|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
17-120 |
6.20e-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: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 17 VIFQNVAKSYLPNAHLECHYTLTPYIHPHSKDWVGIFKVGWSTARDYYTFLWSpmPEHYVEGSTVNCVLAFQGYYLPNDD 96
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 568942384 97 GEFYQFCYVTHKGEIRGASTPFQF 120
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
125-408 |
3.55e-31 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 128.09 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 125 PVEELLTME-----DEGNSDMLVVTTKAGLL------------------ELKIEKTLKEKEELLKLIAVLEKETAQLREQ 181
Cdd:pfam07888 2 PLDELVTLEeeshgEEGGTDMLLVVPRAELLqnrleeclqeraellqaqEAANRQREKEKERYKRDREQWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 182 VGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRK 261
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 262 AQHereqlecQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQscladkenlyraLLL 341
Cdd:pfam07888 162 AGA-------QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT------------QKL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568942384 342 TTSNKEDTLF--LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADT 408
Cdd:pfam07888 223 TTAHRKEAENeaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
704-730 |
2.57e-11 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 58.43 E-value: 2.57e-11
10 20
....*....|....*....|....*..
gi 568942384 704 KKCPLCELMFPPNYDQTKFEEHVESHW 730
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 ... |
731-757 |
3.92e-11 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 57.95 E-value: 3.92e-11
10 20
....*....|....*....|....*..
gi 568942384 731 KVCPMCSEQFPPDYDQQGFERHVQTHF 757
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-422 |
1.12e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 248 KETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIEntkLVSEIQTLKNLDGNKESMITHFKEEISKLQS 327
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 328 CLADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLhtaRLENERVKKQLAD 407
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL---EEEEEALLELLAE 467
|
250
....*....|....*
gi 568942384 408 TLAELQLHAVKKDQA 422
Cdd:COG1196 468 LLEEAALLEAALAEL 482
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
706-729 |
1.61e-10 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 56.27 E-value: 1.61e-10
10 20
....*....|....*....|....
gi 568942384 706 CPLCELMFPPNYDQTKFEEHVESH 729
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-412 |
1.02e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLR--KAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKlvseiQTLKNLDGNKESM---ITHFKEEISKL 325
Cdd:TIGR02168 797 ELKALREALDelRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-----EQIEELSEDIESLaaeIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 326 QSCLADKENLYRALLLTTSNKEDTLF-LKEQLRKAEEQVQATRQELIFLTKELSDAVnvrdktmadLHTARLENERvkKQ 404
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEeLSEELRELESKRSELRRELEELREKLAQLE---------LRLEGLEVRI--DN 940
|
....*...
gi 568942384 405 LADTLAEL 412
Cdd:TIGR02168 941 LQERLSEE 948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-416 |
3.16e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 143 VTTKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMK 222
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 223 RYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQ 302
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 303 TLKNLDGNKESMITHFKEEISKLQsclADKENLYRALLLTTSNKEDtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVN 382
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLE---EELEELEEALAELEEEEEE---EEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270
....*....|....*....|....*....|....
gi 568942384 383 VRDKTMADLHTARLENERVKKQLADTLAELQLHA 416
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
731-757 |
1.10e-08 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 51.11 E-value: 1.10e-08
10 20
....*....|....*....|....*..
gi 568942384 731 KVCPMCSEQFPPDYDQQGFERHVQTHF 757
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
733-756 |
5.42e-08 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 49.11 E-value: 5.42e-08
10 20
....*....|....*....|....
gi 568942384 733 CPMCSEQFPPDYDQQGFERHVQTH 756
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-412 |
6.02e-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: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQ----QLEEDIVSVTHKAI 246
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekigELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 247 EKETDLDSLKDKLRKAQHER-------EQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFK 319
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIdkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 320 EEISKLQSCLAD-KENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLEN 398
Cdd:TIGR02169 392 EKLEKLKREINElKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
250
....*....|....
gi 568942384 399 ERVKKQLADTLAEL 412
Cdd:TIGR02169 472 YDLKEEYDRVEKEL 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-580 |
6.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 168 IAVLEKETAQLREQVGRME---------RELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDI 238
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKelkekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 239 VSVTHKAIEKETD---LDSLKDKLRKAQHEREQLECqLQTEKDEKELYKVHLKNTEIEN--TKLVSEIQTLKNLDGNKES 313
Cdd:PRK03918 348 KELEKRLEELEERhelYEEAKAKKEELERLKKRLTG-LTPEKLEKELEELEKAKEEIEEeiSKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 314 MITHFKEEISKLQSCLA-----DKENLYRALLLTTSNkedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNV-RDKT 387
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRelteeHRKELLEEYTAELKR------IEKELKEIEEKERKLRKELRELEKVLKKESELiKLKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 388 MAD--------LHTARLENERVKKQLADTLAELqLHAVKKDQASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDvk 459
Cdd:PRK03918 501 LAEqlkeleekLKKYNLEELEKKAEEYEKLKEK-LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK-- 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 460 paaSCAETGFdmSTKDHVCEMTKEIAEKIEKYNKCK---QLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEV 536
Cdd:PRK03918 578 ---ELEELGF--ESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568942384 537 EDNYKVQ--------LAEKEKEINGLASYLENL-SREKELTKSLEDQKGRKLE 580
Cdd:PRK03918 653 EKKYSEEeyeelreeYLELSRELAGLRAELEELeKRREEIKKTLEKLKEELEE 705
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
706-729 |
8.83e-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: 8.83e-08
10 20
....*....|....*....|....
gi 568942384 706 CPLCELMFPPNYDQTKFEEHVESH 729
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-408 |
1.02e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL-------LEVSQSLRVENEEFMK 222
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 223 RYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQ 302
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 303 TLKNLDGNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNKEDTLF--LKEQLRK--------------AEEQVQAT 366
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEeeARRRLKRlenkikelgpvnlaAIEEYEEL 998
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568942384 367 RQELIFLTKELSDAVNVRDK---TMADLhtarleNERVKKQLADT 408
Cdd:TIGR02168 999 KERYDFLTAQKEDLTEAKETleeAIEEI------DREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-370 |
1.46e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL 206
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 207 LEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHERE-------QLECQLQTEKDE 279
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 280 KELYKVHLKNTEIENTKLVSEIQTL-KNLDGNK----ESMITHFKEEISKLQSCLADKENLYRAlllttsnkedtlfLKE 354
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELlKKLEEAElkelQAELEELEEELEELQEELERLEEALEE-------------LRE 468
|
250
....*....|....*.
gi 568942384 355 QLRKAEEQVQATRQEL 370
Cdd:TIGR02168 469 ELEEAEQALDAAEREL 484
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
733-756 |
1.49e-07 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 47.80 E-value: 1.49e-07
10 20
....*....|....*....|....
gi 568942384 733 CPMCSEQFPPDYDQQGFERHVQTH 756
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-434 |
1.90e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTE 276
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 277 KDE-KELYKVHLKNTEIENTKLV----SEIQTLKNLDGNKeSMITHFKEEISKLQSCLADKENLyralllttsnKEDTLF 351
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAAL----------RAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 352 LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQASTNSVFTKK 431
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
...
gi 568942384 432 MGS 434
Cdd:COG4942 252 KGK 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-580 |
2.33e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 229 AKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLE--CQLQTEKDEKELYkVHLKNTEientKLVSEIQTLKN 306
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEGY-ELLKEKE----ALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 307 LDGNKESMITHFKEEISKLQSCLADKENLYRALLLTTSNK--EDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVR 384
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 385 DKTMADLHTARLENERVKKQLADtlaelqlHAVKKDQastnsvFTKKMGSQQKVNDASINtdpaastSASAVDVKPAASC 464
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEE-------ERKRRDK------LTEEYAELKEELEDLRA-------ELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 465 AEtgfdmstkdhvcemTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQL 544
Cdd:TIGR02169 385 DE--------------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
330 340 350
....*....|....*....|....*....|....*.
gi 568942384 545 AEKEKEINGLASYLENLSREKELTKSLEDQKGRKLE 580
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-566 |
4.55e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQkgllEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKEL-------YKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISK 324
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 325 LQSCLADKENLYRALlltTSNKEDTlflKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQ 404
Cdd:PRK02224 354 LEERAEELREEAAEL---ESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 405 LADTLAELQlhavkkdqastnsvftkkmgsqqkvndasintdPAASTSASAVDVKPAASCAETGFDMSTKDHVCEMTkEI 484
Cdd:PRK02224 428 EAELEATLR---------------------------------TARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-ED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 485 AEKIEKYNKCKQLLQDEKTKCNK---YAEELAKMElkwKEQVKIAENVKLeLAEVEDNYKVQLAEKEKEINGL---ASYL 558
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEErleRAEDLVEAE---DRIERLEERRED-LEELIAERRETIEEKRERAEELrerAAEL 549
|
....*...
gi 568942384 559 ENLSREKE 566
Cdd:PRK02224 550 EAEAEEKR 557
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-439 |
1.19e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQkglLEVSQSLrvenEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEV---SELEEEI----EELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKEN---LYRALL-LTTSNKEDTLFLKEQLRKA--EEQVQATRQELIFLTKELSDAVNVRDKTMADLhtARLENERVKKQ 404
Cdd:TIGR02168 397 SLNNeieRLEARLeRLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEAL--EELREELEEAE 474
|
250 260 270
....*....|....*....|....*....|....*
gi 568942384 405 LADTLAELQLHAVKKDQASTNSVFTKKMGSQQKVN 439
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-521 |
2.01e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSqekgRCEQLQAEQKGLL-EVSQSLRVENeefmKRYSDATAKVQQLEEDIVSVTHKAIEKE 249
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELS----SLQSELRRIENRLdELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 250 TDLDSLKDKLRKAQHEREQLECQLqtEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLdgnkesmITHFKEEISKLQSCL 329
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLSHSRIPEIQAE-------LSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 330 ADKE-NLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADT 408
Cdd:TIGR02169 815 REIEqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 409 LAELQLHAVKKDQASTnSVFTKKmgSQQKVNDASINtdpAASTSASAVDVKPAASCAETGFDMSTKDhVCEMTKEIAEKI 488
Cdd:TIGR02169 895 EAQLRELERKIEELEA-QIEKKR--KRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEI 967
|
330 340 350
....*....|....*....|....*....|....*..
gi 568942384 489 EKY----NKCKQLLQDEKTKCNKYAEELAKMELKWKE 521
Cdd:TIGR02169 968 RALepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-407 |
4.26e-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: 50.50 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 178 LREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEediVSVTHKAIEKETDLDSLKD 257
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE---ARVSDLELEKVKLVNAGSE 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 258 KLRKA---QHEREQLECQLQTEKDE----KELYKVHLKN-----TEIENT--KL-------VSEIQTLKNLDGNKESMIT 316
Cdd:pfam15921 644 RLRAVkdiKQERDQLLNEVKTSRNElnslSEDYEVLKRNfrnksEEMETTtnKLkmqlksaQSELEQTRNTLKSMEGSDG 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 317 HFKEEISKLQSCLADKENLYRALllttsnKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARL 396
Cdd:pfam15921 724 HAMKVAMGMQKQITAKRGQIDAL------QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
250
....*....|.
gi 568942384 397 ENERVKKQLAD 407
Cdd:pfam15921 798 QERRLKEKVAN 808
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-417 |
8.15e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 197 EQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTE 276
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 277 KDEKELYKV--HLKNTEIENTKLVSEIQTLKNLdgnkesmithfKEEISKLQSCLADKENLYRALLLTTSNKEdtlflKE 354
Cdd:COG4717 129 PLYQELEALeaELAELPERLEELEERLEELREL-----------EEELEELEAELAELQEELEELLEQLSLAT-----EE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568942384 355 QLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLhtARLENERVKKQLADTLAELQLHAV 417
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL--EQLENELEAAALEERLKEARLLLL 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-574 |
8.17e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 175 TAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLeedivsvthkaiekETDLDS 254
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEF--------------EATTCS 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 255 LKDKLRKAQHEREQLECQlqtekdekelykvhLKNTEIENTKLVSEIQTLKNLDGNKESmithfkeEISKLQSCLADKEN 334
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQ--------------LKIITMELQKKSSELEEMTKFKNNKEV-------ELEELKKILAEDEK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 335 LyralllttsnkedtLFLKEQLRKAEEQVQATRQELIFL----TKELSD-AVNVRDKTMADLHTAR--------LENERV 401
Cdd:pfam05483 420 L--------------LDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDlEIQLTAIKTSEEHYLKevedlkteLEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 402 KK-QLADTLAELQLHAVKKDQASTNSVFTKKMGSQQKVND--------ASINT---------DPAASTSASAVDVKPAAS 463
Cdd:pfam05483 486 KNiELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkkqeermlKQIENleekemnlrDELESVREEFIQKGDEVK 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 464 CAETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKcNKYAEELAKmELKWKEQVKIAEN------------VKL 531
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK-NKNIEELHQ-ENKALKKKGSAENkqlnayeikvnkLEL 643
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568942384 532 ELAEVEDNYKVQLAEKEKEINGLASYLENLSREKELTKSLEDQ 574
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
180-625 |
1.33e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 180 EQVGRMERELSQEKGRCEQLQAEQK----GLLEVSQSLRV------------------ENEEFMKRYSDATAKVQQLEED 237
Cdd:pfam15921 253 ESQNKIELLLQQHQDRIEQLISEHEveitGLTEKASSARSqansiqsqleiiqeqarnQNSMYMRQLSDLESTVSQLRSE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 238 IVSVTH----KAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKD--EKELYKVHLKNTEIENTKlvSEIQTLKNLDGNK 311
Cdd:pfam15921 333 LREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDqlQKLLADLHKREKELSLEK--EQNKRLWDRDTGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 312 ESMITHFKEEISKLQSCLADKENLYRALllttsnKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADL 391
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAM------KSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 392 HTARLENERVKKQLADTLAELQlhavKKDQA--STNSVFTK-------KMGSQQKVNDASINTDPAastsasavdvkpAA 462
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQ----EKERAieATNAEITKlrsrvdlKLQELQHLKNEGDHLRNV------------QT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 463 SCAETGFDMSTKDHVCEMTKEIAEK----IEKYNKCKQLLQDEKTKCNKYAE----ELAKME-LKWKEQVKIA------- 526
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENmtqlVGQHGRTAGAMQVEKAQLEKEINdrrlELQEFKiLKDKKDAKIRelearvs 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 527 ----ENVKLELAEVEDNYKVQLAEKEK-----EINGLASYLENLSREKELTKSLEDQKGRKLEgqspqqvsrclntcSEQ 597
Cdd:pfam15921 629 dlelEKVKLVNAGSERLRAVKDIKQERdqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME--------------TTT 694
|
490 500
....*....|....*....|....*....
gi 568942384 598 NGLLPPLSSAQPVL-QYGNPYSAQETRDG 625
Cdd:pfam15921 695 NKLKMQLKSAQSELeQTRNTLKSMEGSDG 723
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
185-422 |
1.46e-05 |
|
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: 48.53 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 185 MERELSQekgRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSdataKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQH 264
Cdd:pfam05622 8 EKDELAQ---RCHELDQQVSLLQEEKNSLQQENKKLQERLD----QLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 265 ERE--QLECQLQtekdEKELYKVHLKNTEIenTKLVSEIQTLknldgnkesmithfKEEISKLQSClADKENLYRALLLT 342
Cdd:pfam05622 81 ARDdyRIKCEEL----EKEVLELQHRNEEL--TSLAEEAQAL--------------KDEMDILRES-SDKVKKLEATVET 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 343 TSNK-EDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRdktmadlhtARLENerVKKQLADTLAELQLHAVKKDQ 421
Cdd:pfam05622 140 YKKKlEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALR---------GQLET--YKRQVQELHGKLSEESKKADK 208
|
.
gi 568942384 422 A 422
Cdd:pfam05622 209 L 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
201-411 |
1.75e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 201 AEQKGLLEVsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLqtEKDEK 280
Cdd:COG1579 4 EDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 281 ELYKVHlKNTEIENtkLVSEIQTLKnldgnkesmithfkEEISKLqscladkenlyralllttsnKEDTLFLKEQLRKAE 360
Cdd:COG1579 81 QLGNVR-NNKEYEA--LQKEIESLK--------------RRISDL--------------------EDEILELMERIEELE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568942384 361 EQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAE 411
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
169-413 |
2.48e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.84 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 169 AVLEKETAQLREQVGR--------MERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVS 240
Cdd:pfam00038 28 KLLETKISELRQKKGAepsrlyslYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 241 ---VTHKA----IEKETDLDSLKDKL--RKAQHERE--QLECQLQTEKdekelykvhlKNTEIENTKLVSEIQTLKNLDG 309
Cdd:pfam00038 108 lrkDLDEAtlarVDLEAKIESLKEELafLKKNHEEEvrELQAQVSDTQ----------VNVEMDAARKLDLTSALAEIRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 310 NKESMITHFKEEIsklqscladkENLYRALL--LTTSNKEDTlflkEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKT 387
Cdd:pfam00038 178 QYEEIAAKNREEA----------EEWYQSKLeeLQQAAARNG----DALRSAKEEITELRRTIQSLEIELQSLKKQKASL 243
|
250 260
....*....|....*....|....*.
gi 568942384 388 MADLHTARLENERVKKQLADTLAELQ 413
Cdd:pfam00038 244 ERQLAETEERYELQLADYQELISELE 269
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-575 |
2.48e-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: 47.79 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 175 TAQLREQVGRMErELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDS 254
Cdd:pfam05483 383 TMELQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 255 LKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLK-NLDGNKESMITHFKEEISKLQSC--LAD 331
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIenLEE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 332 KENLYRALLLTTSN--KEDTLFLKEQLRKAEEQVQATRQELIFLTKE----------LSDAVNVRDKTMADLHTarlENE 399
Cdd:pfam05483 542 KEMNLRDELESVREefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQmkilenkcnnLKKQIENKNKNIEELHQ---ENK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 400 RVKKQLADTLAELQLHAVKKDQ-----ASTNSVFTKKMGSQQK-VNDASINTDPAASTSASAVDVKPAASCAETGFDMST 473
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKlelelASAKQKFEEIIDNYQKeIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 474 KDHVCEMTKEIAEKIEKYNKckqLLQDEKTKCNKY-AEELAKMELKWKEQVKIAeNVKLELAEVEDNYKVQLAEKEKein 552
Cdd:pfam05483 699 QHKIAEMVALMEKHKHQYDK---IIEERDSELGLYkNKEQEQSSAKAALEIELS-NIKAELLSLKKQLEIEKEEKEK--- 771
|
410 420
....*....|....*....|....
gi 568942384 553 glasylenLSRE-KELTKSLEDQK 575
Cdd:pfam05483 772 --------LKMEaKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-413 |
3.58e-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: 46.68 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKENLYR---------------ALLLTTSNKEDTL-------FLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTM 388
Cdd:COG4942 101 AQKEELAellralyrlgrqpplALLLSPEDFLDAVrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180
....*....|....*....|....*
gi 568942384 389 ADLHTARLENERVKKQLADTLAELQ 413
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLE 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
186-468 |
3.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 186 ERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRK-AQH 264
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 265 ereqlecqLQTEKDEKELYKVHLKNTEIENtkLVSEIQTLKNLDGNKESMITHFKEEISKLQScladkenlyrallltts 344
Cdd:COG3883 95 --------LYRSGGSVSYLDVLLGSESFSD--FLDRLSALSKIADADADLLEELKADKAELEA----------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 345 nkedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKKDQAST 424
Cdd:COG3883 148 -------KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568942384 425 NSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAETG 468
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-552 |
5.65e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLrveneefmkrysdatakvqqleedivsvthkaie 247
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL---------------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 248 kETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQS 327
Cdd:TIGR04523 390 -ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 328 CLADKENLYRALLLTTSNKEDTLFLKEQ-LRKAEEQVQATRQELIFLTKELSDAVNVRDKtmadlhtarLENErvKKQLA 406
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKeLKKLNEEKKELEEKVKDLTKKISSLKEKIEK---------LESE--KKEKE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 407 DTLAELQLHAVKKDQASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAEtgfdmstkdhVCEMTKEIAE 486
Cdd:TIGR04523 538 SKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE----------KKDLIKEIEE 607
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568942384 487 KIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELaeveDNYKVQLAEKEKEIN 552
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI----KEIRNKWPEIIKKIK 669
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-440 |
5.69e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 153 KIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQ 232
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 233 QLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKE 312
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 313 SMITHFKEEISKLQSCL-ADKENLYRALLLTTSN---------KEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVN 382
Cdd:TIGR04523 531 SEKKEKESKISDLEDELnKDDFELKKENLEKEIDeknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942384 383 VRDKTMADLHTARLENERV---------KKQLADTLAELQLHAVKKDQASTNSVFTKKMGSQQKVND 440
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLssiikniksKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-422 |
7.65e-05 |
|
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: 46.21 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 176 AQLREQVGRMERE---------LSQEKGRCEQ---------LQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEED 237
Cdd:TIGR02169 194 DEKRQQLERLRRErekaeryqaLLKEKREYEGyellkekeaLERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 238 IVSVTHKaIEKETDLDSL--KDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMI 315
Cdd:TIGR02169 274 LEELNKK-IKDLGEEEQLrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 316 THFKEEISKLQsclaDKENLYRALLLTTSNKEDTLFlkeqlrkaEEQVQAtRQELIFLTKELSDAVNVRDKTMADLHTAR 395
Cdd:TIGR02169 353 DKLTEEYAELK----EELEDLRAELEEVDKEFAETR--------DELKDY-REKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260
....*....|....*....|....*...
gi 568942384 396 LENERVKKQLADTLAEL-QLHAVKKDQA 422
Cdd:TIGR02169 420 EELADLNAAIAGIEAKInELEEEKEDKA 447
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-422 |
8.37e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 169 AVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSL--RVENEEfmkrysdatAKVQQLEEDIVSVTHKAI 246
Cdd:pfam01576 64 ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLeeQLDEEE---------AARQKLQLEKVTTEAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 247 EKETDLDSLKDKLRKAQHEREQLECQLQ------TEKDEKelykvhlknteientklVSEIQTLKNldgNKESMITHFKE 320
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISeftsnlAEEEEK-----------------AKSLSKLKN---KHEAMISDLEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 321 EISKLQSCLADKENLYRALLLTTSNkedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENER 400
Cdd:pfam01576 195 RLKKEEKGRQELEKAKRKLEGESTD------LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
|
250 260
....*....|....*....|..
gi 568942384 401 VKKQLADTLAELQLHAVKKDQA 422
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKA 290
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-563 |
1.01e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 182 VGRMERELSQE----KGRCEQLQAEQKGLLEVSQSlrvENEEFMKRYSDataKVQQL----EEDIVSVTHKAIEKETDLD 253
Cdd:pfam15921 222 ISKILRELDTEisylKGRIFPVEDQLEALKSESQN---KIELLLQQHQD---RIEQLisehEVEITGLTEKASSARSQAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 254 SLKdklrkaqherEQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKesmithfKEEISKlQSCLADKE 333
Cdd:pfam15921 296 SIQ----------SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK-------IEELEK-QLVLANSE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 334 nlyrallLTTSNKEDTLFLKEQlRKAEEQVQATRQELIFLTKELSdAVNVRDKTMADLHTAR-LENERVKKQLADTLAEL 412
Cdd:pfam15921 358 -------LTEARTERDQFSQES-GNLDDQLQKLLADLHKREKELS-LEKEQNKRLWDRDTGNsITIDHLRRELDDRNMEV 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 413 Q-----LHAVKKD-QASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDhVCEMTKEIAE 486
Cdd:pfam15921 429 QrlealLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT-VSDLTASLQE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 487 K---IEKYNKckqllqdEKTKCNkyaeelAKMELKWKE-QVKIAENVKLELAEVE-DNYKVQLAEKEKEINGLASYLENL 561
Cdd:pfam15921 508 KeraIEATNA-------EITKLR------SRVDLKLQElQHLKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQIENM 574
|
..
gi 568942384 562 SR 563
Cdd:pfam15921 575 TQ 576
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
731-758 |
1.10e-04 |
|
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar proteins; spn-F is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. It acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F is a coil-coiled protein containing a C2H2-type zinc binding domain.
Pssm-ID: 412017 Cd Length: 30 Bit Score: 39.82 E-value: 1.10e-04
10 20
....*....|....*....|....*...
gi 568942384 731 KVCPMCSEQFPPDYDQQGFERHVQTHFD 758
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-413 |
1.30e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEedivsvthkaiEKET 250
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-----------SLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKAQHEREQLECQLQtekdekelykvhlknteientKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRK---------------------QLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKENLYRALLLTTSNKEdtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLA 410
Cdd:COG4372 168 ALEQELQALSEAEAEQA----LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
...
gi 568942384 411 ELQ 413
Cdd:COG4372 244 LEE 246
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
731-757 |
1.97e-04 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 39.02 E-value: 1.97e-04
10 20
....*....|....*....|....*..
gi 568942384 731 KVCPMCSEQFPPDYDQQGFERHVQTHF 757
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
172-419 |
3.83e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEIsKLQSCLAD 331
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE-AKDSLEAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 332 KENLYRALLLTTSNKEDTLFLKEQLRK--AEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTL 409
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILkeIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250
....*....|
gi 568942384 410 AELQLHAVKK 419
Cdd:COG4372 311 GALEDALLAA 320
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-580 |
4.74e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIvsvthkaIEKET 250
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-------KELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKAQHEREQlecqlQTEKDEKElykvhlkntEIENTKlvSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQ-----DWNKELKS---------ELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKENlyralllTTSNKEDTLFLKE-QLRKAEEQVQATRQELIFLTKELSDavnvrdktmadLHTARLENERVKKQLADTL 409
Cdd:TIGR04523 353 NSES-------ENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQIND-----------LESKIQNQEKLNQQKDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 410 AELQLHAVKKDQAstnsvfTKKMGSQQKVNDASINtdpaastsasavdvkpaascaetgfdmstkdhvcEMTKEIAEKIE 489
Cdd:TIGR04523 415 KKLQQEKELLEKE------IERLKETIIKNNSEIK----------------------------------DLTNQDSVKEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 490 KYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNyKVQLAEKEKEINGLASYLENLSREKELTK 569
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
410
....*....|.
gi 568942384 570 SLEDQKGRKLE 580
Cdd:TIGR04523 534 KEKESKISDLE 544
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
175-586 |
5.42e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 175 TAQLREQVGRMERELSQE---KGRCEQLQAE-QKGLLEVsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:pfam10174 267 TEDREEEIKQMEVYKSHSkfmKNKIDQLKQElSKKESEL-LALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKAQHEREQLECQLQTEKDEKelykvhlknteienTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLA 330
Cdd:pfam10174 346 EVDALRLRLEEKESFLNKKTKQLQDLTEEK--------------STLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKE----NLYRAL--LLTTSNKEDTLF--LKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVK 402
Cdd:pfam10174 412 DKDkqlaGLKERVksLQTDSSNTDTALttLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 403 KQLADTLAELQLHA-------VKKDqastNSVFTKKMGSQQKVNDAS--INTDPAASTSASAVDVKPAAScaetgfdmst 473
Cdd:pfam10174 492 TEKESSLIDLKEHAsslassgLKKD----SKLKSLEIAVEQKKEECSklENQLKKAHNAEEAVRTNPEIN---------- 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 474 kDHVCEMTKEIAEKIEKYNKCK----QLL------QDEKTKCNKYAEELAKMEL-KWKEQVKIAENVKL--------ELA 534
Cdd:pfam10174 558 -DRIRLLEQEVARYKEESGKAQaeveRLLgilrevENEKNDKDKKIAELESLTLrQMKEQNKKVANIKHgqqemkkkGAQ 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568942384 535 EVEDNYKVQLAEKEkeiNGLASYLENLSREKELTKSLEDQKGRKLegQSPQQ 586
Cdd:pfam10174 637 LLEEARRREDNLAD---NSQQLQLEELMGALEKTRQELDATKARL--SSTQQ 683
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-413 |
7.02e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGL---LEVSQSLRVENEEFMKRYSdatAKVQQLEEDIVSVTHKAIEK 248
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALqeqLQAETELCAEAEEMRARLA---ARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 249 ETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSC 328
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 329 LADKENLYRALLLTTSNKEDTLFLKEQLRKAEEQvqaTRQELIFLTKELSDAVNVRDKTMADLhtaRLENERVKKQLADT 408
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEK---GRQELEKAKRKLEGESTDLQEQIAEL---QAQIAELRAQLAKK 241
|
....*
gi 568942384 409 LAELQ 413
Cdd:pfam01576 242 EEELQ 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-395 |
7.60e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRME---RELSQEKGRCEQLQAEQKGLLEVSQ---SLRVENEEFMKRYSDATAKVQQLEEDIVSVTH- 243
Cdd:PRK04863 892 LADRVEEIREQLDEAEeakRFVQQHGNALAQLEPIVSVLQSDPEqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHf 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 244 ------KAIEKETDL-DSLKDKLRKAQHEREQLECQLQTEKDEKELY-KVHlknteienTKLVSEIQTlknldgnKESMI 315
Cdd:PRK04863 972 syedaaEMLAKNSDLnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYnQVL--------ASLKSSYDA-------KRQML 1036
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 316 THFKEEISKLqSCLADKENLYRAlllttSNKEDTlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTAR 395
Cdd:PRK04863 1037 QELKQELQDL-GVPADSGAEERA-----RARRDE--LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
731-758 |
1.01e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 37.04 E-value: 1.01e-03
10 20
....*....|....*....|....*...
gi 568942384 731 KVCPMCSEQFPpDYDQQGFERHVQTHFD 758
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-281 |
1.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 145 TKAGLLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKG-RCEQLQAEQKGLLEVSQSLRVENEEFMKR 223
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568942384 224 YSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKE 281
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
704-729 |
1.31e-03 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 36.76 E-value: 1.31e-03
10 20
....*....|....*....|....*.
gi 568942384 704 KKCPLCELMFPPNYDQTKFEEHVESH 729
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
172-579 |
1.39e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 172 EKETAQLREqvgRMERELSQEKGRCEQLQAEqkgllevsqslrVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETd 251
Cdd:pfam02463 175 LKKLIEETE---NLAELIIDLEELKLQELKL------------KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 252 ldsLKDKLRKAQHEREQLECQLQTEKDEKELYKvHLKNTEIENTKLVSEIqtlknldgnkesmithfKEEISKLQSCLAD 331
Cdd:pfam02463 239 ---IDLLQELLRDEQEEIESSKQEIEKEEEKLA-QVLKENKEEEKEKKLQ-----------------EEELKLLAKEEEE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 332 KENLYRALLLTTSNKEDTL-FLKEQLRKAEEQVQATRQELIFLTKELSDAVnvrdktmadlhTARLENERVKKQladtLA 410
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLkESEKEKKKAEKELKKEKEEIEELEKELKELE-----------IKREAEEEEEEE----LE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 411 ELQLHAVKKDQASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAEtgfdmstkDHVCEMTKEIAEKIEK 490
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE--------DLLKEEKKEELEILEE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 491 YNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQLAEKE-KEINGLASYLENLSREKELTK 569
Cdd:pfam02463 435 EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVLLA 514
|
410
....*....|
gi 568942384 570 SLEDQKGRKL 579
Cdd:pfam02463 515 LIKDGVGGRI 524
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
704-730 |
2.06e-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: 36.32 E-value: 2.06e-03
10 20
....*....|....*....|....*..
gi 568942384 704 KKCPLCELMFPPNYDQTKFEEHVESHW 730
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-300 |
2.27e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 174 ETAQLREqvgrmerELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLD 253
Cdd:TIGR02169 386 ELKDYRE-------KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568942384 254 SLKDKLRKAQHEREQLECQLQteKDEKELYKVHLKNTEIENTKLVSE 300
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYD--RVEKELSKLQRELAEAEAQARASE 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-589 |
2.65e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 153 KIEKTLKEKEELLKLIAVLEKETAQLREQVGRMEREL--SQEKGRCEQL-QAEQKGLLEVSQSLRVEN---EEFMKRYSD 226
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkkAEEKKKADEAkKAEEKKKADEAKKKAEEAkkaDEAKKKAEE 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 227 ATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYKvhlknTEIENTKLVSEIQTLKN 306
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-----KKAEEKKKADEAKKKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 307 LDGNKESMITHFKEEISKLQSCLADKENLYRALLLTtSNKEDTLFLKEQLRKAEEQVQAtrQELIFLTKELSDAVNVRDK 386
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKA--EEAKKKAEEAKKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 387 T----MADLHTARLENERVKKQLADTLAELQLHA--VKKDQASTNSVFTKKMGSQQKVNDASINTD-PAASTSASAVDVK 459
Cdd:PTZ00121 1479 AeeakKADEAKKKAEEAKKKADEAKKAAEAKKKAdeAKKAEEAKKADEAKKAEEAKKADEAKKAEEkKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 460 PAASC--AETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKyAEELAKME-LKWK-EQVKIAENVK----- 530
Cdd:PTZ00121 1559 KAEEKkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK-AEEAKKAEeAKIKaEELKKAEEEKkkveq 1637
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568942384 531 LELAEVEDNYKVQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLEGQSPQQVSR 589
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-414 |
2.88e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKgrcEQLQAEQKGLLEVSQSLRVENEEfmkrYSDATAKVQQLEEDIVSVTHKAIEKET 250
Cdd:COG4372 64 LEEELEQARSELEQLEEELEELN---EQLQAAQAELAQAQEELESLQEE----AEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKAQHEREQLECQLQTEkdEKELYKVHLKNTEIENTKLVSEIQTLKNlDGNKESMITHFKEEISKLQSCLA 330
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESL--QEELAALEQELQALSEAEAEQALDELLK-EANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKENLYRALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLA 410
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
....
gi 568942384 411 ELQL 414
Cdd:COG4372 294 ELKL 297
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
172-411 |
3.10e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 172 EKETAQLREqVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEfmKRYSDATAKVQQLEEDIVsvthkaiEKETD 251
Cdd:PRK05771 39 ELSNERLRK-LRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLE--ELIKDVEEELEKIEKEIK-------ELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 252 LDSLKDKLRKAQHEREQLECQLQTEKDEKELYK--------VHLKNTEIENTKLVSEIQTLKNLDGNKESM----ITH-- 317
Cdd:PRK05771 109 ISELENEIKELEQEIERLEPWGNFDLDLSLLLGfkyvsvfvGTVPEDKLEELKLESDVENVEYISTDKGYVyvvvVVLke 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 318 FKEEISKLqsclaDKENLYRALLLTTSNKedtlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHtARLE 397
Cdd:PRK05771 189 LSDEVEEE-----LKKLGFERLELEEEGT-----PSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALY-EYLE 257
|
250
....*....|....
gi 568942384 398 NERVKKQLADTLAE 411
Cdd:PRK05771 258 IELERAEALSKFLK 271
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
168-379 |
3.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIE 247
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 248 KETDLDSLKDK---LRKAQHEREQLECQLQTE----KDEKELY-KVHLKNTEIENTK----LVSEIQTLKN-LDGNKESM 314
Cdd:COG1340 97 LRKELAELNKAggsIDKLRKEIERLEWRQQTEvlspEEEKELVeKIKELEKELEKAKkaleKNEKLKELRAeLKELRKEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 315 ithfkEEISKLQSCLADKENLYRALLLTTSNKEDTLF-----LKEQLRKAEEQVQATRQELIFLTKELSD 379
Cdd:COG1340 177 -----EEIHKKIKELAEEAQELHEEMIELYKEADELRkeadeLHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
171-442 |
3.31e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRvENEEFMKRYSDATAKVQQLEEDIVSVThkaiEKET 250
Cdd:pfam05557 130 TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK-ELEFEIQSQEQDSEIVKNSKSELARIP----ELEK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKD---KLRKAQHEREQLECQ---LQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNLDGN-------------- 310
Cdd:pfam05557 205 ELERLREhnkHLNENIENKLLLKEEvedLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDtglnlrspedlsrr 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 311 ----KESMITHfKEEISKLQSCLADKENLYRALLLTTSN-KEDTLFLKEQLRKAEEQVQATRQELIFLTKE---LSDAVN 382
Cdd:pfam05557 285 ieqlQQREIVL-KEENSSLTSSARQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVRRLQRRVLLLTKErdgYRAILE 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568942384 383 VRDKTMADLHTARLENERVkKQLADTLAELQLH---------------AVKKDQASTNSVFTKKMGSQQKVNDAS 442
Cdd:pfam05557 364 SYDKELTMSNYSPQLLERI-EEAEDMTQKMQAHneemeaqlsvaeeelGGYKQQAQTLERELQALRQQESLADPS 437
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-381 |
3.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 195 RCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVsvthkaiEKETDLDSLKDKLRKAQHereqlecQLQ 274
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEE-------QLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 275 TEKDEKELykvhlknteienTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLADKENLYRALllttsnKEDtlfLKE 354
Cdd:COG1579 84 NVRNNKEY------------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL------EAE---LEE 142
|
170 180
....*....|....*....|....*..
gi 568942384 355 QLRKAEEQVQATRQELIFLTKELSDAV 381
Cdd:COG1579 143 KKAELDEELAELEAELEELEAEREELA 169
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-390 |
3.65e-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: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 150 LELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATA 229
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 230 KVQQLEEDIVSVTHKAIEKETDL--DSLKDKLRKAQHEREQL-ECQLQTEKDEKELYKVhLKNTEIENTKLVSEIQTLKN 306
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELkQTQKSLKKKQEEKQEL-IDQKEKEKKDLIKEIEEKEK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 307 LDGNKESMITHFKEEISKLQSCLADKENLYRALllttsnKEDTLFLKEQLRKaeeqVQATRQELIFLTKELSDAVNVRDK 386
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKL------KQEVKQIKETIKE----IRNKWPEIIKKIKESKTKIDDIIE 680
|
....
gi 568942384 387 TMAD 390
Cdd:TIGR04523 681 LMKD 684
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-582 |
4.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 204 KGLLEVSQSL--RVEN-EEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLEcqlqtekdek 280
Cdd:PRK03918 165 KNLGEVIKEIkrRIERlEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE---------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 281 ELyKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISKLQSCLAD------KENLYRALllttsnKEDTLFLKE 354
Cdd:PRK03918 235 EL-KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkeKAEEYIKL------SEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 355 QLRKAEEQVQATRQELIFLTKELSDAVNVRdktmadlhtARLEN-ERVKKQLADTLAELQLHAVKKDQAstnsvftkkmg 433
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKE---------ERLEElKKKLKELEKRLEELEERHELYEEA----------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 434 SQQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTK---DHVCEMTKEIAEK---IEKYNK-------CKQLLQD 500
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISkitARIGELKKEIKELkkaIEELKKakgkcpvCGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 501 EKTK--CNKYAEELAKMELKWKEQVKIAENVKLELAEVED----------NYKV--QLAEKEKEINGLAsyLENLSREKE 566
Cdd:PRK03918 448 EHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeselikLKELaeQLKELEEKLKKYN--LEELEKKAE 525
|
410
....*....|....*.
gi 568942384 567 LTKSLEdQKGRKLEGQ 582
Cdd:PRK03918 526 EYEKLK-EKLIKLKGE 540
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
177-585 |
4.43e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 177 QLREQVGRMERELSQEKGRCEQLQAEQKGLLEvsQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAIEKETDLDSLK 256
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 257 DKLRKAQHEREQLECQLQTEKD------------EKELYKVHLKNTEIENTKLVSEIQTLKNLDGNKESMITHFKEEISK 324
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRLLQTlhsqeihirdahEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 325 LQSCLADKENLYRALLLTTSNKEDTlfLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKT------MADLHTARLEN 398
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLkereqqLQTKEQIHLQE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 399 ERVKKQLADTLAELQ----------LHAVKKDQASTNSvftkkmGSQQKVNDASINTDPAASTSASAVDVKPAASCAETG 468
Cdd:TIGR00618 486 TRKKAVVLARLLELQeepcplcgscIHPNPARQDIDNP------GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 469 FDMSTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAEnvkLELAEVEDNYKVQLAEKE 548
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQDLQDVRLHLQQ 636
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568942384 549 ------KEINGLASYLENLSREKELTKSLEDQKGRKLEGQSPQ 585
Cdd:TIGR00618 637 csqelaLKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-306 |
4.57e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQK--GLLEVSQSLRVENEEFMKRYSDATAKVQ---QLEEDIVSVTHKA 245
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAEL 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568942384 246 IEKETDLDSLKDKLRKAQHER-EQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKN 306
Cdd:COG4717 173 AELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-577 |
4.86e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 338 ALLLTTSNKEDTLFLKEQLRKAEEQVQATRQELIFLTKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAV 417
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 418 KKDQASTNSVFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAETGFDMSTKDHvcEMTKEIAEKIEKYNKCKQL 497
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR--EQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 498 LQDEKTKCNKYAEELAKMELKWKEQVKIAENVKLELAEVEDNYKVQLAEKEKEINGLASYLENLSRE------KELTKSL 571
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEaaaaaeRTPAAGF 248
|
....*.
gi 568942384 572 EDQKGR 577
Cdd:COG4942 249 AALKGK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-281 |
5.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 168 IAVLEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSL------------RVENEEFMKRYSDATAKVQQLE 235
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaereIAELEAELERLDASSDDLAALE 691
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568942384 236 EDIVSVTHKAIEKETDLDSLKDKLRKAQHEREQLECQLQTEKDEKE 281
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-593 |
5.89e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 315 ITHFKEEISKLQSCLAD-KENLYRAlllttsnkEDTLF-LKEQLRKAEEQVQATrQELIFLTKELSDA---VNVRDKTma 389
Cdd:TIGR02168 167 ISKYKERRKETERKLERtRENLDRL--------EDILNeLERQLKSLERQAEKA-ERYKELKAELRELelaLLVLRLE-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 390 DLHTARLENERVKKQLADTLAELQLHAVKKDQAST------NSVFTKKMGSQQKVNDASI------NTDPAASTSASAVD 457
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEelrlevSELEEEIEELQKELYALANeisrleQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 458 VKPAASCAETGFDMSTKDHVCEMTKEIAEKIEKYNKCKQLLQDEKTKcnkYAEELAKMELKWKEQVKIAENVKLELAEVE 537
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE---LEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568942384 538 DnykvQLAEKEKEINGLASYLENLSREKELTKSLEDQKGRKLEGQSPQQVSRCLNT 593
Cdd:TIGR02168 393 L----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
476-573 |
7.54e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 476 HVCEMTKEI-AEKIEKY-------NKCKQLLQDEKTKCNKYAEELAKME-LKWKEQVKIAENvklELAEVEDNYKvqlaE 546
Cdd:PRK05771 32 HIEDLKEELsNERLRKLrslltklSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEE---ELEKIEKEIK----E 104
|
90 100
....*....|....*....|....*..
gi 568942384 547 KEKEINGLASYLENLSREKELTKSLED 573
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPWGN 131
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-559 |
8.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATAKVQQLEEDIVSVTHKAiekeT 250
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----D 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 251 DLDSLKDKLRKaqhEREQLECQLQTEKDEKELYKvhlknTEIEntKLVSEIQTLKNLDGNKEsmiTHFKEEISKLQSCLA 330
Cdd:PRK02224 353 DLEERAEELRE---EAAELESELEEAREAVEDRR-----EEIE--ELEEEIEELRERFGDAP---VDLGNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 331 DKENLY-RALLLTTSNKEdtlfLKEQLRKAEEQVQATR-----QELifltKE------LSDAVNVRDKTMADLHTARLEN 398
Cdd:PRK02224 420 ERDELReREAELEATLRT----ARERVEEAEALLEAGKcpecgQPV----EGsphvetIEEDRERVEELEAELEDLEEEV 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 399 ERVKKQL--ADTLAELQLHAVKKDQASTNS---VFTKKMGSQQKVNDASINTDPAASTSASAVDVKPAASCAEtgfdmst 473
Cdd:PRK02224 492 EEVEERLerAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE------- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 474 kdhvcEMTKEIAEKIEKYNKCKQLLQDEKTKCNKYAEELAKMELKWKEQVKIAENVKlELAEVEDNYKVQLAEKEKEING 553
Cdd:PRK02224 565 -----EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE-ALAELNDERRERLAEKRERKRE 638
|
....*.
gi 568942384 554 LASYLE 559
Cdd:PRK02224 639 LEAEFD 644
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-309 |
9.08e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 149 LLELKIEKTLKEKEELLKLIAVLEKETAQLREQVGRMERELSQEKGRCEQLQAE-------QKGLLEVSQSLRVENEEFM 221
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQiekkrkrLSELKAKLEALEEELSEIE 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 222 KR-------------YSDATAKVQQLEEDIVS---VTHKAIEK----ETDLDSLKDKLRKAQHEREQLecQLQTEKDEKE 281
Cdd:TIGR02169 938 DPkgedeeipeeelsLEDVQAELQRVEEEIRAlepVNMLAIQEyeevLKRLDELKEKRAKLEEERKAI--LERIEEYEKK 1015
|
170 180
....*....|....*....|....*...
gi 568942384 282 LYKVHLKNTEIENTKLVSEIQTLKNLDG 309
Cdd:TIGR02169 1016 KREVFMEAFEAINENFNEIFAELSGGTG 1043
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-284 |
9.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 171 LEKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLrvenEEFMKRYSDATAK-VQQLEEDIVSVTHKAIEKE 249
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL----EELLEQLSLATEEeLQDLAEELEELQQRLAELE 212
|
90 100 110
....*....|....*....|....*....|....*
gi 568942384 250 TDLDSLKDKLRKAQHEREQLECQLQTEKDEKELYK 284
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-306 |
9.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942384 172 EKETAQLREQVGRMERELSQEKGRCEQLQAEQKGLLEVSQSLRVEneefmkRYSDATAKVQQLEEDIVSVTHKAIEKETD 251
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568942384 252 LDSLKDKLRKAQ----HEREQLECQLQTEKDEKELYKVHLKNTEIENTKLVSEIQTLKN 306
Cdd:COG4913 361 RARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
|
| |
