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLdgnkesmITHFKEEISKLQSCL 329
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLSHSRIPEIQAE-------LSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 330 ADKEnlyralllttSNKEDTLFLKEQLRKAeeqvqatRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTL 409
Cdd:TIGR02169 815 REIE----------QKLNRLTLEKEYLEKE-------IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1244518170 410 AEL--QLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADH 448
Cdd:TIGR02169 878 RDLesRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
782-805 |
6.16e-08 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 49.11 E-value: 6.16e-08
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-471 |
8.07e-08 |
|
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: 55.16 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKENLYRALL--LTTSNKEDTLFLkeqLRKAEEQVQATRQELIF--LTKELSDAVNVRDKTMADLHTARLENERVKKQLA 406
Cdd:COG4942 101 AQKEELAELLraLYRLGRQPPLAL---LLSPEDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1244518170 407 DTLAELQlhavkKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAA 471
Cdd:COG4942 178 ALLAELE-----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
755-778 |
1.00e-07 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 48.34 E-value: 1.00e-07
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
782-805 |
1.54e-07 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 47.80 E-value: 1.54e-07
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-447 |
1.80e-07 |
|
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: 55.12 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 178 LREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEediVSVTHKAIEKETDLDSLKD 257
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE---ARVSDLELEKVKLVNAGSE 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 258 KLRKA---QHEREQLECQLQTEKDE----KELYKVHLKN-----TEIENT--KL-------VSEIQTLKNLDGNKESMIT 316
Cdd:pfam15921 644 RLRAVkdiKQERDQLLNEVKTSRNElnslSEDYEVLKRNfrnksEEMETTtnKLkmqlksaQSELEQTRNTLKSMEGSDG 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 317 HFKEEISKLQSCLADKENLYRALllttsnKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARL 396
Cdd:pfam15921 724 HAMKVAMGMQKQITAKRGQIDAL------QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 397 ENERVKKQLADTLAELQlHAVKKDQEKTDTLEhelRREVEDLKLRLQMAAD 447
Cdd:pfam15921 798 QERRLKEKVANMEVALD-KASLQFAECQDIIQ---RQEQESVRLKLQHTLD 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-408 |
1.80e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATA 229
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 230 KVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDG 309
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 310 NKESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTLF--LKEQLRK--------------AEEQVQATRQELIFL 373
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEeeARRRLKRlenkikelgpvnlaAIEEYEELKERYDFL 1005
|
250 260 270
....*....|....*....|....*....|....*...
gi 1244518170 374 TKELSDAVNVRDK---TMADLhtarleNERVKKQLADT 408
Cdd:TIGR02168 1006 TAQKEDLTEAKETleeAIEEI------DREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-370 |
2.87e-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: 54.29 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL 206
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 207 LEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHERE-------QLECQLQTEKDE 279
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 280 KELYKVHLKNTEIENTKLVSEIQTL-KNLDGNK----ESMITHFKEEISKLQSCLADKENLYRAlllttsnkedtlfLKE 354
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELlKKLEEAElkelQAELEELEEELEELQEELERLEEALEE-------------LRE 468
|
250
....*....|....*.
gi 1244518170 355 QLRKAEEQVQATRQEL 370
Cdd:TIGR02168 469 ELEEAEQALDAAEREL 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-448 |
1.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL 206
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 207 LEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVH 286
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 287 LKNTEIENTKLVSEIQTLK-NLDGNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQA 365
Cdd:COG1196 402 LEELEEAEEALLERLERLEeELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 366 TRQELIFLTKELSDAVNVRDKTMADLHTAR-LENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQM 444
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
....
gi 1244518170 445 AADH 448
Cdd:COG1196 562 AIEY 565
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-434 |
1.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQS 327
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 328 CLADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTmADLHTARLENERVKKQLAD 407
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA-GAVAVLIGVEAAYEAALEA 542
|
250 260
....*....|....*....|....*..
gi 1244518170 408 TLAELQLHAVKKDQEKTDTLEHELRRE 434
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-413 |
3.63e-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: 50.15 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTE 276
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 277 KDE-KELYKVHLKNTEIENTKLV----SEIQTLKNLDGNKeSMITHFKEEISKLQsclADKENLYRalllttsnkedtlf 351
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLK-YLAPARREQAEELR---ADLAELAA-------------- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518170 352 LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQ 413
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
185-475 |
4.09e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.07 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 185 MERELSQekgRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSdataKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQH 264
Cdd:pfam05622 8 EKDELAQ---RCHELDQQVSLLQEEKNSLQQENKKLQERLD----QLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 265 EREQLecQLQTEKDEKELYKVHLKNTEIenTKLVSEIQTLknldgnkesmithfKEEISKLQSClADKENLYRALLLTTS 344
Cdd:pfam05622 81 ARDDY--RIKCEELEKEVLELQHRNEEL--TSLAEEAQAL--------------KDEMDILRES-SDKVKKLEATVETYK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 345 NK-EDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRdktmadlhtARLENerVKKQLADTLAELQLHAVKKD--- 420
Cdd:pfam05622 142 KKlEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALR---------GQLET--YKRQVQELHGKLSEESKKADkle 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 421 ------QEKTDTLEHElrrevedlKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTNS 475
Cdd:pfam05622 211 feykklEEKLEALQKE--------KERLIIERDTLRETNEELRCAQLQQAELSQADALLSP 263
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
177-624 |
6.69e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 177 QLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEdIVSVTHKAIEKETDLDSLK 256
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK-ILAEDEKLLDEKKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 257 DKLRKAQHE-------REQ----LECQLQTEKDEKELY-------KVHLKNTEIENTKLVSEIQTL----KNLDGNKESM 314
Cdd:pfam05483 432 EELKGKEQElifllqaREKeihdLEIQLTAIKTSEEHYlkevedlKTELEKEKLKNIELTAHCDKLllenKELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 315 ITHFKEEISKLQSCLADKENLYRalllttsnkedtlflkeQLRKAEEQVQATRQELIFLTKEL---SDAVNVR-DKTmaD 390
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLK-----------------QIENLEEKEMNLRDELESVREEFiqkGDEVKCKlDKS--E 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 391 LHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAAdhyrekfKECQRLQKQINKLSDQA 470
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN-------KQLNAYEIKVNKLELEL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 471 ASTNSVFTKKMGSQQK-VNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTKEIAEKIEKYNKckqLLQD 549
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKeIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDK---IIEE 722
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1244518170 550 EKTKCNKY-AEELAKMELKWKEQVKIAeNVKLELAEVEDNYKVQLAEKEKeinglasylenLSRE-KELTKSLEDQK 624
Cdd:pfam05483 723 RDSELGLYkNKEQEQSSAKAALEIELS-NIKAELLSLKKQLEIEKEEKEK-----------LKMEaKENTAILKDKK 787
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
169-450 |
9.83e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 169 AVLEKETAQLREQVGR--------MERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVS 240
Cdd:pfam00038 28 KLLETKISELRQKKGAepsrlyslYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 241 ---VTHKA----IEKETDLDSLKDKL--RKAQHEREQLECQLQTEKDEkelykvhlKNTEIENTKLVSEIQTLKNLDGNK 311
Cdd:pfam00038 108 lrkDLDEAtlarVDLEAKIESLKEELafLKKNHEEEVRELQAQVSDTQ--------VNVEMDAARKLDLTSALAEIRAQY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 312 ESMITHFKEEIsklqscladkENLYRALL--LTTSNKEDTlflkEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMA 389
Cdd:pfam00038 180 EEIAAKNREEA----------EEWYQSKLeeLQQAAARNG----DALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518170 390 DLHTARLENERVKKQLADTLAEL--QLHAVKKDQEKtdtleheLRREVEDL---KLRLQMAADHYR 450
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELeaELQETRQEMAR-------QLREYQELlnvKLALDIEIATYR 304
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
186-631 |
1.96e-05 |
|
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: 48.58 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 186 ERELSQEKGRCEQLQA---EQKGLLEVSQSLRVENEEfmkrysdATAKvQQLEEDIVSVTH-----KAIEK-----ETDL 252
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEE-------ASGK-KIYEHDSMSTMHfrslgSAISKilrelDTEI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 253 DSLKDKLRKAQHEREQLECQLQTEKDEkeLYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADK 332
Cdd:pfam15921 234 SYLKGRIFPVEDQLEALKSESQNKIEL--LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 333 ENLYRALLlttSNKEDTLF-LKEQLRKA----EEQVQATRQELIFLTKELSDAVNVRDKTMADlhTARLENErVKKQLAD 407
Cdd:pfam15921 312 NSMYMRQL---SDLESTVSqLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQE--SGNLDDQ-LQKLLAD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 408 TLAELQLHAVKKDQEK---------TDTLEHeLRREVEDLKLRLQMAADHYREKFKECQ-RLQKQINKLSDQAASTNSV- 476
Cdd:pfam15921 386 LHKREKELSLEKEQNKrlwdrdtgnSITIDH-LRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 477 -FTKKMGSQQK-----VNDASINTDPAASTSASAVDVKPAASCAETGFDmSTKDHVCEMTKEIAEKIEKYnkckQLLQDE 550
Cdd:pfam15921 465 sLTAQLESTKEmlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIE-ATNAEITKLRSRVDLKLQEL----QHLKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 551 KTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVED----------NYKVQLAEKEKEINGLASYLEnlsrEKELTKSL 620
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagAMQVEKAQLEKEINDRRLELQ----EFKILKDK 615
|
490
....*....|.
gi 1244518170 621 EDQKGRKLEGQ 631
Cdd:pfam15921 616 KDAKIRELEAR 626
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
179-629 |
2.25e-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: 48.09 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 179 REQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDK 258
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 259 LRKAQHEREQLECQLQTEKD-EKELYKVHLKNTEIENT--KLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADKENL 335
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSlESQISELKKQNNQLKDNieKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 336 YRALLLTTSNKEDTL--------------------FLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTAR 395
Cdd:TIGR04523 276 LEQNNKKIKELEKQLnqlkseisdlnnqkeqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 396 LENERVKKQLADTLAELQLhAVKKDQEKTDTLEhELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQaastns 475
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEK-LKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE------ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 476 vfTKKMGSQQKVNDASINtdpaastsasavdvkpaascaetgfdmstkdhvcEMTKEIAEKIEKYNKCKQLLQDEKTKCN 555
Cdd:TIGR04523 428 --IERLKETIIKNNSEIK----------------------------------DLTNQDSVKELIIKNLDNTRESLETQLK 471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1244518170 556 KYAEELAKMELKWKEQVKIAENVKLELAEVEDNyKVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLE 629
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-417 |
2.45e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTE 276
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 277 KDEKELYKV--HLKNTEIENTKLVSEIQTLKNLdgnkesmithfKEEISKLQSCLADKENLYRALLLTTSNKEdtlflKE 354
Cdd:COG4717 129 PLYQELEALeaELAELPERLEELEERLEELREL-----------EEELEELEAELAELQEELEELLEQLSLAT-----EE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1244518170 355 QLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLhtARLENERVKKQLADTLAELQLHAV 417
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL--EQLENELEAAALEERLKEARLLLL 253
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
168-597 |
5.40e-05 |
|
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: 47.04 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKE----TAQLREqvGRMER-ELSQEKGRCE-QLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKvqqleedivSV 241
Cdd:pfam15921 344 IEELEKQlvlaNSELTE--ARTERdQFSQESGNLDdQLQKLLADLHKREKELSLEKEQNKRLWDRDTGN---------SI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 242 THKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKD-------EKELYKVHLKNTEIENTK---------LVSEIQTLK 305
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqgkNESLEKVSSLTAQLESTKemlrkvveeLTAKKMTLE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 306 NLD----------GNKESMITHFKEEISKLQScladKENLYRALLLTTSNKEDTL--------FLKEQLRKAEEQVQATR 367
Cdd:pfam15921 493 SSErtvsdltaslQEKERAIEATNAEITKLRS----RVDLKLQELQHLKNEGDHLrnvqteceALKLQMAEKDKVIEILR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 368 QELifltKELSDAVNVRDKTMADLhtaRLENERVKKQLADTLAELQLHAVKKDqeKTDTLEHELRREVEDLKL------- 440
Cdd:pfam15921 569 QQI----ENMTQLVGQHGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKD--KKDAKIRELEARVSDLELekvklvn 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 441 ----RLQMAADHYREK---FKECQRLQKQINKLSDQAASTNSVF----------TKKMGSQQKVNDASINTDPAASTSAS 503
Cdd:pfam15921 640 agseRLRAVKDIKQERdqlLNEVKTSRNELNSLSEDYEVLKRNFrnkseemettTNKLKMQLKSAQSELEQTRNTLKSME 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 504 AVDVKPAASCAETGFDMSTK----DHVCEMTKEIAEKIEKYNKCKQLLQDEKTKC-----------NKYAEELAKM---E 565
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLsqelstvatekNKMAGELEVLrsqE 799
|
490 500 510
....*....|....*....|....*....|....*.
gi 1244518170 566 LKWKEQVKIAE----NVKLELAEVEDnyKVQLAEKE 597
Cdd:pfam15921 800 RRLKEKVANMEvaldKASLQFAECQD--IIQRQEQE 833
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-443 |
5.78e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 169 AVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEfmkrysdATAKVQQLEEDIVSVTHKAIEK 248
Cdd:pfam01576 64 ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-------EEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 249 ETDLDSLKDKLRKAQHEREQLECQLQtekdekelykvHLKNTEIENTKLVSEIQTLKNldgNKESMITHFKEEISKLQSC 328
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLEERIS-----------EFTSNLAEEEEKAKSLSKLKN---KHEAMISDLEERLKKEEKG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 329 LADKENLYRALLLTTSNkedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADT 408
Cdd:pfam01576 203 RQELEKAKRKLEGESTD------LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL 276
|
250 260 270
....*....|....*....|....*....|....*
gi 1244518170 409 LAELQLHavKKDQEKTDTLEHELRREVEDLKLRLQ 443
Cdd:pfam01576 277 QEDLESE--RAARNKAEKQRRDLGEELEALKTELE 309
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
201-411 |
6.58e-05 |
|
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: 45.30 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 201 AEQKGLLEVsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLqtEKDEK 280
Cdd:COG1579 4 EDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 281 ELYKVHlKNTEIENtkLVSEIQTLKnldgnkesmithfkEEISKLqscladkenlyralllttsnKEDTLFLKEQLRKAE 360
Cdd:COG1579 81 QLGNVR-NNKEYEA--LQKEIESLK--------------RRISDL--------------------EDEILELMERIEELE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 361 EQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAE 411
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-634 |
8.23e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 315 ITHFKEEISKLQSCLAD-KENLYRAlllttsnkEDTLF-LKEQLRKAEEQVQATrQELIFLTKELSDA---VNVRDKTma 389
Cdd:TIGR02168 167 ISKYKERRKETERKLERtRENLDRL--------EDILNeLERQLKSLERQAEKA-ERYKELKAELRELelaLLVLRLE-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 390 DLHTARLENERVKKQLADTLAELQLHAVKKdQEKTDTLE---HELRREVEDLKLRLQMAAdhyrekfKECQRLQKQINKL 466
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQEL-EEKLEELRlevSELEEEIEELQKELYALA-------NEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 467 SDQAASTNsvftkkmgSQQKVNDASINTDPaastsasavdvkpaascaetgfdmSTKDHVCEMTKEIAEKIEKYNKCKQL 546
Cdd:TIGR02168 308 RERLANLE--------RQLEELEAQLEELE------------------------SKLDELAEELAELEEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 547 LQDEKTkcnKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKV---QLAEKEKEINGLASYLENLSREKE-LTKSLED 622
Cdd:TIGR02168 356 LEAELE---ELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEeLLKKLEE 432
|
330
....*....|..
gi 1244518170 623 QKGRKLEGQSPQ 634
Cdd:TIGR02168 433 AELKELQAELEE 444
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
351-469 |
9.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 351 FLKEQLRKAEEQVQATRQEL-IFLTK----ELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTD 425
Cdd:COG3206 179 FLEEQLPELRKELEEAEAALeEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1244518170 426 TLEH----ELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQ 469
Cdd:COG3206 259 LLQSpviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
172-448 |
1.25e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITH-FKEEISKLQSCLA 330
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAeELLEAKDSLEAKL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLA 410
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
250 260 270
....*....|....*....|....*....|....*...
gi 1244518170 411 ELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADH 448
Cdd:COG4372 312 ALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
780-807 |
1.29e-04 |
|
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar proteins; spn-F is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. It acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F is a coil-coiled protein containing a C2H2-type zinc binding domain.
Pssm-ID: 412017 Cd Length: 30 Bit Score: 39.82 E-value: 1.29e-04
10 20
....*....|....*....|....*...
gi 1244518170 780 KVCPMCSEQFPPDYDQQGFERHVQTHFD 807
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-400 |
1.41e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 153 KIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQ 232
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 233 QLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKE 312
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 313 SMITHFKEEISKLQSCL-ADKENLYRALLLTTSN---------KEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVN 382
Cdd:TIGR04523 531 SEKKEKESKISDLEDELnKDDFELKKENLEKEIDeknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
250
....*....|....*...
gi 1244518170 383 VRDKTMADLHTARLENER 400
Cdd:TIGR04523 611 KISSLEKELEKAKKENEK 628
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
780-806 |
2.45e-04 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 39.02 E-value: 2.45e-04
10 20
....*....|....*....|....*..
gi 1244518170 780 KVCPMCSEQFPPDYDQQGFERHVQTHF 806
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-472 |
3.67e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLrveneefmkrysdatakvqqleedivsvthkaie 247
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL---------------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 248 kETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQS 327
Cdd:TIGR04523 390 -ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 328 CLADKENLYRALLLTTSNKEDTLFLKEQ-LRKAEEQVQATRQELIFLTKELSDAVNVRDKtmadlhtarLENErvKKQLA 406
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKeLKKLNEEKKELEEKVKDLTKKISSLKEKIEK---------LESE--KKEKE 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 407 DTLAELQLHAVKKDQEKT-DTLEHELR---REVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAS 472
Cdd:TIGR04523 538 SKISDLEDELNKDDFELKkENLEKEIDeknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
320-479 |
5.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 320 EEISKLQSCLADKENLYRALLlTTSNKEDTLflkEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENE 399
Cdd:COG4913 225 EAADALVEHFDDLERAHEALE-DAREQIELL---EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 400 RvkKQLADTLAELQLHAVKKDQ--EKTDTLEHELR----REVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAST 473
Cdd:COG4913 301 R--AELARLEAELERLEARLDAlrEELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
....*.
gi 1244518170 474 NSVFTK 479
Cdd:COG4913 379 AEEFAA 384
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-629 |
5.70e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 204 KGLLEVSQSL--RVEN-EEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLEcqlqtekdek 280
Cdd:PRK03918 165 KNLGEVIKEIkrRIERlEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE---------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 281 ELyKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLAD------KENLYRALllttsnKEDTLFLKE 354
Cdd:PRK03918 235 EL-KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkeKAEEYIKL------SEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 355 QLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMadlhtarlENERVKKQLADTLAELQ-----LHAVKKDQEKTDTLEH 429
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEerhelYEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 430 ELR-REVEDLKLRLQMAadhyrEKFKEcqRLQKQINKLSDQAASTNSVFTKKMGSQQKVNDASintdpaastsasavdvk 508
Cdd:PRK03918 380 RLTgLTPEKLEKELEEL-----EKAKE--EIEEEISKITARIGELKKEIKELKKAIEELKKAK----------------- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 509 paASCAETGFDMsTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWK---------EQVKIAENV- 578
Cdd:PRK03918 436 --GKCPVCGREL-TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKELEEKl 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 579 -KLELAEVEDNY------KVQLAEKEKEINGLASYLEnlsREKELTKSLE--DQKGRKLE 629
Cdd:PRK03918 513 kKYNLEELEKKAeeyeklKEKLIKLKGEIKSLKKELE---KLEELKKKLAelEKKLDELE 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
174-638 |
5.83e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 174 ETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETdld 253
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK--- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 254 slKDKLRKAQHEREQLECQLQTEKDEKelyKVHLKNTEIENTKLVSEIQtlKNLDGNKESMITHFKEEISKLQSCLADKE 333
Cdd:PTZ00121 1292 --ADEAKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEAKKKADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 334 NLYRALLLTTSNKEDTLFLK---EQLRKAEEQVQATRQElifltKELSDAVNVRDKTMADLHTARLENERVKKqlADTLA 410
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEED-----KKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 411 ELQLHAVKKDQEKTDTLEH----------ELRREVEDLKLRLQMA--ADHYREKFKECQRLQKQINKLSD---QAASTNS 475
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAkkaeeakkkaEEAKKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEakkKADEAKK 1517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 476 VFTKKMGSQQKVNDASINTDPA--ASTSASAVDVKPAASC--------AETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQ 545
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEELkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 546 LLQDEKTKCNKyAEELAKME-LKWK-EQVKIAENVK-----LELAEVEDNYKVQLAEKEKEINGLASYLENLSREKELTK 618
Cdd:PTZ00121 1598 MKLYEEEKKMK-AEEAKKAEeAKIKaEELKKAEEEKkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
490 500
....*....|....*....|
gi 1244518170 619 SLEDQKGRKLEGQSPQQVSR 638
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKK 1696
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-477 |
5.85e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEedivsvthkaiEKET 250
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-----------SLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQLECQLQtekdekelykvhlknteientKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRK---------------------QLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTAR-----LENERVKKQL 405
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGlalsaLLDALELEED 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518170 406 ADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTNSVF 477
Cdd:COG4372 248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-471 |
6.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLrvenEEFMKRYSDATAK-VQQLEEDIVSVTHKAIEKE 249
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL----EELLEQLSLATEEeLQDLAEELEELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 250 TDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYK--------------VHLKNTEIENTKLVSEIQTL----------- 304
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallalLGLGGSLLSLILTIAGVLFLvlgllallfll 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 305 ---KNLDGNKESMITHFKEEISKLQSclADKENLYRALLLTTSNKEDTLF--------LKEQLRKAEEQV-QATRQELIF 372
Cdd:COG4717 293 larEKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLelldrieeLQELLREAEELEeELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 373 LTKELSDAVNVRDKTM-ADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYRE 451
Cdd:COG4717 371 EIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
330 340
....*....|....*....|
gi 1244518170 452 KFKECQRLQKQINKLSDQAA 471
Cdd:COG4717 451 LREELAELEAELEQLEEDGE 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-629 |
6.78e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQK--GLLEVSQSLRVENEEFMKRYSDATAKVQQLEedivsvthkaiEK 248
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR-----------EL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 249 ETDLDSLKDKLRKAQHEREQLECQLQTEKDEkelykvHLKNTEIENTKLVSEIQTLknldgnkesmithfKEEISKLQSC 328
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAEL--------------EEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 329 LADKENLYRALllttSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKT------MADLHTARLENERVK 402
Cdd:COG4717 222 LEELEEELEQL----ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 403 KQLADTLAELQLHAVKKDQEktdtlEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAStnsvftkkmg 482
Cdd:COG4717 298 ASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE---------- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 483 SQQKVNDASINtdpaastsasavdvkpaASCAETGFDMSTK-DHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEEL 561
Cdd:COG4717 363 LQLEELEQEIA-----------------ALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1244518170 562 AKMELKWKeqvkiAENVKLELAEVEDnykvQLAEKEKEINGLASYLENLSREKELTKsLEDQKGRKLE 629
Cdd:COG4717 426 DEEELEEE-----LEELEEELEELEE----ELEELREELAELEAELEQLEEDGELAE-LLQELEELKA 483
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-425 |
7.66e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL---LEVSQSLRVENEEFMKRYSdatAKVQQLEEDIVSVTHKAIEK 248
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALqeqLQAETELCAEAEEMRARLA---ARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 249 ETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSC 328
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 329 LADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQvqaTRQELIFLTKELSDAVNVRDKTMADLhtaRLENERVKKQLADT 408
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEK---GRQELEKAKRKLEGESTDLQEQIAEL---QAQIAELRAQLAKK 241
|
250
....*....|....*..
gi 1244518170 409 LAELQLHAVKKDQEKTD 425
Cdd:pfam01576 242 EEELQAALARLEEETAQ 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-450 |
8.05e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEqkglleVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQ------LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 252 LDSLKDKLRKAQHEREQLECQL---------------------------------------------QTEKDEKELYKVH 286
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 287 LKNT--EIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTLFLK----------- 353
Cdd:COG4717 309 ALPAleELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagvedeeelr 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 354 ------EQLRKAEEQVQATRQELIFLTKELSDAVNVRDKT--MADLHTARLENERVKKQLADTLAEL-QLHAVKKDQEKT 424
Cdd:COG4717 389 aaleqaEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELaELEAELEQLEED 468
|
330 340
....*....|....*....|....*.
gi 1244518170 425 DTLEhELRREVEDLKLRLQMAADHYR 450
Cdd:COG4717 469 GELA-ELLQELEELKAELRELAEEWA 493
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
175-635 |
8.68e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 175 TAQLREQVGRMERELSQE---KGRCEQLQAE-QKGLLEVsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:pfam10174 267 TEDREEEIKQMEVYKSHSkfmKNKIDQLKQElSKKESEL-LALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKelykvhlknteienTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:pfam10174 346 EVDALRLRLEEKESFLNKKTKQLQDLTEEK--------------STLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKEnlyralllttsnkedtlflkEQLRKAEEQVQATRQelifltkelsDAVNVrDKTMADLHTARLENERVkkqladtLA 410
Cdd:pfam10174 412 DKD--------------------KQLAGLKERVKSLQT----------DSSNT-DTALTTLEEALSEKERI-------IE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 411 ELQLHAVKKDQEKTDTLEhELRREVEDLKLRLQMAADHYREKfkecqrlQKQINKLSDQAASTNSVFTKKMGS------- 483
Cdd:pfam10174 454 RLKEQREREDRERLEELE-SLKKENKDLKEKVSALQPELTEK-------ESSLIDLKEHASSLASSGLKKDSKlksleia 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 484 -QQKVNDAS--INTDPAASTSASAVDVKPAAScaetgfdmstkDHVCEMTKEIAEKIEKYNKCK----QLL------QDE 550
Cdd:pfam10174 526 vEQKKEECSklENQLKKAHNAEEAVRTNPEIN-----------DRIRLLEQEVARYKEESGKAQaeveRLLgilrevENE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 551 KTKCNKYAEELAKMEL-KWKEQVKIAENVKLELAEVEDNYKVQLAEKEKEINGLAS-----YLENLSREKELTKSLEDQK 624
Cdd:pfam10174 595 KNDKDKKIAELESLTLrQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsqqlQLEELMGALEKTRQELDAT 674
|
490
....*....|.
gi 1244518170 625 GRKLegQSPQQ 635
Cdd:pfam10174 675 KARL--SSTQQ 683
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-443 |
1.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDA-TAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQT 275
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 276 EKDEKELYKvHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTLFLKEQ 355
Cdd:PTZ00121 1642 EAEEKKKAE-ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 356 LRKAEEQVQATRQELIFLTKElsdavnvrDKTMADlhTARLENERvKKQLADTLAELQLHAVKKDQEKTDTLEHELRREV 435
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE--------DKKKAE--EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
....*...
gi 1244518170 436 EDLKLRLQ 443
Cdd:PTZ00121 1790 EKRRMEVD 1797
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-437 |
1.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 247 EKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKN--TEIENTKLVSEIQTLKN-----LDGNKEsmITHFK 319
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswDEIDVASAEREIAELEAelerlDASSDD--LAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 320 EEISKLQSCLADKENLYRALllttsnkedtlflKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENE 399
Cdd:COG4913 692 EQLEELEAELEELEEELDEL-------------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
170 180 190
....*....|....*....|....*....|....*...
gi 1244518170 400 RVKKQLADTLAELQlHAVKKDQEKTDTLEHELRREVED 437
Cdd:COG4913 759 LGDAVERELRENLE-ERIDALRARLNRAEEELERAMRA 795
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
780-807 |
1.16e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 37.04 E-value: 1.16e-03
10 20
....*....|....*....|....*...
gi 1244518170 780 KVCPMCSEQFPpDYDQQGFERHVQTHFD 807
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-442 |
1.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSL------------RVENEEFMKRYSDATAKVQQLE 235
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaereIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 236 EDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKElykvhlkntEIENTKLVSEIQTLknldgnkesmi 315
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---------AAEDLARLELRALL----------- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 316 thfkeeisklqscladkENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELI-----------FLTKELSDAVNVR 384
Cdd:COG4913 752 -----------------EERFAAALGDAVERELRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESL 814
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 385 DKTMADLHtaRLENE---RVKKQLADTLAELQlhavkkDQEKTDtLEHELRREVEDLKLRL 442
Cdd:COG4913 815 PEYLALLD--RLEEDglpEYEERFKELLNENS------IEFVAD-LLSKLRRAIREIKERI 866
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
227-517 |
1.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 227 ATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLEcqlqtekdekelykvhlknTEIENTKlvSEIQTLkn 306
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ-------------------AELEALQ--AEIDKL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 307 ldgnkesmithfKEEISKLQSCLADKENLyralllttsnkedtlfLKEQLRKAEEQ-VQATRQELIFLTKELSDAVNvR- 384
Cdd:COG3883 71 ------------QAEIAEAEAEIEERREE----------------LGERARALYRSgGSVSYLDVLLGSESFSDFLD-Rl 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 385 ----------DKTMADLHTARLENERVKKQLADTLAELQ--LHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREK 452
Cdd:COG3883 122 salskiadadADLLEELKADKAELEAKKAELEAKLAELEalKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1244518170 453 FKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAETG 517
Cdd:COG3883 202 EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
394-626 |
1.34e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 394 ARLENERVKKQLADTLAELQlhAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAST 473
Cdd:COG4942 25 AEAELEQLQQEIAELEKELA--ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 474 NSVFTKKMGSQQKVNDAS-----INTDPAASTSASAVDVKpaascaetgfdmSTKDHVCEMTKEIAEKIEKYNKCKQLLQ 548
Cdd:COG4942 103 KEELAELLRALYRLGRQPplallLSPEDFLDAVRRLQYLK------------YLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 549 DEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQLAEKEKEINGLASYLENLSRE------KELTKSLED 622
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEaaaaaeRTPAAGFAA 250
|
....
gi 1244518170 623 QKGR 626
Cdd:COG4942 251 LKGK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
234-464 |
1.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 234 LEE-DIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLEcqlQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKE 312
Cdd:COG4913 218 LEEpDTFEAADALVEHFDDLERAHEALEDAREQIELLE---PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 313 SMITHFKEEISKLQSCLADKENLYRALllttsnKEDTLFLKEQLRKAE-EQVQATRQELIFLTKELSDAVNVRDKTMADL 391
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDAL------REELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1244518170 392 HTARLENERVKKQLADTLAELQLHAvkkdqEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQIN 464
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALL-----EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-281 |
1.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 145 TKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKG-RCEQLQAEQKGLLEVSQSLRVENEEFMKR 223
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1244518170 224 YSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKE 281
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
753-778 |
1.51e-03 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 36.76 E-value: 1.51e-03
10 20
....*....|....*....|....*.
gi 1244518170 753 KKCPLCELMFPPNYDQTKFEEHVESH 778
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-469 |
1.57e-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: 41.93 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQslrvENEEFMKRYSDATAKVQQLEEDIvsvthkaIEKET 250
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKD----EQNKIKKQLSEKQKELEQNNKKI-------KELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQ-----LECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLK----NLDGNKESMITHFKEE 321
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKkeltNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 322 ISKLQSCLADKENLYRALLLTTSNKEDtlfLKEQLRKAEEQVQATRQELIFLTKELsdavNVRDKTMADLHTARLENERV 401
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEK----ELLEKEIERLKETIIKNNSE 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 402 KKQLADTLAELQLhAVKKDQEKTDTLEHELR---REVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQ 469
Cdd:TIGR04523 442 IKDLTNQDSVKEL-IIKNLDNTRESLETQLKvlsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
173-490 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 173 KETAQLREQVgRMERELS-QEKGRCEQL--------------QAEQKGL---LEVSQSLRVENEEFMKRYSDATAKVQQ- 233
Cdd:pfam07111 73 QELRRLEEEV-RLLRETSlQQKMRLEAQameldalavaekagQAEAEGLraaLAGAEMVRKNLEEGSQRELEEIQRLHQe 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 234 --------LEEDIVSVTHKAIEKETDLDSLKDK-------LRKAQHEREQLECQLQTEKDEKE----------------- 281
Cdd:pfam07111 152 qlssltqaHEEALSSLTSKAEGLEKSLNSLETKrageakqLAEAQKEAELLRKQLSKTQEELEaqvtlveslrkyvgeqv 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 282 LYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADKENLyrallLTTSNKEDTLFLKEQLRKAEE 361
Cdd:pfam07111 232 PPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEE-----LTRKIQPSDSLEPEFPKKCRS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 362 QVQATRQELIFLtkelsdavnvrdktMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTdTLEHELRR-----EVE 436
Cdd:pfam07111 307 LLNRWREKVFAL--------------MVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQA-ILQRALQDkaaevEVE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1244518170 437 DLKLR-LQMAADHYREKFKecqRLQKQINKLSDQ----AASTNSVFTKKMGSQQKVNDA 490
Cdd:pfam07111 372 RMSAKgLQMELSRAQEARR---RQQQQTASAEEQlkfvVNAMSSTQIWLETTMTRVEQA 427
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-395 |
1.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRME---RELSQEKGRCEQLQAEQKGLLEVSQ---SLRVENEEFMKRYSDATAKVQQLEEDIVSVTH- 243
Cdd:PRK04863 892 LADRVEEIREQLDEAEeakRFVQQHGNALAQLEPIVSVLQSDPEqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHf 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 244 ------KAIEKETDL-DSLKDKLRKAQHEREQLECQLQTEKDEKELY-KVHlknteienTKLVSEIQTlknldgnKESMI 315
Cdd:PRK04863 972 syedaaEMLAKNSDLnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYnQVL--------ASLKSSYDA-------KRQML 1036
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 316 THFKEEISKLqSCLADKENLYRAlllttSNKEDTlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTAR 395
Cdd:PRK04863 1037 QELKQELQDL-GVPADSGAEERA-----RARRDE--LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
294-631 |
1.79e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 294 NTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADkenLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFL 373
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 374 TKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTdtlehELRREVEDLKLRLQMAADHYREKF 453
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQ-----STNSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 454 KECQRLQKQINKLSDQaastnsvftkkmgsQQKVNDASINTdpaASTSASAVDVKPAASCAETGFDM-STKDHVCEMTKE 532
Cdd:pfam05557 153 QLRQNLEKQQSSLAEA--------------EQRIKELEFEI---QSQEQDSEIVKNSKSELARIPELeKELERLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 533 IAEKIEKYNKCKQLLQDEKTKCNKYAE----------ELAKMELKWKEQVKIAENVKLELAEVED--NYKVQLAEKEKEI 600
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKyreeaatlelEKEKLEQELQSWVKLAQDTGLNLRSPEDlsRRIEQLQQREIVL 295
|
330 340 350
....*....|....*....|....*....|.
gi 1244518170 601 NGLASYLENLSREKELTKSLEDQKGRKLEGQ 631
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
161-476 |
1.85e-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: 41.88 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 161 KeellkliAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVS 240
Cdd:pfam02463 175 L-------KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 241 VTHKAIEKETDLdsLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQT----LKNLDGNKESMIT 316
Cdd:pfam02463 248 DEQEEIESSKQE--IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 317 HFKEEISKLQSCLADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHtaRL 396
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS--EE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 397 ENERvkkQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTNSV 476
Cdd:pfam02463 404 EKEA---QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-601 |
1.97e-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: 41.93 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 230 KVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEreqlecqLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDG 309
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNE-------IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 310 NKESMI--------------THFKEEISKLQSCLADKENLYRALLLTTSNKEDTL-FLKEQLRKAEEQVQATRQELIFLT 374
Cdd:TIGR04523 409 QKDEQIkklqqekellekeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTReSLETQLKVLSRSINKIKQNLEQKQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 375 KELSDAVNVRDKtmadlhtarLENErvKKQLADTLAEL--QLHAVKKDQEKTDTLEHELRREVEDLKLRLQmaADHYREK 452
Cdd:TIGR04523 489 KELKSKEKELKK---------LNEE--KKELEEKVKDLtkKISSLKEKIEKLESEKKEKESKISDLEDELN--KDDFELK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 453 F----KECQRLQKQINKLS-DQAASTNSVFTKKMGSQQKvndasintdpaastsasavdvkpaascaetgfdmstKDHVC 527
Cdd:TIGR04523 556 KenleKEIDEKNKEIEELKqTQKSLKKKQEEKQELIDQK------------------------------------EKEKK 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1244518170 528 EMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELaeveDNYKVQLAEKEKEIN 601
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI----KEIRNKWPEIIKKIK 669
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
172-452 |
1.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLR--------VENEEFMKRYSDATAKVQQLEEDIVSVTH 243
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlnlLADETLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 244 --KAIEKetdLDSLKDKLRKAQHEREQLECQLQTEKDEKELYK-------------VHLKNTE-----IENTKLVSEIQT 303
Cdd:PRK04863 916 hgNALAQ---LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqqafaltevvqrrAHFSYEDaaemlAKNSDLNEKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 304 -LKnldgNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTLF-LKEQLRK--------AEEQVQATRQELifl 373
Cdd:PRK04863 993 rLE----QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQeLKQELQDlgvpadsgAEERARARRDEL--- 1065
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 374 tkelsdavnvrdktMADLHTARLENERVKKQLadTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLR----LQMAADHY 449
Cdd:PRK04863 1066 --------------HARLSANRSRRNQLEKQL--TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGwcavLRLVKDNG 1129
|
...
gi 1244518170 450 REK 452
Cdd:PRK04863 1130 VER 1132
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
254-629 |
2.42e-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: 41.54 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 254 SLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTL----KNLDGNKESMITHFKEEISKLQSCL 329
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSnnkiKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 330 ADKENLYRALlltTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTL 409
Cdd:TIGR04523 103 SDLSKINSEI---KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 410 AELQlhavkKDQEKTDTLEHELRRevedLKLRLqMAADHYREKFKEcqrLQKQINKLSDQAASTNSVFTKKMGSQQKVND 489
Cdd:TIGR04523 180 KEKL-----NIQKNIDKIKNKLLK----LELLL-SNLKKKIQKNKS---LESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 490 ASINTDPAASTsasavdvkpaascaetgfdmsTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAkmELKWK 569
Cdd:TIGR04523 247 EISNTQTQLNQ---------------------LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS--DLNNQ 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1244518170 570 EQVKIAENVKLELAEVED---NYKVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLE 629
Cdd:TIGR04523 304 KEQDWNKELKSELKNQEKkleEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
215-439 |
2.47e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 215 VENEEFMKRYSDATA-------KVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQL--ECQLQTEKDEkELYKV 285
Cdd:pfam05622 169 LQLEEELKKANALRGqletykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLiiERDTLRETNE-ELRCA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 286 HLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQS-----CLADKENLYRAL-----LLTTSNKEDTLfLKEQ 355
Cdd:pfam05622 248 QLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHenkmlRLGQEGSYRERLtelqqLLEDANRRKNE-LETQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 356 LRKAEEQVQATRQELIFLTKELS-------DAVNVRDKT---MADLHTARLENERVKKQLAdtlaELQLHAVKKDQEKTD 425
Cdd:pfam05622 327 NRLANQRILELQQQVEELQKALQeqgskaeDSSLLKQKLeehLEKLHEAQSELQKKKEQIE----ELEPKQDSNLAQKID 402
|
250
....*....|....
gi 1244518170 426 TLEHELRREVEDLK 439
Cdd:pfam05622 403 ELQEALRKKDEDMK 416
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
753-779 |
2.49e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 35.94 E-value: 2.49e-03
10 20
....*....|....*....|....*..
gi 1244518170 753 KKCPLCELMFPPNYDQTKFEEHVESHW 779
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-615 |
3.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 218 EEFMKRYSDATAKVQQLEEDivsvthkaieKETDLDSLKDklrkaqhereQLEcqlqtEKDEKELYKVhLKNTEIENTKL 297
Cdd:PRK02224 165 EEYRERASDARLGVERVLSD----------QRGSLDQLKA----------QIE-----EKEEKDLHER-LNGLESELAEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 298 VSEIqtlKNLDGNKE----------SMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDtlfLKEQLRKAEEQVQATR 367
Cdd:PRK02224 219 DEEI---ERYEEQREqaretrdeadEVLEEHEERREELETLEAEIEDLRETIAETEREREE---LAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 368 QEL--IFLTKELSDAvnvrDKTMADLHTARLENErvKKQLADTLAELQLHA------VKKDQEKTDTLEH---ELRREVE 436
Cdd:PRK02224 293 EERddLLAEAGLDDA----DAEAVEARREELEDR--DEELRDRLEECRVAAqahneeAESLREDADDLEEraeELREEAA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 437 DLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAST-----------NSVFTKKMGSQQKVNDASINTDPAASTSASAV 505
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdlgnaedflEELREERDELREREAELEATLRTARERVEEAE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 506 DVKPAASCAETGFDMSTKDHVCEMTkEIAEKIEKYNKCKQLLQDEKTKCNK---YAEELAKMElkwKEQVKIAENVKLeL 582
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVEEVEErleRAEDLVEAE---DRIERLEERRED-L 521
|
410 420 430
....*....|....*....|....*....|....*.
gi 1244518170 583 AEVEDNYKVQLAEKEKEINGL---ASYLENLSREKE 615
Cdd:PRK02224 522 EELIAERRETIEEKRERAEELrerAAELEAEAEEKR 557
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
172-411 |
3.34e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREqVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEfmKRYSDATAKVQQLEEDIVsvthkaiEKETD 251
Cdd:PRK05771 39 ELSNERLRK-LRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLE--ELIKDVEEELEKIEKEIK-------ELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKELYK--------VHLKNTEIENTKLVSEIQTLKNLDGNKESM----ITH-- 317
Cdd:PRK05771 109 ISELENEIKELEQEIERLEPWGNFDLDLSLLLGfkyvsvfvGTVPEDKLEELKLESDVENVEYISTDKGYVyvvvVVLke 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 318 FKEEISKLqsclaDKENLYRALLLTTSNKedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHtARLE 397
Cdd:PRK05771 189 LSDEVEEE-----LKKLGFERLELEEEGT-----PSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALY-EYLE 257
|
250
....*....|....
gi 1244518170 398 NERVKKQLADTLAE 411
Cdd:PRK05771 258 IELERAEALSKFLK 271
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-629 |
3.83e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 352 LKEQLRKAEEQVQATRQeliflTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHEL 431
Cdd:COG1196 198 LERQLEPLERQAEKAER-----YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 432 RREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAStNSVFTKKMGSQQKVNDASINTDPA--ASTSASAVDVKP 509
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-LEERLEELEEELAELEEELEELEEelEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 510 AASCAETGFDMSTKDHVcEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNY 589
Cdd:COG1196 352 ELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1244518170 590 KVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLE 629
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-300 |
4.09e-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: 40.82 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 174 ETAQLREqvgrmerELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLD 253
Cdd:TIGR02169 386 ELKDYRE-------KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1244518170 254 SLKDKLRKAQHEREQLECQLQteKDEKELYKVHLKNTEIENTKLVSE 300
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYD--RVEKELSKLQRELAEAEAQARASE 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-467 |
4.43e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQA------EQKGLLEVSQSLRVENE--EFMKRYsdaTAKVQQLEEDIV 239
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkKAKGKCPVCGRELTEEHrkELLEEY---TAELKRIEKELK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 240 svthKAIEKETDLDSLKDKLRKAQHEREQLECQLQT----EKDEKELYKVHL-----KNTEIENTK-----LVSEIQTLK 305
Cdd:PRK03918 470 ----EIEEKERKLRKELRELEKVLKKESELIKLKELaeqlKELEEKLKKYNLeelekKAEEYEKLKeklikLKGEIKSLK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 306 NLDGNKESMITHFKEEISKLQSCLADKENLYRAL--LLTTSNKEDTLFLKE---------QLRKAEEQVQATRQELIFLT 374
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELeeLGFESVEELEERLKElepfyneylELKDAEKELEREEKELKKLE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 375 KELSDAVNVRDKTMADLhtarlenERVKKQladtLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFK 454
Cdd:PRK03918 626 EELDKAFEELAETEKRL-------EELRKE----LEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
330
....*....|...
gi 1244518170 455 ECQRLQKQINKLS 467
Cdd:PRK03918 695 TLEKLKEELEERE 707
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
200-465 |
5.80e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 200 QAEQKGLLEVSQSLRV-----ENEEFMKRYSDATAKVQQLEEDivsvthkaieketdLDSLKDKLRKAQHEREQLECQLQ 274
Cdd:COG0497 131 QHEHQSLLDPDAQRELldafaGLEELLEEYREAYRAWRALKKE--------------LEELRADEAERARELDLLRFQLE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 275 tekdekELYKVHLKNTEIEntKLVSEIQTLKN--------------LDGNKESMITHFKEEISKLQScLADKENLYRALL 340
Cdd:COG0497 197 ------ELEAAALQPGEEE--ELEEERRRLSNaeklrealqealeaLSGGEGGALDLLGQALRALER-LAEYDPSLAELA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 341 lttsnkedtlflkEQLRKAEEQVQATRQELifltKELSDAVnvrdktmaDLHTARLE--NER------VKKQLADTLAEL 412
Cdd:COG0497 268 -------------ERLESALIELEEAASEL----RRYLDSL--------EFDPERLEevEERlallrrLARKYGVTVEEL 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 413 -QLHAvkKDQEKTDTLEH------ELRREVEDLKLRLQMAADHYREKFKEC-QRLQKQINK 465
Cdd:COG0497 323 lAYAE--ELRAELAELENsderleELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTA 381
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
169-634 |
5.92e-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: 40.34 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 169 AVLEKETAQLREqvgrmerELSQEKGRCEQLQAEQKgLLEVSQSLRVENEEFMKRYSDATAKVQQLEEdivsvTHKAIEK 248
Cdd:TIGR00618 222 QVLEKELKHLRE-------ALQQTQQSHAYLTQKRE-AQEEQLKKQQLLKQLRARIEELRAQEAVLEE-----TQERINR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 249 EtdldslKDKLRKAQHEREQLECQLQTEKDEKElykvhLKNTEIENTKLVSEIQTL----KNLDGNKESMITHFKEEISK 324
Cdd:TIGR00618 289 A------RKAAPLAAHIKAVTQIEQQAQRIHTE-----LQSKMRSRAKLLMKRAAHvkqqSSIEEQRRLLQTLHSQEIHI 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 325 LQSclADKENLYRALL-LTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKElsdavnvrdKTMADLHTARLENERVKK 403
Cdd:TIGR00618 358 RDA--HEVATSIREIScQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE---------QATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 404 QLADTLAELQlhavkkdQEKTDTLEHELRREVEDLKLRlQMAADHYREKFKECQRLQKQINKLSDQAASTNSVFTKKMGS 483
Cdd:TIGR00618 427 AHAKKQQELQ-------QRYAELCAAAITCTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 484 QQKVNDASINTDPAASTSASAVDVKPAASC---------AETGFDMSTKDHVC-EMTKEIAEKIEKYNKCKQLLQDEKTK 553
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmqrgeqtyAQLETSEEDVYHQLtSERKQRASLKEQMQEIQQSFSILTQC 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 554 CNKYAEELAK-------------MELKWKEQVKIAENV-KLELAEVEDNYKVQLAEKE------KEINGLASYLENLSRE 613
Cdd:TIGR00618 579 DNRSKEDIPNlqnitvrlqdlteKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQcsqelaLKLTALHALQLTLTQE 658
|
490 500
....*....|....*....|.
gi 1244518170 614 KELTKSLEDQKGRKLEGQSPQ 634
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQ 679
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
126-463 |
6.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 126 VEELLTMEDEGNSDMLVVTTKAGLLELKIektlkekEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKG 205
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEA-------ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 206 LLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQ----------------- 268
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphve 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 269 --LECQLQTEKDEKELYKVHLKNTEIEN--------TKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADKENlyRA 338
Cdd:PRK02224 469 tiEEDRERVEELEAELEDLEEEVEEVEErleraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE--RA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 339 LLLTTSNKEDtlflKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDK--TMADLHTARLENERVKKQLADTLAELQ-LH 415
Cdd:PRK02224 547 AELEAEAEEK----REAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAeLN 622
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518170 416 AVKKDQ-----EKTDTLEHELRRE-VEDLKLRLQMA-------ADHYREKFKECQRLQKQI 463
Cdd:PRK02224 623 DERRERlaekrERKRELEAEFDEArIEEAREDKERAeeyleqvEEKLDELREERDDLQAEI 683
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
172-637 |
6.15e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 172 EKETAQLREQVGRME---RELSQEKGRCE------QLQAE-------QKGLLEVSQSLRVENEEFmKRYSDATAKVQQLE 235
Cdd:TIGR00606 318 ERELVDCQRELEKLNkerRLLNQEKTELLveqgrlQLQADrhqehirARDSLIQSLATRLELDGF-ERGPFSERQIKNFH 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 236 E-DIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLkntEIENTKLVSEIQTLKNLDGNKESM 314
Cdd:TIGR00606 397 TlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL---EKKQEELKFVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 315 ITHFKEEISKLQSC-LADKENLYRALLL-TTSNKEDTLFLKEQLRKAEEQVQ------ATRQELIFLTKELSDAVN-VRD 385
Cdd:TIGR00606 474 LELDQELRKAERELsKAEKNSLTETLKKeVKSLQNEKADLDRKLRKLDQEMEqlnhhtTTRTQMEMLTKDKMDKDEqIRK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 386 KTM--ADLHTARLENERVKKQLADTLaelqlHAVKKDQEKTdtlehelRREVEDLKLRLQMAADHYREKFKECQRLQKQI 463
Cdd:TIGR00606 554 IKSrhSDELTSLLGYFPNKKQLEDWL-----HSKSKEINQT-------RDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 464 NKLSD---QAASTNSVFTKKMGSQQKVNDASINTDPAASTSAsAVDVKPAASCAETGFDMSTKDHVCEMTKEIAEKIEKY 540
Cdd:TIGR00606 622 SSYEDklfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATA-VYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 541 NKCKQLLQDEKTKCNKyaeELAKMELKWKEQvkiaenvkLELAEVEDNykvQLAEKEKEINGLASYLENLSREKELTKSL 620
Cdd:TIGR00606 701 QSKLRLAPDKLKSTES---ELKKKEKRRDEM--------LGLAPGRQS---IIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
490
....*....|....*..
gi 1244518170 621 EDQKGRKLEGQSPQQVS 637
Cdd:TIGR00606 767 IEEQETLLGTIMPEEES 783
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-438 |
6.80e-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: 40.00 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATA 229
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 230 KVQQLEEDIVSVTHKAIEKETDL--DSLKDKLRKAQHEREQL-ECQLQTEKDEKELYKVhLKNTEIENTKLVSEIQTLKN 306
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELkQTQKSLKKKQEEKQEL-IDQKEKEKKDLIKEIEEKEK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 307 LDGNKESMITHFKEEISKLQSCLADKENLYRALllttsnKEDTLFLKEQLRKaeeqVQATRQELIFLTKELSDAVNVRDK 386
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKL------KQEVKQIKETIKE----IRNKWPEIIKKIKESKTKIDDIIE 680
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1244518170 387 TMAD------LHTARLENERVKKQLADTLAELQLHaVKKDQEKTDTLEHELRREVEDL 438
Cdd:TIGR04523 681 LMKDwlkelsLHYKKYITRMIRIKDLPKLEEKYKE-IEKELKKLDEFSKELENIIKNF 737
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
171-491 |
7.22e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 171 LEKETAQLREQVGRMERELSQEKGrceQLQAEQKGLlevsQSLRVENEEFMKRYSDATAKVQQLEEDIVsvthkaiEKET 250
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRA---QLAKKEEEL----QAALARLEEETAQKNNALKKIRELEAQIS-------ELQE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 251 DLDSLKDKLRKAQHEREQLECQLQTEKdekelykvhlknTEIENTKLVSEIQtlKNLDGNKEsmithfkEEISKLQSCLA 330
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALK------------TELEDTLDTTAAQ--QELRSKRE-------QEVTELKKALE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 331 DKENLYRALLLTTSNKEDTLF--LKEQL---RKAEEQVQATRQELIFLTKELSDAVNVrdktmadLHTARLENERVKKQL 405
Cdd:pfam01576 338 EETRSHEAQLQEMRQKHTQALeeLTEQLeqaKRNKANLEKAKQALESENAELQAELRT-------LQQAKQDSEHKRKKL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 406 ADTLAELQLHAVKKDQEKTDTLE--HELRREVEDLKLRLQMAAdhyrekfKECQRLQKQINKLSDQAASTNSVFTKKmgS 483
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEklSKLQSELESVSSLLNEAE-------GKNIKLSKDVSSLESQLQDTQELLQEE--T 481
|
....*...
gi 1244518170 484 QQKVNDAS 491
Cdd:pfam01576 482 RQKLNLST 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-469 |
7.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 352 LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRD--KTMADLHTARLENERVKKQLADtlAELQLHAVKKDQektDTLEh 429
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAE--LEAELERLDASS---DDLA- 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1244518170 430 ELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQ 469
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
525-622 |
8.13e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 525 HVCEMTKEI-AEKIEKY-------NKCKQLLQDEKTKCNKYAEELAKME-LKWKEQVKIAENvklELAEVEDNYKvqlaE 595
Cdd:PRK05771 32 HIEDLKEELsNERLRKLrslltklSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEE---ELEKIEKEIK----E 104
|
90 100
....*....|....*....|....*..
gi 1244518170 596 KEKEINGLASYLENLSREKELTKSLED 622
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPWGN 131
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
177-661 |
8.68e-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: 39.95 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 177 QLREQVGRMERELSQEKGRCEQLQAEQKGLLEvsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLK 256
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 257 DKLRKAQHEREQLECQLQTEKD------------EKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISK 324
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRLLQTlhsqeihirdahEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 325 LQSCLADKENLYRALLLTTSNKEDTlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMAD---LHTARLENERV 401
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqqLQTKEQIHLQE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 402 KKQLADTLAELQLHAVKKDQEKTDTLEHELRR----EVEDLKLRLQMAADHYREKFK-------ECQRLQKQINKLSDQA 470
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidNPGPLTRRMQRGEQTYAQLETseedvyhQLTSERKQRASLKEQM 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 471 ASTNSVFTKkmgSQQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTKEIA--EKIEKYNKCKQLLQ 548
Cdd:TIGR00618 566 QEIQQSFSI---LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqDVRLHLQQCSQELA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518170 549 DEKTKCNKYAEELAKMELkwKEQVKIAENVKLELAEVEDNykvQLAEKEKEINGLASYLENLSREKELTKSLEDqkgrKL 628
Cdd:TIGR00618 643 LKLTALHALQLTLTQERV--REHALSIRVLPKELLASRQL---ALQKMQSEKEQLTYWKEMLAQCQTLLRELET----HI 713
|
490 500 510
....*....|....*....|....*....|...
gi 1244518170 629 EGQSPQQVSRCLNTCSEQNGLLPPLSSAQPVLQ 661
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| |
