|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
17-120 |
5.67e-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: 5.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 17 VIFQNVAKSYLPNAHLECHYTLTPYIHPHSKDWVGIFKVGWSTARDYYTFLWSpmPEHYVEGSTVNCVLAFQGYYLPNDD 96
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 1244518284 97 GEFYQFCYVTHKGEIRGASTPFQF 120
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
125-398 |
9.58e-23 |
|
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: 102.28 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 125 PVEELLTME-----DEGNSDMLVVTTKAGLL------------------ELKIEKTLKEKEELLKLIAVLEKETAQLREQ 181
Cdd:pfam07888 2 PLDELVTLEeeshgEEGGTDMLLVVPRAELLqnrleeclqeraellqaqEAANRQREKEKERYKRDREQWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 182 VGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRK 261
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 262 A-------QHEREQLECQL-QTEKDEKELYKE-------------------DTLF------------------LKEQLRK 296
Cdd:pfam07888 162 AgaqrkeeEAERKQLQAKLqQTEEELRSLSKEfqelrnslaqrdtqvlqlqDTITtltqklttahrkeaeneaLLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 297 AEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQ-------------LHAVKKDQEKTD 363
Cdd:pfam07888 242 LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegrarwaqeretlQQSAEADKDRIE 321
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1244518284 364 TLEHELRREVEDL--------KLRLQMAADhyrekfKECQRLQ 398
Cdd:pfam07888 322 KLSAELQRLEERLqeermereKLEVELGRE------KDCNRVQ 358
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-426 |
2.21e-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: 73.94 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKgllEVSQSLRVENEEFmkrySDATA 229
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS---RLEQQKQILRERL----ANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 230 KVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELykedtlfLKEQLRKAEEQVQATRQELI 309
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE-------LESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 310 FLTKELSDA-----VNVRDKTMADLHTARLENERvkKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAA 384
Cdd:TIGR02168 390 QLELQIASLnneieRLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1244518284 385 DHYREKFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVN 426
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-410 |
1.43e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 143 VTTKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEqkgLLEVSQSLRVENEefmk 222
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEE---- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 223 RYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQ 302
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 303 ATRQELIFLTKELSDAvnvrDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQM 382
Cdd:COG1196 390 EALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*...
gi 1244518284 383 AADhyREKFKECQRLQKQINKLSDQAAS 410
Cdd:COG1196 466 AEL--LEEAALLEAALAELLEELAEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-410 |
1.68e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIvsvthkaie 247
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI--------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 ketdlDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMA 327
Cdd:COG1196 305 -----ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 328 DLHTARLENERVKKQLADTLAEL-----QLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQIN 402
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLeeleeAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
....*...
gi 1244518284 403 KLSDQAAS 410
Cdd:COG1196 460 ALLELLAE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-548 |
4.06e-12 |
|
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: 70.09 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 233 QLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLT 312
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 313 KELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQlhAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFK 392
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK--ALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 393 ECQRLQKQINKLSDQAASTNSVftkkmgsqqkVNDASINTDPAASTSASAVDVKPAASCAEtgfdMSTKDHVCEMTKEIA 472
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAE----------IEELEELIEELESELEALLNERASLEEAL----ALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 473 EKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKE-QVKIAENVKLELAEVEDNYKV---QLAEKEKEINGLASYLENL 548
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKiedDEEEARRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-409 |
4.53e-12 |
|
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: 68.25 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTE 276
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 277 KDEkelykedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAV----------NVRDKTMADLHTARLENERVKKQLADT 346
Cdd:COG4942 103 KEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1244518284 347 LAELQ--LHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAA 409
Cdd:COG4942 173 RAELEalLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-393 |
2.54e-11 |
|
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: 67.39 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATA 229
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 230 KVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELI 309
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 310 FLTKELSDAVNVRDKTMADLHTARLENErvkkQLADTLAELQLHAVKKDQEKtdtleHELRREVEDLKLRLQ---MAADH 386
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELE----ELSEELRELESKRSELRREL-----EELREKLAQLELRLEgleVRIDN 940
|
....*..
gi 1244518284 387 YREKFKE 393
Cdd:TIGR02168 941 LQERLSE 947
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
691-717 |
3.36e-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: 58.04 E-value: 3.36e-11
10 20
....*....|....*....|....*..
gi 1244518284 691 KKCPLCELMFPPNYDQTKFEEHVESHW 717
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
718-744 |
6.16e-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: 57.57 E-value: 6.16e-11
10 20
....*....|....*....|....*..
gi 1244518284 718 KVCPMCSEQFPPDYDQQGFERHVQTHF 744
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 ... |
693-716 |
2.28e-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: 55.89 E-value: 2.28e-10
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-385 |
4.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL 206
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 207 LEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKED 286
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 287 TLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQlhAVKKDQEKTDTLE 366
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--ELLEEAALLEAAL 479
|
250
....*....|....*....
gi 1244518284 367 HELRREVEDLKLRLQMAAD 385
Cdd:COG1196 480 AELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-410 |
4.62e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMK-------RYSDATAKVQQLEEDIVSVTH 243
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieeleeRLEEAEEELAEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 KAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRD 323
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 324 KTMADLhtARLENERVKkqladtlAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHyREKFK-ECQRLQKQIN 402
Cdd:TIGR02168 870 ELESEL--EALLNERAS-------LEEALALLRSELEELSEELRELESKRSELRRELEELREK-LAQLElRLEGLEVRID 939
|
....*...
gi 1244518284 403 KLSDQAAS 410
Cdd:TIGR02168 940 NLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-408 |
7.25e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEfmkrysdATAKVQQLEEDIVSVTHKAIE 247
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-------LEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELykedtlfLKEQLRKAEEQVQATRQelifltkELSDAVNVRDKTMA 327
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-------LREALDELRAELTLLNE-------EAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 328 DLHTARLENERVKKQLADTLAELQlhAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQ 407
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIE--SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
.
gi 1244518284 408 A 408
Cdd:TIGR02168 910 R 910
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-567 |
1.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMErELSQEKGRCEQLQAEQKGLLEVSQ-------SLRVENEEFMKRYSDATAKVQQLEEdivs 240
Cdd:PRK03918 268 IEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELReiekrlsRLEEEINGIEERIKELEEKEERLEE---- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 241 VTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVN 320
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 321 VRDKTMADLHTAR---------LENERVKKQLADTLAELQlhAVKKDQEKTDTLEHELRREVEDLK---------LRLQM 382
Cdd:PRK03918 423 ELKKAIEELKKAKgkcpvcgreLTEEHRKELLEEYTAELK--RIEKELKEIEEKERKLRKELRELEkvlkkeselIKLKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 383 AADHYRE---------------KFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDvkp 447
Cdd:PRK03918 501 LAEQLKEleeklkkynleelekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK--- 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 448 aaSCAETGFdmSTKDHVCEMTKEIAEKIEKYNKCK---QLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVE 524
Cdd:PRK03918 578 --ELEELGF--ESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1244518284 525 DNYKVQ--------LAEKEKEINGLASYLENL-SREKELTKSLEDQKGRKLE 567
Cdd:PRK03918 654 KKYSEEeyeelreeYLELSRELAGLRAELEELeKRREEIKKTLEKLKEELEE 705
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-561 |
2.44e-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: 60.89 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 175 TAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLE------EDIVSVTHKAIEK 248
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEattcslEELLRTEQQRLEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 249 ETD-LDSLKDKLRKAQHEREQLECQLQTEKDEKELYK------EDTLFLKEQLRKAEEQVQATRQELIFLtkelsdaVNV 321
Cdd:pfam05483 375 NEDqLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaedEKLLDEKKQFEKIAEELKGKEQELIFL-------LQA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 322 RDKTMADLH----TARLENERVKKQLADTLAELQLHAVKKDQEKTDT----LEH-ELRREVEDLKLRLQMAADHYREKFK 392
Cdd:pfam05483 448 REKEIHDLEiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCdkllLENkELTQEASDMTLELKKHQEDIINCKK 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 393 ECQRLQKQINKLSDQAAS-TNSVFTKKMGSQQKVNDASINTDPAASTSASAvdvkpAASCAETGFDMSTKDHVCEMTKei 471
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENARSI-----EYEVLKKEKQMKILENKCNNLK-- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 472 aEKIEKYNKCKQLLQDE----KTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYkvqlaEKEKEINGLASylEN 547
Cdd:pfam05483 601 -KQIENKNKNIEELHQEnkalKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY-----QKEIEDKKISE--EK 672
|
410
....*....|....
gi 1244518284 548 LSREKELTKSLEDQ 561
Cdd:pfam05483 673 LLEEVEKAKAIADE 686
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-546 |
2.95e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAiekeT 250
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----D 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKaqhEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQ---------ATRQELifLTKELSDAVNV 321
Cdd:PRK02224 353 DLEERAEELRE---EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlgnaEDFLEE--LREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 322 RDKTMADLHTARlenERVKKqladtlAELQLHAVK--------KDQEKTDTLEH------ELRREVEDLKLRlQMAADHY 387
Cdd:PRK02224 428 EAELEATLRTAR---ERVEE------AEALLEAGKcpecgqpvEGSPHVETIEEdrerveELEAELEDLEEE-VEEVEER 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 388 REKFKECQRLQKQINKLSDQA-ASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAEtgfdmstkdhvcE 466
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERReDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE------------E 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 467 MTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKlELAEVEDNYKVQLAEKEKEINGLASYLE 546
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE-ALAELNDERRERLAEKRERKRELEAEFD 644
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-386 |
4.40e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQL---REQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1196 297 LARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDklRKAQHEREQLECQLQTEKDEKELykEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMA 327
Cdd:COG1196 377 AEEELEELAE--ELLEALRAAAELAAQLEELEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1244518284 328 DLhtaRLENERVKKQLADTLAELQLHavkkdQEKTDTLEHELRREVEDLKLRLQMAADH 386
Cdd:COG1196 453 EL---EEEEEALLELLAELLEEAALL-----EAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-409 |
6.58e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQ----QLEEDIVSVTHKAI 246
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekigELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 247 EKETDLDSLKDKLRKAQHER-------EQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQ-------ATRQELIFLT 312
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIdkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkefaETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 313 KELSDAVN-------VRDKTMADLHTARLENERVKKQLADTLAEL-QLHAVKKD-QEKTDTLEHELRREVEDLKlrlqMA 383
Cdd:TIGR02169 392 EKLEKLKReinelkrELDRLQEELQRLSEELADLNAAIAGIEAKInELEEEKEDkALEIKKQEWKLEQLAADLS----KY 467
|
250 260
....*....|....*....|....*.
gi 1244518284 384 ADHYREKFKECQRLQKQINKLSDQAA 409
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-375 |
9.20e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 176 AQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVeneefMKRYSDATAKVQQLEEDIVsvthkAIEKE-TDLDS 254
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIA-----ELEAElERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 255 LKDKLRKAQHEREQLECQLQTEKDEKELykedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARL 334
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDE-------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1244518284 335 ENERVKKQLADTLAELQlHAVKKDQEKTDTLEHELRREVED 375
Cdd:COG4913 756 AAALGDAVERELRENLE-ERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-567 |
1.09e-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: 58.93 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 229 AKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLE--CQLQTEKDEKELY-----KEDtlfLKEQLRKAEEQV 301
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEGYellkeKEA---LERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 302 QATRQELIFLTKELSDavnvRDKTMADLHTARLE-NERVKKQLADTLAELQ--LHAVKKDQEKTDTLEHELRREVEDLKL 378
Cdd:TIGR02169 247 ASLEEELEKLTEEISE----LEKRLEEIEQLLEElNKKIKDLGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 379 RLQMAADHYREKFKECQRLQKQINKLSDQAASTNSVFTKKmgsqQKVNDASINtdpaastSASAVDVKPAASCAEtgfdm 458
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL----KEELEDLRA-------ELEEVDKEFAETRDE----- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 459 stkdhvcemTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQLAEKEKEI 538
Cdd:TIGR02169 387 ---------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340
....*....|....*....|....*....
gi 1244518284 539 NGLASYLENLSREKELTKSLEDQKGRKLE 567
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
718-744 |
1.37e-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: 50.72 E-value: 1.37e-08
10 20
....*....|....*....|....*..
gi 1244518284 718 KVCPMCSEQFPPDYDQQGFERHVQTHF 744
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-569 |
1.38e-08 |
|
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: 58.59 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 182 VGRMERELSQE----KGRCEQLQAEQKGLLEVSQSlrvENEEFMKRYSDataKVQQL----EEDIVSVTHKAIEKETDLD 253
Cdd:pfam15921 222 ISKILRELDTEisylKGRIFPVEDQLEALKSESQN---KIELLLQQHQD---RIEQLisehEVEITGLTEKASSARSQAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 254 SLKDKLR----KAQHEREQLECQL-QTEKDEKELYKEdtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRD----- 323
Cdd:pfam15921 296 SIQSQLEiiqeQARNQNSMYMRQLsDLESTVSQLRSE----LREAKRMYEDKIEELEKQLVLANSELTEARTERDqfsqe 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 324 ---------KTMADLHTAR----LENERvKKQLADtlaelqlhavkKDQEKTDTLEHeLRREVEDLKLRLQMAADHYREK 390
Cdd:pfam15921 372 sgnlddqlqKLLADLHKREkelsLEKEQ-NKRLWD-----------RDTGNSITIDH-LRRELDDRNMEVQRLEALLKAM 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 391 FKECQ-RLQKQINKLSDQAASTNSV--FTKKMGSQQK-----VNDASINTDPAASTSASAVDVKPAASCAETGFDmSTKD 462
Cdd:pfam15921 439 KSECQgQMERQMAAIQGKNESLEKVssLTAQLESTKEmlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIE-ATNA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 463 HVCEMTKEIAEKIEKYnkckQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVED----------NYKVQLA 532
Cdd:pfam15921 518 EITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagAMQVEKA 593
|
410 420 430
....*....|....*....|....*....|....*..
gi 1244518284 533 EKEKEINGLASYLEnlsrEKELTKSLEDQKGRKLEGQ 569
Cdd:pfam15921 594 QLEKEINDRRLELQ----EFKILKDKKDAKIRELEAR 626
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-406 |
4.36e-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: 57.00 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSqekgRCEQLQAEQKGLL-EVSQSLRVENeefmKRYSDATAKVQQLEEDIVSVTHKAIEKE 249
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELS----SLQSELRRIENRLdELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 250 TDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLrkAEEQVQATRQELIFLTKELSD---AVNVRDKTM 326
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRieaRLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 327 ADLHTAR--LENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKL 404
Cdd:TIGR02169 822 NRLTLEKeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
..
gi 1244518284 405 SD 406
Cdd:TIGR02169 902 ER 903
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-402 |
5.42e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 222 KRYSDATAKVQQLEEDIVSVTHKAIEKETDLdsLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAE-EQ 300
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 301 VQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAvkkdqEKTDTLEHELRREVEDLKLRL 380
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL-----EALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|..
gi 1244518284 381 QMAADHYREKFKECQRLQKQIN 402
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKS 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-524 |
5.53e-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: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 174 ETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVsQSLRVENEEFmkRYSDATAKVQQLEEDIVSVTHK--AIEKE-T 250
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAIERQlaSLEEElE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKAQHEREQLECQLQTEKdeKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLH 330
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI--KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 331 TARLENERVKKQLADtlaelqlhaVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLsdqaas 410
Cdd:TIGR02169 333 KLLAEIEELEREIEE---------ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL------ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 411 tnsvfTKKMGSQQKVNDASIntDPAASTSASAVDVKPAASCAE---TGFDMSTKDhvceMTKEIAEKIEKYNKCKQLLQD 487
Cdd:TIGR02169 398 -----KREINELKRELDRLQ--EELQRLSEELADLNAAIAGIEakiNELEEEKED----KALEIKKQEWKLEQLAADLSK 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 1244518284 488 EKTKCNKYAEELAKMElkwKEQvkiaENVKLELAEVE 524
Cdd:TIGR02169 467 YEQELYDLKEEYDRVE---KEL----SKLQRELAEAE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-553 |
6.45e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQkgllEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKELYK---EDTLFLKEQLRKAEEQVQAT-RQELIFLTKELSDAVNVRDKtmA 327
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGLDDadaEAVEARREELEDRDEELRDRlEECRVAAQAHNEEAESLRED--A 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 328 DLHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHE---LRREVEDLKLRLQMAADHYREKFKECQRLQKQINKL 404
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieeLRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 405 SdqaastnsvftkkmgsqqkvndASINTdpAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTkEIAEKIEKYNKCKQL 484
Cdd:PRK02224 432 E----------------------ATLRT--ARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEAELED 486
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1244518284 485 LQDEKTKCNK---YAEELAKMElkwKEQVKIAENVKLeLAEVEDNYKVQLAEKEKEINGL---ASYLENLSREKE 553
Cdd:PRK02224 487 LEEEVEEVEErleRAEDLVEAE---DRIERLEERRED-LEELIAERRETIEEKRERAEELrerAAELEAEAEEKR 557
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
720-743 |
8.35e-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: 48.34 E-value: 8.35e-08
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
227-455 |
1.08e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 227 ATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELykedtlfLKEQLRKAEEQVQATRQ 306
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-------LQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 307 EL-------------------IFLTKELSDAVNvR-----------DKTMADLHTARLENERVKKQLADTLAELQ--LHA 354
Cdd:COG3883 87 ELgeraralyrsggsvsyldvLLGSESFSDFLD-RlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEalKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 355 VKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVNDASINTDP 434
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260
....*....|....*....|.
gi 1244518284 435 AASTSASAVDVKPAASCAETG 455
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAAG 266
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
693-716 |
1.35e-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: 47.95 E-value: 1.35e-07
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
720-743 |
2.01e-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: 47.41 E-value: 2.01e-07
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-346 |
2.64e-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: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 146 KAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYS 225
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 226 DATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQL----------------ECQLQTEKDEKELYKEDTLf 289
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysltleeaeALENKIEDDEEEARRRLKR- 976
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1244518284 290 LKEQLRK-------AEEQVQATRQELIFLTKELSDAVNVRDK---TMADLhtarleNERVKKQLADT 346
Cdd:TIGR02168 977 LENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETleeAIEEI------DREARERFKDT 1037
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-390 |
5.17e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRME---RELSQEKGRCEQLQAEQKGLLEVSQ---SLRVENEEFMKRYSDATAKVQQLEEDIVSVTH- 243
Cdd:PRK04863 892 LADRVEEIREQLDEAEeakRFVQQHGNALAQLEPIVSVLQSDPEqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHf 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 ------KAIEKETDL-DSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLT---- 312
Cdd:PRK04863 972 syedaaEMLAKNSDLnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpad 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 313 -KELSDAVNVRDKTMADLHTARLENERVKKQLadTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLR----LQMAADHY 387
Cdd:PRK04863 1052 sGAEERARARRDELHARLSANRSRRNQLEKQL--TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGwcavLRLVKDNG 1129
|
...
gi 1244518284 388 REK 390
Cdd:PRK04863 1130 VER 1132
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
171-349 |
5.97e-07 |
|
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: 51.08 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELsqekgrcEQLQAEQKGLLEvsqslRVENEEfmKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:COG1579 15 LDSELDRLEHRLKELPAEL-------AELEDELAALEA-----RLEAAK--TELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDklrkaQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLH 330
Cdd:COG1579 81 QLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*....
gi 1244518284 331 TARLENERVKKQLADTLAE 349
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
172-385 |
1.85e-06 |
|
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: 51.66 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 172 EKETAQLREQVGRMErELSQEKGRCEQLQAEQkglLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIV----SVTHKAIE 247
Cdd:pfam15921 614 DKKDAKIRELEARVS-DLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkrNFRNKSEE 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDKLRKAQHEREQ---------------------LECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQ 306
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKE 769
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1244518284 307 ELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQlHAVKKDQEKTDTLEhelRREVEDLKLRLQMAAD 385
Cdd:pfam15921 770 EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALD-KASLQFAECQDIIQ---RQEQESVRLKLQHTLD 844
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
222-393 |
1.86e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 222 KRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQV 301
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 302 QATRQELIFLTKELSDAVNVRDKTMA---DLHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKL 378
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAqiaELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170
....*....|....*
gi 1244518284 379 RLQMAADHYREKFKE 393
Cdd:COG4372 191 EANRNAEKEEELAEA 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-412 |
2.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTE 276
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 277 KDEKELYKedtlfLKEQLRKAEEQVQATRQELifltkelsdavnvrdktmADLHTARLENERVKKQLADTLAELQLHAVK 356
Cdd:COG4717 129 PLYQELEA-----LEAELAELPERLEELEERL------------------EELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 357 KDQEKTDTLEhELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTN 412
Cdd:COG4717 186 LSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-567 |
2.59e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIvsvthkaIEKET 250
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-------KELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKAQHEREQlecqlqtekdekELYKEdtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLH 330
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQ------------DWNKE----LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 331 TARLENERVKKQLADTLAELQLhaVKKD-QEKTDTLEhELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQaa 409
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEK--LKKEnQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE-- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 410 stnsvfTKKMGSQQKVNDASINtdpaastsasavdvkpaascaetgfdmstkdhvcEMTKEIAEKIEKYNKCKQLLQDEK 489
Cdd:TIGR04523 428 ------IERLKETIIKNNSEIK----------------------------------DLTNQDSVKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1244518284 490 TKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNyKVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLE 567
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-355 |
2.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQK--GLLEVSQSLRVENEEFMKRYSDATAKVQQLEedivsvthkaiEK 248
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR-----------EL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 249 ETDLDSLKDKLRKAQHEREQLECQLQTEKdekelykedtlflKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMAD 328
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLAT-------------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....*..
gi 1244518284 329 LhtARLENERVKKQLADTLAELQLHAV 355
Cdd:COG4717 229 L--EQLENELEAAALEERLKEARLLLL 253
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
176-377 |
3.91e-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: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 176 AQLREQVGRMER---ELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFmkrysdataKVQQLEEDIVSVTHKAIEKETD- 251
Cdd:pfam05622 197 GKLSEESKKADKlefEYKKLEEKLEALQKEKERLIIERDTLRETNEEL---------RCAQLQQAELSQADALLSPSSDp 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 252 LDSL---------KDKLRKAQHEREQLECQ-----------LQTEKDEKELYKEDtlfLKEQLRKAEEQVQATRQELIFL 311
Cdd:pfam05622 268 GDNLaaeimpaeiREKLIRLQHENKMLRLGqegsyrerlteLQQLLEDANRRKNE---LETQNRLANQRILELQQQVEEL 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 312 TKELS-------DAVNVRDKT---MADLHTARLENERVKKQLAdtlaELQLHAVKKDQEKTDTLEHELRREVEDLK 377
Cdd:pfam05622 345 QKALQeqgskaeDSSLLKQKLeehLEKLHEAQSELQKKKEQIE----ELEPKQDSNLAQKIDELQEALRKKDEDMK 416
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-425 |
4.73e-06 |
|
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: 50.12 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 178 LREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEediVSVTHKAIEKETDLDSLKD 257
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE---ARVSDLELEKVKLVNAGSE 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 258 KLRKA---QHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATrqelifltkelsdavnvRDKTMADLHTARL 334
Cdd:pfam15921 644 RLRAVkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT-----------------TNKLKMQLKSAQS 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 335 ENERVKKQLaDTLAELQLHAVK--KDQEKTDTLEhelRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSdQAASTN 412
Cdd:pfam15921 707 ELEQTRNTL-KSMEGSDGHAMKvaMGMQKQITAK---RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS-QELSTV 781
|
250
....*....|...
gi 1244518284 413 SVFTKKMGSQQKV 425
Cdd:pfam15921 782 ATEKNKMAGELEV 794
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
172-406 |
7.36e-06 |
|
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: 49.58 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFmkrySDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:pfam02463 204 EQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE----IESSKQEIEKEEEKLAQVLKENKEEEK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 252 LDSLKDKLRKA-QHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVR---DKTMA 327
Cdd:pfam02463 280 EKKLQEEELKLlAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKReaeEEEEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 328 DLHTARLENERVKKQLADTLAEL--QLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLS 405
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLEseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
.
gi 1244518284 406 D 406
Cdd:pfam02463 440 E 440
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
174-425 |
7.49e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 174 ETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFmkrySDATAKVQQLEEDIVSVTHKAIEKETDLD 253
Cdd:COG4372 46 ELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 254 SLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELS----DAVNVRDKTMADL 329
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAeqalDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 330 HTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHEL----RREVEDLKLRLQMAADHYREKFKECQRLQKQINKLS 405
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALldalELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260
....*....|....*....|
gi 1244518284 406 DQAASTNSVFTKKMGSQQKV 425
Cdd:COG4372 279 EIAALELEALEEAALELKLL 298
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-576 |
8.35e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 153 KIEKTLKEKEELLKLIAVLEKETAQLREQVGRMEREL--SQEKGRCEQL-QAEQKGLLEVSQSLRVEN---EEFMKRYSD 226
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkkAEEKKKADEAkKAEEKKKADEAKKKAEEAkkaDEAKKKAEE 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 227 ATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTlflkEQLRKAEEQVQATRQ 306
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA----EEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 307 ElifltKELSDAVNVRDKTMADLHTARLENERVKKqlADTLAELQLHAVKKDQEKTDTLEH----------ELRREVEDL 376
Cdd:PTZ00121 1403 D-----KKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAkkaeeakkkaEEAKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 377 KLRLQMA--ADHYREKFKECQRLQKQINKLSD---QAASTNSVFTKKMGSQQKVNDASINTDPA--ASTSASAVDVKPAA 449
Cdd:PTZ00121 1476 KKKAEEAkkADEAKKKAEEAKKKADEAKKAAEakkKADEAKKAEEAKKADEAKKAEEAKKADEAkkAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 450 SC--------AETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKyAEELAKME-LKWK-EQVKIAENVK-- 517
Cdd:PTZ00121 1556 ELkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK-AEEAKKAEeAKIKaEELKKAEEEKkk 1634
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518284 518 ---LELAEVEDNYKVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLEGQSPQQVSR 576
Cdd:PTZ00121 1635 veqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-386 |
1.44e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMA 327
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 328 DLHTAR-LENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADH 386
Cdd:COG1196 506 FLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
177-572 |
1.69e-05 |
|
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: 48.43 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 177 QLREQVGRMERELSQEKGRCEQLQAEQKGLLEvsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLK 256
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 257 DKLRKAQHER------EQLECQLQTEKDEKELYKEDTLFLKEQLRKA---EEQVQATRQELIFLTKELSDAVNVRDKTMA 327
Cdd:TIGR00618 328 MKRAAHVKQQssieeqRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtlTQHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 328 DLHTA--RLENERV-KKQLADTLAELQLhavkkDQEKTDTLEHELRREVEDLKLRlQMAADHYREKFKECQRLQKQINKL 404
Cdd:TIGR00618 408 EQATIdtRTSAFRDlQGQLAHAKKQQEL-----QQRYAELCAAAITCTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQI 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 405 SDQAASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASC---------AETGFDMSTKDHVC-EMTKEIAEK 474
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmqrgeqtyAQLETSEEDVYHQLtSERKQRASL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 475 IEKYNKCKQLLQDEKTKCNKYAEELAK-------------MELKWKEQVKIAENV-KLELAEVEDNYKVQLAEKE----- 535
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNlqnitvrlqdlteKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQcsqel 641
|
410 420 430
....*....|....*....|....*....|....*...
gi 1244518284 536 -KEINGLASYLENLSREKELTKSLEDQKGRKLEGQSPQ 572
Cdd:TIGR00618 642 aLKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
168-411 |
3.04e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDK---LRKAQHEREQLECQLQTE----KDEKELYKEDTLfLKEQLRKAEEQVQATRQeliflTKELSdavn 320
Cdd:COG1340 97 LRKELAELNKAggsIDKLRKEIERLEWRQQTEvlspEEEKELVEKIKE-LEKELEKAKKALEKNEK-----LKELR---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 321 vrdktmADLHTARLENERVKKQLAdTLAELQLHAVKKDQEKTDTLEhELRREVEDLK---LRLQMAADHYREKFKECQR- 396
Cdd:COG1340 167 ------AELKELRKEAEEIHKKIK-ELAEEAQELHEEMIELYKEAD-ELRKEADELHkeiVEAQEKADELHEEIIELQKe 238
|
250
....*....|....*...
gi 1244518284 397 ---LQKQINKLSDQAAST 411
Cdd:COG1340 239 lreLRKELKKLRKKQRAL 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-567 |
3.89e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLrvenEEFMKRYSDATAK-VQQLEEDIVSVTHKAIEKE 249
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL----EELLEQLSLATEEeLQDLAEELEELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 250 TDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLkeqlrkaeeqVQATRQELIFLTKELSDAVNVRDKTMAD- 328
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL----------IAAALLALLGLGGSLLSLILTIAGVLFLv 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 329 ---LHTARLENERVKKQLADTLAELQLHAVKKDQEktdtlEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLS 405
Cdd:COG4717 283 lglLALLFLLLAREKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 406 DQAAStnsvftkkmgSQQKVNDASINtdpaastsasavdvkpaASCAETGFDMSTK-DHVCEMTKEIAEKIEKYNKCKQL 484
Cdd:COG4717 358 ELEEE----------LQLEELEQEIA-----------------ALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 485 LQDEKTKCNKYAEELAKMELKWKeqvkiAENVKLELAEVEDnykvQLAEKEKEINGLASYLENLSREKELTKsLEDQKGR 564
Cdd:COG4717 411 LEELLGELEELLEALDEEELEEE-----LEELEEELEELEE----ELEELREELAELEAELEQLEEDGELAE-LLQELEE 480
|
...
gi 1244518284 565 KLE 567
Cdd:COG4717 481 LKA 483
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
168-442 |
4.23e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKgrceqlqaEQKGLLEVSQslrveneefmkrysDATAKVQQLEedivsvthkaiE 247
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFR--------QKNGLVDLSE--------------EAKLLLQQLS-----------E 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLF--LKEQLRKAEEQVQATRQElifLTKELSDAVNVRDKt 325
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqLRAQLAELEAELAELSAR---YTPNHPDVIALRAQ- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 326 MADLhtarleNERVKKQLADTLAELQlhavkKDQEKTDTLEHELRREVEDLKLRLQMAAdhyrekfkecqRLQKQINKLS 405
Cdd:COG3206 300 IAAL------RAQLQQEAQRILASLE-----AELEALQAREASLQAQLAQLEARLAELP-----------ELEAELRRLE 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1244518284 406 DQAASTNSVFTK--------KMGSQQKVNDASINTDPAASTSASA 442
Cdd:COG3206 358 REVEVARELYESllqrleeaRLAEALTVGNVRVIDPAVVPLKPVS 402
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
233-553 |
4.71e-05 |
|
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: 46.96 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 233 QLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLT 312
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 313 KELsDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFK 392
Cdd:TIGR00606 772 TLL-GTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 393 ECQRLQKQINKLSdqaASTNSVFTKKMgsqqkvndaSINTDPAASTSASAVDVKPAASCAETGFDMSTKDhvcEMTKEIA 472
Cdd:TIGR00606 851 LIQDQQEQIQHLK---SKTNELKSEKL---------QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAK---EQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 473 EKIEKYNKCKQLLQDEKTKCNKYAE-ELAKMELKWKEQVKIAENVKLELAEVEDNYKVQlaeKEKEINGLASYLENLSRE 551
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ---KETELNTVNAQLEECEKH 992
|
..
gi 1244518284 552 KE 553
Cdd:TIGR00606 993 QE 994
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
253-407 |
6.01e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 253 DSLKDKLRKAQHEREQLECQLQTekdekelykedtlfLKEQLRKAEEQVQATRQE--LIFLTKELSDAVNVRDKTMADLH 330
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPE--------------LRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1244518284 331 TARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQ 407
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
171-403 |
6.33e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRME---RELSQE-KGRCEQLQAEQKGLLEvsQSLRVENEEFMKRYSDATAKVQQLEEDIvsvthkai 246
Cdd:pfam06160 184 LEEETDALEELMEDIPplyEELKTElPDQLEELKEGYREMEE--EGYALEHLNVDKEIQQLEEQLEENLALL-------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 247 eKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTK--ELS--DAVNVR 322
Cdd:pfam06160 254 -ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsyTLNenELERVR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 323 D--------KTMADLHTARLENERVK-KQLADTLAEL--QLHAVKKDQ----EKTDTLE-----------------HELR 370
Cdd:pfam06160 333 GlekqleelEKRYDEIVERLEEKEVAySELQEELEEIleQLEEIEEEQeefkESLQSLRkdelearekldefklelREIK 412
|
250 260 270
....*....|....*....|....*....|....*..
gi 1244518284 371 REVEdlKLRLQMAADHYREKFK----ECQRLQKQINK 403
Cdd:pfam06160 413 RLVE--KSNLPGLPESYLDYFFdvsdEIEDLADELNE 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-424 |
6.34e-05 |
|
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: 45.91 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLh 330
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 331 tarlenERVKKQLADTLAELQL---------------------------HAVKKDQEKTDTLEHELrREVEDLKLRLQMA 383
Cdd:COG4942 100 ------EAQKEELAELLRALYRlgrqpplalllspedfldavrrlqylkYLAPARREQAEELRADL-AELAALRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1244518284 384 ADHYREKFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQK 424
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
174-562 |
6.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 174 ETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEefmkRYSDATAKVQQLEEDIVSVTHKAIEKETDLD 253
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA----KKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 254 SLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQAtrQELIFLTKELSDAVNVRDKT-----MAD 328
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAeeakkKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 329 LHTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLE---HELRREVEDLKLRLQ--MAADHYREKFKECQRLQKQINK 403
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKK 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 404 LSDQAASTNSVfTKKMGSQQKVNDASintdPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQ 483
Cdd:PTZ00121 1413 AAAAKKKADEA-KKKAEEKKKADEAK----KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 484 lLQDEKTKCNKYAEELAKMELKWK--EQVKIAENVKL--ELAEVEDNYKVQLAEKEKEINGlasyLENLSREKELTKSLE 559
Cdd:PTZ00121 1488 -AKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKK----ADELKKAEELKKAEE 1562
|
...
gi 1244518284 560 DQK 562
Cdd:PTZ00121 1563 KKK 1565
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
180-562 |
7.55e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 180 EQVGRMERELSQEKGRCEQLQAEqkgllevSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKL 259
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAH-------CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKE 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 260 RKAQHEREQLECQLQTEKDEkelykedtlfLKEQLRKAEEQVQAtrqelifltkelsdavnvrdktmadlhtarLENERV 339
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDE----------VKCKLDKSEENARS------------------------------IEYEVL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 340 KKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAAdhyrekfKECQRLQKQINKLSDQAASTNSVFTKKM 419
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN-------KQLNAYEIKVNKLELELASAKQKFEEII 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 420 GSQQK-VNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTKEIAEKIEKYNKckqLLQDEKTKCNKY-AE 497
Cdd:pfam05483 657 DNYQKeIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDK---IIEERDSELGLYkNK 733
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 498 ELAKMELKWKEQVKIAeNVKLELAEVEDNYKVQLAEKEKeinglasylenLSRE-KELTKSLEDQK 562
Cdd:pfam05483 734 EQEQSSAKAALEIELS-NIKAELLSLKKQLEIEKEEKEK-----------LKMEaKENTAILKDKK 787
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
249-390 |
8.47e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.49 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 249 ETDLDSLKDKLRKAQHEREQLEC---QLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKT 325
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAeldRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1244518284 326 MADLHTARLENERVKKQLAD---TLAELQLHAVKKDQEKTDTLEhELRREVEDLKLRLQmAADHYREK 390
Cdd:pfam00529 137 GISRESLVTAGALVAQAQANllaTVAQLDQIYVQITQSAAENQA-EVRSELSGAQLQIA-EAEAELKL 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-308 |
8.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 145 TKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKG-RCEQLQAEQKGLlevsqslrveneefMKR 223
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERL--------------ERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 224 YSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEkelykedtlfLKEQLRKAEEQVQA 303
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE----------AEAALRDLRRELRE 423
|
....*
gi 1244518284 304 TRQEL 308
Cdd:COG4913 424 LEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-572 |
9.43e-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: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 285 EDTLF-LKEQLRKAEEQVQATrQELIFLTKELSDA---VNVRDKTmaDLHTARLENERVKKQLADTLAELQLHAVKKdQE 360
Cdd:TIGR02168 192 EDILNeLERQLKSLERQAEKA-ERYKELKAELRELelaLLVLRLE--ELREELEELQEELKEAEEELEELTAELQEL-EE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 361 KTDTLE---HELRREVEDLKLRLQMAAdhyrekfKECQRLQKQINKLSDQAAstNSVFTKKMGSQQKVNDAsintdpaas 437
Cdd:TIGR02168 268 KLEELRlevSELEEEIEELQKELYALA-------NEISRLEQQKQILRERLA--NLERQLEELEAQLEELE--------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 438 tsasavdvkpaascaetgfdmSTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTkcnKYAEELAKMELKWKEQVKIAENVK 517
Cdd:TIGR02168 330 ---------------------SKLDELAEELAELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1244518284 518 LELAEVEDNYKV---QLAEKEKEINGLASYLENLSREKE-LTKSLEDQKGRKLEGQSPQ 572
Cdd:TIGR02168 386 SKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEE 444
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
169-553 |
1.09e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 169 AVLEKETAQLREQVGRMERELSQEKGRCEQLQ----AEQKGLLEVsqsLRVENEEFMKRYSDATAKVQQLEEDIV-SVTH 243
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELElqlfPQAGTLLHF---LRKEAPDWEQSIGKVISPELLHRTDLDpEVWD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 KAIEKETDLDSLKDKLRKAQH-EREQLECQLQTEKDEkelYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAvnVR 322
Cdd:pfam12128 572 GSVGGELNLYGVKLDLKRIDVpEWAASEEELRERLDK---AEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RT 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 323 DKTMADLHTARLENErvKKQLADTLAELQLHAVKKDQEKTDTLEHELRRevedLKLRLQMAADHYREKFKEcQRLQKQ-- 400
Cdd:pfam12128 647 ALKNARLDLRRLFDE--KQSEKDKKNKALAERKDSANERLNSLEAQLKQ----LDKKHQAWLEEQKEQKRE-ARTEKQay 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 401 ----INKLSDQAASTNSVFTKKMgSQQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTK-EIAE-- 473
Cdd:pfam12128 720 wqvvEGALDAQLALLKAAIAARR-SGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRqEVLRyf 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 474 --KIEKYNKCKQLLQDEKTKCNKYAEELaKMELKwkeqvKIAENVKLELAEVEDNYKV---QLAEKEKEINGLASYLENL 548
Cdd:pfam12128 799 dwYQETWLQRRPRLATQLSNIERAISEL-QQQLA-----RLIADTKLRRAKLEMERKAsekQQVRLSENLRGLRCEMSKL 872
|
....*
gi 1244518284 549 SREKE 553
Cdd:pfam12128 873 ATLKE 877
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
169-396 |
1.11e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 169 AVLEKETAQLREQVGR--------MERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVS 240
Cdd:pfam00038 28 KLLETKISELRQKKGAepsrlyslYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 241 ---VTHKA----IEKETDLDSLKDKL--RKAQHERE--QLECQLQTEKDEKEL----YKEDTLFLKEQLRKAEEQVQATR 305
Cdd:pfam00038 108 lrkDLDEAtlarVDLEAKIESLKEELafLKKNHEEEvrELQAQVSDTQVNVEMdaarKLDLTSALAEIRAQYEEIAAKNR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 306 QEL--IFLTK--ELSDAVNVRDktmADLHTARLENERVKKQLADTLAELQlhAVKKdqeKTDTLEHELrREVEDlklRLQ 381
Cdd:pfam00038 188 EEAeeWYQSKleELQQAAARNG---DALRSAKEEITELRRTIQSLEIELQ--SLKK---QKASLERQL-AETEE---RYE 255
|
250
....*....|....*
gi 1244518284 382 MAADHYREKFKECQR 396
Cdd:pfam00038 256 LQLADYQELISELEA 270
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-536 |
1.17e-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: 45.55 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 169 AVLEKETAQLREQVgrmeRELSQEKGRCEQLQAEQKGLLevsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKaiek 248
Cdd:pfam01576 380 QALESENAELQAEL----RTLQQAKQDSEHKRKKLEGQL---QELQARLSESERQRAELAEKLSKLQSELESVSSL---- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 249 etdLDSLKDKLRKAQHEREQLECQLQtekDEKELYKEDT---LFLKEQLRKAEEQVQATRQELifltKELSDAvnvrdkt 325
Cdd:pfam01576 449 ---LNEAEGKNIKLSKDVSSLESQLQ---DTQELLQEETrqkLNLSTRLRQLEDERNSLQEQL----EEEEEA------- 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 326 madlhtarleNERVKKQLADTLAELQlHAVKKDQEKTDTLE------HELRREVEDLKLRLQMAADHYREKFKECQRLQK 399
Cdd:pfam01576 512 ----------KRNVERQLSTLQAQLS-DMKKKLEEDAGTLEaleegkKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 400 QINKLS---DQAASTNSVFTKKmgsqQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTKEIAEKIE 476
Cdd:pfam01576 581 ELDDLLvdlDHQRQLVSNLEKK----QKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELE 656
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1244518284 477 KYNKCKQLLQDE----KTKCNKYAEELAKMELKWKEQVkiaENVKLELAEVEDnyKVQLAEKEK 536
Cdd:pfam01576 657 RTNKQLRAEMEDlvssKDDVGKNVHELERSKRALEQQV---EEMKTQLEELED--ELQATEDAK 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-351 |
1.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEkgRCEQLQAEQKGLLEvsqslrvENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG4913 271 LAELEYLRAALRLWFAQRRLELLEA--ELEELRAELARLEA-------ELERLEARLDALREELDELEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 K-ETDLDSLKDKLRKAQHEREQLECQLQTekdekelykedtlfLKEQLRKAEEQVQATRQElifLTKELSDAVNVRDKTM 326
Cdd:COG4913 342 QlEREIERLERELEERERRRARLEALLAA--------------LGLPLPASAEEFAALRAE---AAALLEALEEELEALE 404
|
170 180
....*....|....*....|....*
gi 1244518284 327 ADLHTARLENERVKKQLADTLAELQ 351
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIA 429
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
718-745 |
1.44e-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: 39.43 E-value: 1.44e-04
10 20
....*....|....*....|....*...
gi 1244518284 718 KVCPMCSEQFPPDYDQQGFERHVQTHFD 745
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
177-309 |
1.45e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 177 QLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRveneefmkrySDATAKVQQLEE------DI-VSVTHKAIEK- 248
Cdd:COG3096 988 KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLK----------SSRDAKQQTLQEleqeleELgVQADAEAEERa 1057
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518284 249 ETDLDSLKDKLRKAQHEREQLECQLQ-TEKDEKELYKEdtlflkeqLRKAEEQVQATRQELI 309
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTrCEAEMDSLQKR--------LRKAERDYKQEREQVV 1111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-568 |
1.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 218 EEFMKRYSDATAKVQQLEEDivsvthkaieKETDLDSLKD----KLRKAQHER-EQLECQLQTEKDEKELYKEDTLFLKE 292
Cdd:PRK02224 165 EEYRERASDARLGVERVLSD----------QRGSLDQLKAqieeKEEKDLHERlNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 293 QLRKAEEQVQA---TRQELIFLTKELSD-------AVNVRDKTMADLHTARLENERVKKQLADTLAELQL-----HAVKK 357
Cdd:PRK02224 235 TRDEADEVLEEheeRREELETLEAEIEDlretiaeTEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 358 DQEKTDTLEHELRREVEDLKLRLQMA---ADHYREKFK----ECQRLQKQINKLSDQAASTNSVFTKKMGSQ-------- 422
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHneeAESLREDADdleeRAEELREEAAELESELEEAREAVEDRREEIeeleeeie 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 423 ---QKVNDASINTDPAASTSASAVDVKPAA--SCAETGFDMSTKDHVCEMTKEIAEKiEKYNKCKQLLQDEKTKC--NKY 495
Cdd:PRK02224 395 elrERFGDAPVDLGNAEDFLEELREERDELreREAELEATLRTARERVEEAEALLEA-GKCPECGQPVEGSPHVEtiEED 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1244518284 496 AEELAKMELKwkeqvkiAENVKLELAEVED--NYKVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLEG 568
Cdd:PRK02224 474 RERVEELEAE-------LEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
172-408 |
1.62e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLR--------VENEEFMKRYSDATAKVQQLEEDIVSVTH 243
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 --KAIEKetdLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEdTLF------------------------------LK 291
Cdd:COG3096 915 hgKALAQ---LEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQ-QIFalsevvqrrphfsyedavgllgensdlnekLR 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 292 EQLRKAEEQVQATRQELIFLTKELSDAVNVrdktMADLHTARLENERVKKQLADTLAELQLH----AVKKDQEKTDTLEH 367
Cdd:COG3096 991 ARLEQAEEARREAREQLRQAQAQYSQYNQV----LASLKSSRDAKQQTLQELEQELEELGVQadaeAEERARIRRDELHE 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1244518284 368 EL------RREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQA 408
Cdd:COG3096 1067 ELsqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-393 |
1.89e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDI---------VSV 241
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleaalrdLES 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 242 THKAIEKEtdLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATrQELIFLTKELSDAVNV 321
Cdd:TIGR02169 883 RLGDLKKE--RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEIPEEELSLEDVQAE 959
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518284 322 RDKTMADLHTARLENERVKKQLADTLAELqlhavKKDQEKTDTLEhelrREVEDLKLRLQMAADHYREKFKE 393
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRL-----DELKEKRAKLE----EERKAILERIEEYEKKKREVFME 1022
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
718-744 |
2.84e-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: 38.63 E-value: 2.84e-04
10 20
....*....|....*....|....*..
gi 1244518284 718 KVCPMCSEQFPPDYDQQGFERHVQTHF 744
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
171-404 |
2.92e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQ----KGLLEVSQSLRVENEEFM--KRYSDATAKVQQLEEDIV----- 239
Cdd:PRK10246 424 LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQtqrnAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAqlqag 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 240 -------SVTHKAIEKETDLdslkdKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLT 312
Cdd:PRK10246 504 qpcplcgSTSHPAVEAYQAL-----EPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALT 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 313 KE---LSDAVNVRDKTMADLH---TARLENERVKKQLADTLA-----ELQLHAVKKDQEKTDTLEHELRREVEDLKLRL- 380
Cdd:PRK10246 579 QQwqaVCASLNITLQPQDDIQpwlDAQEEHERQLRLLSQRHElqgqiAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLp 658
|
250 260 270
....*....|....*....|....*....|....*.
gi 1244518284 381 ------------QMAADHYREKFKECQRLQKQINKL 404
Cdd:PRK10246 659 qedeeaswlatrQQEAQSWQQRQNELTALQNRIQQL 694
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-381 |
3.20e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFmkrySDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKAQHEREQLECQLQTekdekelykedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRdktmadlh 330
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAE--------------LQSEIAEREEELKELEEQLESLQEELAALEQEL-------- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1244518284 331 tARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQ 381
Cdd:COG4372 174 -QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
168-309 |
3.40e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEvsQSLRVENEefmKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE--QLGNVRNN---KEYEALQKEIESLKRRISDLEDEILE 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518284 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDtlflkeqLRKAEEQVQATRQELI 309
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAE-------LEAELEELEAEREELA 169
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
174-307 |
5.47e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 174 ETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLD 253
Cdd:pfam15905 199 KVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1244518284 254 SLKDKLRKAQHEREQLECQlqtEKDEKELYKEDTLFLKEQLRKAEEQVQATRQE 307
Cdd:pfam15905 279 DLNEKCKLLESEKEELLRE---YEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
187-410 |
6.84e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 187 RELSQEKGRC--------EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDK 258
Cdd:PHA02562 177 RELNQQIQTLdmkidhiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 259 LRKAQHEREQLECQLQTEKDEKELYKEDTL--FLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKtmadlhtarlEN 336
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE----------LE 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 337 ERVkkqlaDTLAELQ--LHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAS 410
Cdd:PHA02562 327 EIM-----DEFNEQSkkLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-567 |
8.01e-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: 42.70 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 235 EEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKE 314
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 315 LSDavnvRDKTMADLHTarlENERVKKQLADTlaELQLHAVKKD----QEKTDTLEHELRRevedLKLRLqMAADHYREK 390
Cdd:TIGR04523 147 IKK----KEKELEKLNN---KYNDLKKQKEEL--ENELNLLEKEklniQKNIDKIKNKLLK----LELLL-SNLKKKIQK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 391 FKEcqrLQKQINKLSDQAAS-TNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKpaascaetgfdmstkdhvcemtK 469
Cdd:TIGR04523 213 NKS---LESQISELKKQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK----------------------K 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 470 EIAEKIEKYNKCKQLLQDEKTKCNKYAEELAkmELKWKEQVKIAENVKLELAEVED---NYKVQLAEKEKEINGLASYLE 546
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEIS--DLNNQKEQDWNKELKSELKNQEKkleEIQNQISQNNKIISQLNEQIS 345
|
330 340
....*....|....*....|.
gi 1244518284 547 NLSREKELTKSLEDQKGRKLE 567
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELE 366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
234-417 |
9.44e-04 |
|
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: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 234 LEE-DIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLEcqlqtekdekelykedtlflkeQLRKAEEQVQATRQELIFLT 312
Cdd:COG4913 218 LEEpDTFEAADALVEHFDDLERAHEALEDAREQIELLE----------------------PIRELAERYAAARERLAELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 313 KELSDAVNVRDKTMADLHTARLENERvkKQLADTLAELQLHAVKKDQ--EKTDTLEHELR----REVEDLKLRLQMAADH 386
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELR--AELARLEAELERLEARLDAlrEELDELEAQIRgnggDRLEQLEREIERLERE 353
|
170 180 190
....*....|....*....|....*....|.
gi 1244518284 387 YREKFKECQRLQKQINKLSDQAASTNSVFTK 417
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAA 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
201-377 |
9.55e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 201 AEQKGLLEVsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLqtEKDEK 280
Cdd:COG1579 4 EDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 281 EL-----YKEDTLFLKEqLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLhtarlenERVKKQLADTLAELQlhav 355
Cdd:COG1579 81 QLgnvrnNKEYEALQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAEL-------AELEAELEEKKAELD---- 148
|
170 180
....*....|....*....|..
gi 1244518284 356 kKDQEKTDTLEHELRREVEDLK 377
Cdd:COG1579 149 -EELAELEAELEELEAEREELA 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-564 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 332 ARLENERVKKQLADTLAELQlhAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAAST 411
Cdd:COG4942 25 AEAELEQLQQEIAELEKELA--ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 412 NSVFTKKMGSQQKVNDAS-----INTDPAASTSASAVDVKpaascaetgfdmSTKDHVCEMTKEIAEKIEKYNKCKQLLQ 486
Cdd:COG4942 103 KEELAELLRALYRLGRQPplallLSPEDFLDAVRRLQYLK------------YLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 487 DEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQLAEKEKEINGLASYLENLSRE------KELTKSLED 560
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEaaaaaeRTPAAGFAA 250
|
....
gi 1244518284 561 QKGR 564
Cdd:COG4942 251 LKGK 254
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-363 |
1.10e-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: 42.47 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 169 AVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSL--RVENEEfmkrysdatAKVQQLEEDIVSVTHKAI 246
Cdd:pfam01576 64 ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLeeQLDEEE---------AARQKLQLEKVTTEAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 247 EKETDLDSLKDKLRKAQHEREQLECQLQ------TEKDEK-------ELYKEDTLFLKEQLRKAEEQvqaTRQELIFLTK 313
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISeftsnlAEEEEKakslsklKNKHEAMISDLEERLKKEEK---GRQELEKAKR 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1244518284 314 ELSDAVNVRDKTMADLhtaRLENERVKKQLADTLAELQLHAVKKDQEKTD 363
Cdd:pfam01576 212 KLEGESTDLQEQIAEL---QAQIAELRAQLAKKEEELQAALARLEEETAQ 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-388 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 200 QAEQKGLLEVSQSLRVEN-EEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLE-CQLQTEK 277
Cdd:COG4717 303 EAEELQALPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAlLAEAGVE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 278 DEKELYKEDTLFlkEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKT--MADLHTARLENERVKKQLADTLAEL-QLHA 354
Cdd:COG4717 383 DEEELRAALEQA--EEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELaELEA 460
|
170 180 190
....*....|....*....|....*....|....
gi 1244518284 355 VKKDQEKTDTLEhELRREVEDLKLRLQMAADHYR 388
Cdd:COG4717 461 ELEQLEEDGELA-ELLQELEELKAELRELAEEWA 493
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-385 |
1.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEfmkrYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:COG4372 64 LEEELEQARSELEQLEEELEELN---EQLQAAQAELAQAQEELESLQEE----AEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKAQHEREQLECQLQTEKDE-KELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADL 329
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEElAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 330 HTARLENERVKKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAAD 385
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
718-745 |
1.25e-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: 36.66 E-value: 1.25e-03
10 20
....*....|....*....|....*...
gi 1244518284 718 KVCPMCSEQFPpDYDQQGFERHVQTHFD 745
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
244-553 |
1.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 KAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQA---TRQELIFLTKELSDAVN 320
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 321 VRD-KTMADLHTARLENERvkKQLADTLAELQLHAVKKDQEKTDTLEHELRREVEDlKLRLQMAADHYREKFKECQRLQK 399
Cdd:PTZ00121 1557 LKKaEEKKKAEEAKKAEED--KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 400 QINKLSDQAAStnsvfTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDhvcEMTKEIAEKIEKYN 479
Cdd:PTZ00121 1634 KVEQLKKKEAE-----EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA---EALKKEAEEAKKAE 1705
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 480 KCKQLLQDEKTKCN--KYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQLAEKEKEINGLAsylENLSREKE 553
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEelKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA---EEIRKEKE 1778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-351 |
1.63e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLlevSQSLRVENEEFMKRYSDATA 229
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 230 KVQQLEEDIVSVTHKAIEKETDLDSLKdklRKAQHEREQLEcQLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELI 309
Cdd:COG4942 116 LGRQPPLALLLSPEDFLDAVRRLQYLK---YLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1244518284 310 FLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQ 351
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
184-575 |
1.71e-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: 41.96 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 184 RMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDK---LR 260
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELdqeLR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 261 KAQHEREQLECQLQTE---KDEKELYKEDTLFLKEQLRKAEEQVQ-----ATRQELIFLTKELSDAVN-VRDKTM--ADL 329
Cdd:TIGR00606 482 KAERELSKAEKNSLTEtlkKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtTTRTQMEMLTKDKMDKDEqIRKIKSrhSDE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 330 HTARLENERVKKQLADTLaelqlHAVKKDQEKTdtlehelRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSD--- 406
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWL-----HSKSKEINQT-------RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklf 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 407 QAASTNSVFTKKMGSQQKVNDASINTDPAASTSAsAVDVKPAASCAETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQLLQ 486
Cdd:TIGR00606 630 DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATA-VYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAP 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 487 DEKTKCNKyaeELAKMELKWKEQvkiaenvkLELAEVEDNykvQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKL 566
Cdd:TIGR00606 709 DKLKSTES---ELKKKEKRRDEM--------LGLAPGRQS---IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL 774
|
....*....
gi 1244518284 567 EGQSPQQVS 575
Cdd:TIGR00606 775 GTIMPEEES 783
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
691-716 |
1.73e-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: 36.38 E-value: 1.73e-03
10 20
....*....|....*....|....*.
gi 1244518284 691 KKCPLCELMFPPNYDQTKFEEHVESH 716
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
277-553 |
2.02e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 277 KDEKELYKEDTLFLKEQLRKAEEQVQ---ATRQELIFLTKELSDAVN----VRDKTMADLHTARLENERVKKQLADTLAE 349
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKelaEKRDELNAQVKELREEAQelreKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 350 L-QLHAVKKDQEKTDTLEHELRREVEDLKLRLQ---MAADHYREKFKECQRLQKQINKLSDQAASTNSVftkkmgsqqkv 425
Cdd:COG1340 94 LdELRKELAELNKAGGSIDKLRKEIERLEWRQQtevLSPEEEKELVEKIKELEKELEKAKKALEKNEKL----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 426 ndasintdpaASTSASAVDVKPAAScaetgfdmstkdhvcEMTKEIAEKIEKYNKCKQLLQDEKTKcnkyAEEL-AKMEL 504
Cdd:COG1340 163 ----------KELRAELKELRKEAE---------------EIHKKIKELAEEAQELHEEMIELYKE----ADELrKEADE 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1244518284 505 KWKEQVKIAENVKlELAEVEDNYKVQLAEKEKEINGLASYLENLSREKE 553
Cdd:COG1340 214 LHKEIVEAQEKAD-ELHEEIIELQKELRELRKELKKLRKKQRALKREKE 261
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
691-717 |
2.83e-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: 2.83e-03
10 20
....*....|....*....|....*..
gi 1244518284 691 KKCPLCELMFPPNYDQTKFEEHVESHW 717
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
172-379 |
3.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLR--------VENEEFMKRYSDATAKVQQLEEDIVSVth 243
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlnlLADETLADRVEEIREQLDEAEEAKRFV-- 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 kaieketdldslkdklrkAQHER--EQLECQLQTEKDEKELYkedtlflkEQLRKAEEQVQATRQEL---IFLTKEL--- 315
Cdd:PRK04863 914 ------------------QQHGNalAQLEPIVSVLQSDPEQF--------EQLKQDYQQAQQTQRDAkqqAFALTEVvqr 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 316 ------SDAVNVRDKT-------MADLHTARLENERVKKQLADTLAEL-QLHAVKKD-----QEKTDTLEhELRREVEDL 376
Cdd:PRK04863 968 rahfsyEDAAEMLAKNsdlneklRQRLEQAEQERTRAREQLRQAQAQLaQYNQVLASlkssyDAKRQMLQ-ELKQELQDL 1046
|
...
gi 1244518284 377 KLR 379
Cdd:PRK04863 1047 GVP 1049
|
|
| DUF6236 |
pfam19749 |
Family of unknown function (DUF6236); This entry represents a member of a biosynthetic gene ... |
368-460 |
3.27e-03 |
|
Family of unknown function (DUF6236); This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0001432) is described by MIBiG as an example of the following biosynthetic classes, NRP (non-ribosomal peptide) and polyketide. It includes a member from the myxochromide D biosynthetic gene cluster from Stigmatella erecta.
Pssm-ID: 437581 Cd Length: 328 Bit Score: 40.34 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 368 ELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLsDQAASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKP 447
Cdd:pfam19749 206 ALRQELADIYLEIPEAGDPELKKDAEVERFESALEDL-DRAMKESGLSTKKGSLSAKFNLPDFTGLAGTVGGAGAGIAAG 284
|
90
....*....|...
gi 1244518284 448 AASCAETGFDMST 460
Cdd:pfam19749 285 ANSGAVFAGAAAA 297
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-539 |
3.45e-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: 40.77 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDKLRKAQHEREQLECQ---LQTEKDEKELYKEDtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDK 324
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRES---LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 325 tmadlhtarLENErvKKQLADTLAEL--QLHAVKKDQEKTDTLEHELRREVEDLKLRLQmaADHYREKF----KECQRLQ 398
Cdd:TIGR04523 501 ---------LNEE--KKELEEKVKDLtkKISSLKEKIEKLESEKKEKESKISDLEDELN--KDDFELKKenleKEIDEKN 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 399 KQINKLS-DQAASTNSVFTKKMGSQQKvndasintdpaastsasavdvkpaascaetgfdmstKDHVCEMTKEIAEKIEK 477
Cdd:TIGR04523 568 KEIEELKqTQKSLKKKQEEKQELIDQK------------------------------------EKEKKDLIKEIEEKEKK 611
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1244518284 478 YNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELaeveDNYKVQLAEKEKEIN 539
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI----KEIRNKWPEIIKKIK 669
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
218-351 |
3.48e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.63 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 218 EEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKA 297
Cdd:pfam00261 109 EEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEA 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1244518284 298 EEQVQATRQELIFLTKELsdavnvrDKTMADLHTARLENERVKKQLADTLAELQ 351
Cdd:pfam00261 189 ETRAEFAERSVQKLEKEV-------DRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-405 |
3.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQ-AEQkgLLEVSQSLRVENEEFMKR----YSDATAKVQQLEEDIVSVt 242
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKElAEQ--LKELEEKLKKYNLEELEKkaeeYEKLKEKLIKLKGEIKSL- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 243 HKAIEKETDLDS----LKDKLRKAQHEREQLECQL-----QTEKDEKELYKEDTLFLKE--QLRKAEEQVQATRQELIFL 311
Cdd:PRK03918 545 KKELEKLEELKKklaeLEKKLDELEEELAELLKELeelgfESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 312 TKELSDAVNVRDKTMADLhtarlenERVKKQLAdtlaELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYREKF 391
Cdd:PRK03918 625 EEELDKAFEELAETEKRL-------EELRKELE----ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
250
....*....|....
gi 1244518284 392 KECQRLQKQINKLS 405
Cdd:PRK03918 694 KTLEKLKEELEERE 707
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
173-410 |
3.80e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 173 KETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEE--FMKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:COG5185 260 EQNTDLRLEKLGENAESSKRL---NENANNLIKQFENTKEKIAEYTKsiDIKKATESLEEQLAAAEAEQELEESKRETET 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFlKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMAD-L 329
Cdd:COG5185 337 GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKS-SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 330 HTARLENERVKKQLADTLAELQlHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADH-YREKFKECQRLQKQINKLSDQA 408
Cdd:COG5185 416 KAADRQIEELQRQIEQATSSNE-EVSKLLNELISELNKVMREADEESQSRLEEAYDEiNRSVRSKKEDLNEELTQIESRV 494
|
..
gi 1244518284 409 AS 410
Cdd:COG5185 495 ST 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
171-573 |
4.06e-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: 40.54 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMEReLSQEKGRCEQ----LQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAI 246
Cdd:pfam01576 554 LEALTQQLEEKAAAYDK-LEKTKNRLQQelddLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAR 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 247 EKETDLDSLKDKLRKAQHEREQLE---CQLQTEKDEKELYKEDT----LFLKEQLRKAEEQVQATRQELIFLTKELSDAV 319
Cdd:pfam01576 633 EKETRALSLARALEEALEAKEELErtnKQLRAEMEDLVSSKDDVgknvHELERSKRALEQQVEEMKTQLEELEDELQATE 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 320 NVR---DKTMA--------DLHTARLENERVKKQLADTLAELQ--LHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADH 386
Cdd:pfam01576 713 DAKlrlEVNMQalkaqferDLQARDEQGEEKRRQLVKQVRELEaeLEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 387 YREKFKECQRLQKQ----INKLSDQAASTNSVFTKKMGSQQKvndasintdpAASTSASAVDVKPAASCAEtgfdmSTKD 462
Cdd:pfam01576 793 REEAVKQLKKLQAQmkdlQRELEEARASRDEILAQSKESEKK----------LKNLEAELLQLQEDLAASE-----RARR 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 463 HVCEMTKEIAEKIEKYNKCKQLLQDEK----TKCNKYAEEL----AKMEL---KWKEQVKIAENVKLELA------EVED 525
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKrrleARIAQLEEELeeeqSNTELlndRLRKSTLQVEQLTTELAaerstsQKSE 937
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1244518284 526 NYKVQLAEKEKEINGLASYLENL--SREKELTKSLEdQKGRKLEGQSPQQ 573
Cdd:pfam01576 938 SARQQLERQNKELKAKLQEMEGTvkSKFKSSIAALE-AKIAQLEEQLEQE 986
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
213-323 |
4.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 213 LRVENEEFMKRYSDATAKVQQLEEDIvsvthKAIEKETD------LDSLKDKLRKAQHEREQLECQLQTEKD---EKELY 283
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEK-----EALKKEQDeasferLAELRDELAELEEELEALKARWEAEKElieEIQEL 476
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1244518284 284 KEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRD 323
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEED 516
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
171-388 |
4.77e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDI----------VS 240
Cdd:pfam00038 66 LTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELaflkknheeeVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 241 VTHKAIEKETDL----DSLKDKLRKAQHE-REQLECQLQTEKDE-KELYKEDTLFLKEQLRKAEEQVQATRQELifltKE 314
Cdd:pfam00038 146 ELQAQVSDTQVNvemdAARKLDLTSALAEiRAQYEEIAAKNREEaEEWYQSKLEELQQAAARNGDALRSAKEEI----TE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 315 LSDAVNVRDktmADLHTARLENERVKKQLADTLAELQLhAVKKDQEKTDTLEHELR----------REVEDL---KLRLQ 381
Cdd:pfam00038 222 LRRTIQSLE---IELQSLKKQKASLERQLAETEERYEL-QLADYQELISELEAELQetrqemarqlREYQELlnvKLALD 297
|
....*..
gi 1244518284 382 MAADHYR 388
Cdd:pfam00038 298 IEIATYR 304
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
168-361 |
4.90e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSqEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDI-VSVTHKAI 246
Cdd:pfam15905 124 VASLEKQLLELTRVNELLKAKFS-EDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLeHSKGKVAQ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 247 EKETDLDSLKDKLRKAQHEREQLEC--QLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDK 324
Cdd:pfam15905 203 LEEKLVSTEKEKIEEKSETEKLLEYitELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
170 180 190
....*....|....*....|....*....|....*...
gi 1244518284 325 TMADLHTARLENERVKKQLADTL-AELQLHAVKKDQEK 361
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLnAELEELKEKLTLEE 320
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
173-616 |
6.04e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 173 KETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQS------LRVENEEFMKRYSDATAKVQQLE--------EDI 238
Cdd:pfam10174 130 KELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSkglpkkSGEEDWERTRRIAEAEMQLGHLEvlldqkekENI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 239 ------------------VSVTHKAIE-KETDLDSLKDKLRKAQHEREQLEC-------QLQTEKDEKELYKEDTLF--- 289
Cdd:pfam10174 210 hlreelhrrnqlqpdpakTKALQTVIEmKDTKISSLERNIRDLEDEVQMLKTngllhteDREEEIKQMEVYKSHSKFmkn 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 290 ----LKEQLRKAEEQVQATRQELIFLTKELSD----------AVNVRDKTMADLHTA----RLENERVKKQLADTLAELQ 351
Cdd:pfam10174 290 kidqLKQELSKKESELLALQTKLETLTNQNSDckqhievlkeSLTAKEQRAAILQTEvdalRLRLEEKESFLNKKTKQLQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 352 lhavkKDQEKTDTLEHELRreveDLKLRLQMaadhyreKFKECQRLQKQINKLSDQAASTNSVFTKKMGSQQKVNDASIN 431
Cdd:pfam10174 370 -----DLTEEKSTLAGEIR----DLKDMLDV-------KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 432 TDPAASTSASAVDVKP----------AASCAETGFDMST--------KDHVCEMTKEIAEK------------------I 475
Cdd:pfam10174 434 TDTALTTLEEALSEKEriierlkeqrEREDRERLEELESlkkenkdlKEKVSALQPELTEKesslidlkehasslassgL 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 476 EKYNKCKQL---LQDEKTKCNKYAEELAKM-ELKWKEQVKIAENVKLELAEVEDNYKVQLAEK-EKEINGLASYLenlsR 550
Cdd:pfam10174 514 KKDSKLKSLeiaVEQKKEECSKLENQLKKAhNAEEAVRTNPEINDRIRLLEQEVARYKEESGKaQAEVERLLGIL----R 589
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1244518284 551 EKELTKSLEDQKGRKLEGQSPQQvsrclntCSEQNGLLPPLSSAQPVLQYGNPYSAQETRDGADGA 616
Cdd:pfam10174 590 EVENEKNDKDKKIAELESLTLRQ-------MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNL 648
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
244-381 |
7.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 244 KAIEKETDLD----------SLKDKLRKAQHEREQLEcqLQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQEliflTK 313
Cdd:COG2433 357 KKVPPDVDRDevkarvirglSIEEALEELIEKELPEE--EPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE----VE 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1244518284 314 ELSDAVNVRDKTMADLhtaRLENERVKKQLADTLAELQlhAVKKDQEKTDTLEHEL---RREVEDLKLRLQ 381
Cdd:COG2433 431 ELEAELEEKDERIERL---ERELSEARSEERREIRKDR--EISRLDREIERLERELeeeRERIEELKRKLE 496
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
463-560 |
7.38e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 463 HVCEMTKEI-AEKIEKY-------NKCKQLLQDEKTKCNKYAEELAKME-LKWKEQVKIAENvklELAEVEDNYKvqlaE 533
Cdd:PRK05771 32 HIEDLKEELsNERLRKLrslltklSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEE---ELEKIEKEIK----E 104
|
90 100
....*....|....*....|....*..
gi 1244518284 534 KEKEINGLASYLENLSREKELTKSLED 560
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPWGN 131
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
290-418 |
7.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 290 LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADtlAELQLHAVKKDQEKTDtleheL 369
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--YEEQLGNVRNNKEYEA-----L 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1244518284 370 RREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQAASTNSVFTKK 418
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
168-361 |
7.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVThkAIE 247
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD--VLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 248 KETDLDSLKDKL----RKAQHEREQLEcQLQTEKDEKELykedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRD 323
Cdd:COG3883 110 GSESFSDFLDRLsalsKIADADADLLE-ELKADKAELEA-------KKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1244518284 324 KTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEK 361
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
290-407 |
7.78e-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: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 290 LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRD--KTMADLHTARLENERVKKQLADtlAELQLHAVKKDQektDTLEh 367
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAE--LEAELERLDASS---DDLA- 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1244518284 368 ELRREVEDLKLRLQMAADHYREKFKECQRLQKQINKLSDQ 407
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
246-569 |
7.88e-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: 39.72 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 246 IEKETDLDSLKDKLRKAQ--HEREQLECQ-----LQTEKDEKELYKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDA 318
Cdd:pfam05557 5 IESKARLSQLQNEKKQMEleHKRARIELEkkasaLKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 319 VNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQEKTdtlehELRREVEDLKLRLQMAADHYREKFKECQRLQ 398
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQ-----STNSELEELQERLDLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 399 KQINKLSDQaastnsvftkkmgsQQKVNDASINTdpaASTSASAVDVKPAASCAETGFDM-STKDHVCEMTKEIAEKIEK 477
Cdd:pfam05557 160 KQQSSLAEA--------------EQRIKELEFEI---QSQEQDSEIVKNSKSELARIPELeKELERLREHNKHLNENIEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 478 YNKCKQLLQDEKTKCNKYAE----------ELAKMELKWKEQVKIAENVKLELAEVED--NYKVQLAEKEKEINGLASYL 545
Cdd:pfam05557 223 KLLLKEEVEDLKRKLEREEKyreeaatlelEKEKLEQELQSWVKLAQDTGLNLRSPEDlsRRIEQLQQREIVLKEENSSL 302
|
330 340
....*....|....*....|....
gi 1244518284 546 ENLSREKELTKSLEDQKGRKLEGQ 569
Cdd:pfam05557 303 TSSARQLEKARRELEQELAQYLKK 326
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
178-389 |
8.02e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 178 LREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLrveneefmkrysdatAKVQQLEEDIvsvthkaiekETDLDSLKD 257
Cdd:COG3096 283 LSERALELRRELFGAR---RQLAEEQYRLVEMAREL---------------EELSARESDL----------EQDYQAASD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 258 KLRKAQhereqlECQLQTEKDEKelYKEDTLFLKEQLRKAEEQVQATRQElifltkelsdavnvRDKTMADLHTARLENE 337
Cdd:COG3096 335 HLNLVQ------TALRQQEKIER--YQEDLEELTERLEEQEEVVEEAAEQ--------------LAEAEARLEAAEEEVD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 338 RVKKQLAD-----------------------------TLAELQLHAVKKDQEKTDTLEHELRREVEDLKLRLQMAADHYR 388
Cdd:COG3096 393 SLKSQLADyqqaldvqqtraiqyqqavqalekaralcGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARR 472
|
.
gi 1244518284 389 E 389
Cdd:COG3096 473 Q 473
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-376 |
8.75e-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: 39.62 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 168 IAVLEKETAQLREQVGRMERELSQE--KGRCEQLQAEQKGLLEVSQSLRVENEEFMKrysdataKVQQLEEDIVSVTHKA 245
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQE-------LIDQKEKEKKDLIKEI 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1244518284 246 IEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKEDTLFLKEQLRKaeeqVQATRQELIFLTKELSDAVNVRDKT 325
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE----IRNKWPEIIKKIKESKTKIDDIIEL 681
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1244518284 326 MAD------LHTARLENERVKKQLADTLAELQLHaVKKDQEKTDTLEHELRREVEDL 376
Cdd:TIGR04523 682 MKDwlkelsLHYKKYITRMIRIKDLPKLEEKYKE-IEKELKKLDEFSKELENIIKNF 737
|
|
| |
