|
Name |
Accession |
Description |
Interval |
E-value |
| DOT1 |
pfam08123 |
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ... |
112-314 |
6.53e-107 |
|
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.
Pssm-ID: 149273 Cd Length: 205 Bit Score: 339.28 E-value: 6.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 112 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 190
Cdd:pfam08123 1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 191 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 269
Cdd:pfam08123 81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958790070 270 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 314
Cdd:pfam08123 161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
|
|
| CC_DOT1L |
cd20902 |
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ... |
478-542 |
3.41e-35 |
|
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.
Pssm-ID: 411016 [Multi-domain] Cd Length: 65 Bit Score: 128.58 E-value: 3.41e-35
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790070 478 ALQKLLESFKIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLF 542
Cdd:cd20902 1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
503-656 |
3.36e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.23 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQLLGTAQQLfshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 579
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790070 580 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 656
Cdd:COG4372 113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
503-656 |
2.99e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQL------LGTAQQLFSHCQAQ----KEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEI 566
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLsekqkeLEQNNKKIKELEKQlnqlKSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 567 SAHNQ---QLREQSEQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCL 633
Cdd:TIGR04523 331 SQNNKiisQLNEQISQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQK 410
|
170 180
....*....|....*....|...
gi 1958790070 634 ELQISIVELEKTQRQQELLQLKS 656
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKE 433
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
471-656 |
1.03e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 55.00 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 471 LVAPTPPALQKLLESFKIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLfSHCQAQKEEIRRLFQQKLDEL 549
Cdd:pfam12795 63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRP-ERAQQQLSEARQRLQQIRNRL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 550 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 628
Cdd:pfam12795 137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210
|
170 180
....*....|....*....|....*...
gi 1958790070 629 QRhclelqisiVELEKTQRQQELLQLKS 656
Cdd:pfam12795 211 RL---------QEAEQAVAQTEQLAEEA 229
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
781-1122 |
2.09e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.78 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 781 SQDHTGASKAATSEPHPRPEHAKENSLPYQSPGLSNSMKLSPQDPPLASPATSPLTSERGSEKGVKERAYSSHGetitSL 860
Cdd:PHA03307 99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA----AL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 861 PVSIPLSTVQPnklpVSIPLASVVlPSRAERARSTPSPVPQPRDSSSTLEKQIgASTHGAGGAAAGSRSLTVAPTGFYAG 940
Cdd:PHA03307 175 PLSSPEETARA----PSSPPAEPP-PSTPPAAASPRPPRRSSPISASASSPAP-APGRSAADDAGASSSDSSSSESSGCG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 941 SVAISGALASSPAPLASGMESAVFEESSGPSSLFGTMGSRSTPPQHPPLLPQSRNSGPASPAHQLAASPRLSVTTQGSLP 1020
Cdd:PHA03307 249 WGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1021 DTGKGELPADPAFSDPESEAkrrivfsiSAGASSRQSPSTRHSPltsgtrgdcvqshgqdsRKRSRRKRASAGTPSLTTG 1100
Cdd:PHA03307 329 TSSSSESSRGAAVSPGPSPS--------RSPSPSRPPPPADPSS-----------------PRKRPRPSRAPSSPAASAG 383
|
330 340
....*....|....*....|..
gi 1958790070 1101 VSPKRRALPTVAGLFTQSSGSP 1122
Cdd:PHA03307 384 RPTRRRARAAVAGRARRRDATG 405
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
474-651 |
2.13e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 474 PTPPALQKLLESFKIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFSHCQAQKEEIRRL--- 541
Cdd:PRK11281 36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 542 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 611
Cdd:PRK11281 110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958790070 612 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 651
Cdd:PRK11281 177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
479-639 |
6.37e-04 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 42.64 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 479 LQKLLESFKIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfshcqaQKEEIRRLFQQKLDELGVKALTynd 558
Cdd:cd16855 27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 559 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 621
Cdd:cd16855 91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151
|
170
....*....|....*...
gi 1958790070 622 RSQISEKQRHCLELQISI 639
Cdd:cd16855 152 RQQIKRAERLKQKLPIPL 169
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
536-644 |
1.93e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 536 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 610
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226
|
90 100 110
....*....|....*....|....*....|....
gi 1958790070 611 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 644
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
156-264 |
2.49e-03 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 39.34 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 156 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 234
Cdd:cd02440 2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69
|
90 100 110
....*....|....*....|....*....|..
gi 1958790070 235 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 264
Cdd:cd02440 70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DOT1 |
pfam08123 |
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ... |
112-314 |
6.53e-107 |
|
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.
Pssm-ID: 149273 Cd Length: 205 Bit Score: 339.28 E-value: 6.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 112 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 190
Cdd:pfam08123 1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 191 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 269
Cdd:pfam08123 81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958790070 270 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 314
Cdd:pfam08123 161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
|
|
| CC_DOT1L |
cd20902 |
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ... |
478-542 |
3.41e-35 |
|
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.
Pssm-ID: 411016 [Multi-domain] Cd Length: 65 Bit Score: 128.58 E-value: 3.41e-35
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790070 478 ALQKLLESFKIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLF 542
Cdd:cd20902 1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
503-656 |
3.36e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.23 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQLLGTAQQLfshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 579
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790070 580 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 656
Cdd:COG4372 113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
503-656 |
8.42e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQLLGTAQQLfshcQAQKEEIRRLfQQKLDelgvkaltyndliQAQKEISAHNQQLREQSEQLEK 582
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQL-EEELE-------------QARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790070 583 DNSELRS--QSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 656
Cdd:COG4372 92 AQAELAQaqEELESLQEEAEELQEE-----LEELQKERQDLEQQRKQ-----LEAQIAELQSEIAEREEELKELEE 157
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
503-656 |
2.99e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQL------LGTAQQLFSHCQAQ----KEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEI 566
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLsekqkeLEQNNKKIKELEKQlnqlKSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 567 SAHNQ---QLREQSEQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCL 633
Cdd:TIGR04523 331 SQNNKiisQLNEQISQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQK 410
|
170 180
....*....|....*....|...
gi 1958790070 634 ELQISIVELEKTQRQQELLQLKS 656
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKE 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-689 |
1.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 501 QYKANLQQLLDQEKEKNTQLLGTAQQLfSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 580
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 581 EKDNSELRSQSLRLLRARcEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKScvpp 660
Cdd:COG1196 392 LRAAAELAAQLEELEEAE-EALLER-----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL---- 461
|
170 180
....*....|....*....|....*....
gi 1958790070 661 dDALSLHLRGKGALGRELESDAGRLRLEL 689
Cdd:COG1196 462 -LELLAELLEEAALLEAALAELLEELAEA 489
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
471-656 |
1.03e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 55.00 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 471 LVAPTPPALQKLLESFKIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLfSHCQAQKEEIRRLFQQKLDEL 549
Cdd:pfam12795 63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRP-ERAQQQLSEARQRLQQIRNRL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 550 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 628
Cdd:pfam12795 137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210
|
170 180
....*....|....*....|....*...
gi 1958790070 629 QRhclelqisiVELEKTQRQQELLQLKS 656
Cdd:pfam12795 211 RL---------QEAEQAVAQTEQLAEEA 229
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-655 |
2.39e-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: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 501 QYKANLQQLLDQEKEKNTQLLGTAQQLfSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 580
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAEL-QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790070 581 EKDNSELRSQSLRLLRARcEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEK--TQRQQELLQLK 655
Cdd:TIGR02168 315 ERQLEELEAQLEELESKL-DELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
501-654 |
2.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 501 QYKANLQQLLDQEKEKNT------------QLLGTAQQLFSHCQAQKEEIRRL--FQQKLDELGVKALTYNDLIQAQKEI 566
Cdd:COG4717 89 EYAELQEELEELEEELEEleaeleelreelEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 567 SAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQ 646
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-----LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
....*...
gi 1958790070 647 RQQELLQL 654
Cdd:COG4717 244 RLKEARLL 251
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
483-656 |
7.23e-07 |
|
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: 54.26 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 483 LESFKIQYLQFLAYTKTPQYKANLQQLLDQeKEKNTQLLGTAQQLFSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA 562
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISEL-KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 563 QKEISAHNQQLREQSEQLEKDNSELRSqslrlLRARCEElrlDWSTL---SLENLRKEKQALRSQISEKQRHCLEL--QI 637
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKEQ---DWNKElksELKNQEKKLEEIQNQISQNNKIISQLneQI 344
|
170 180 190
....*....|....*....|....*....|...
gi 1958790070 638 SIVELEKT--------------QRQQELLQLKS 656
Cdd:TIGR04523 345 SQLKKELTnsesensekqreleEKQNEIEKLKK 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
485-688 |
1.87e-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: 53.20 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 485 SFKIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLlgtaqQLFSHCQAQKEEIRRLFQQKLDELGVKALTyndLIQAQK 564
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMT---LESSER 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 565 EISAHNQQLREQSEQLEKDNSE---LRSQ----------------SLRLLRARCEELRLDWSTLS--LENLRKEKQALRS 623
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEitkLRSRvdlklqelqhlknegdHLRNVQTECEALKLQMAEKDkvIEILRQQIENMTQ 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790070 624 QISEKQRHCLELQISIVELEK--TQRQQELLQLKscVPPDDalslhlrgKGALGRELESDAGRLRLE 688
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKeiNDRRLELQEFK--ILKDK--------KDAKIRELEARVSDLELE 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-653 |
2.70e-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: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 501 QYKANLQQLLDQEKEKNTQL------LGTAQQLFSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLR 574
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLeeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 575 EQSEQLEKDNSELRSQsLRLLRARCEELrldwsTLSLENLRKEKQALRSQISEKQRHCLELQISIV--ELEKTQRQQELL 652
Cdd:TIGR02168 386 SKVAQLELQIASLNNE-IERLEARLERL-----EDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERL 459
|
.
gi 1958790070 653 Q 653
Cdd:TIGR02168 460 E 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
478-688 |
2.97e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 478 ALQKLLESFKIQyLQFLAYTktpQYKANLQQLLDQEKEKNTQLLGTAQQLfSHCQAQKEEIRRLFQQKLDELGVKALTYN 557
Cdd:COG1196 217 ELKEELKELEAE-LLLLKLR---ELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 558 ----DLIQAQKEISAHNQQLREQSEQLEKDNSELRS--QSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRH 631
Cdd:COG1196 292 ellaELARLEQDIARLEERRRELEERLEELEEELAEleEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790070 632 CLELQISIVELEKT--QRQQELLQLKScvppdDALSLHLRGKGALGRELESDAGRLRLE 688
Cdd:COG1196 367 LLEAEAELAEAEEEleELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLE 420
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
503-655 |
1.45e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.45 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRL-------------FQQKLDELGVKA-------LTYNDLIQA 562
Cdd:pfam12795 4 ELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYqkalddapaelreLRQELAALQAKAeaapkeiLASLSLEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 563 QKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCE-----------ELRLDWSTLSLENLRK--------EKQALRS 623
Cdd:pfam12795 84 EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQlsearqrlqqiRNRLNGPAPPGEPLSEaqrwalqaELAALKA 163
|
170 180 190
....*....|....*....|....*....|..
gi 1958790070 624 QISEKQrhcLELQISIVELEKTQRQQELLQLK 655
Cdd:pfam12795 164 QIDMLE---QELLSNNNRQDLLKARRDLLTLR 192
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
506-650 |
1.75e-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: 48.99 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 506 LQQLLDQEKEKNTQLLGTAQQLfshcqAQKEEIRRLFQQKLDELGVKALTY------------NDLIQAQKEISAHNQQL 573
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaEELRADLAELAALRAEL 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790070 574 REQSEQLEKDNSELRSQSLRLLRARCEELRLdwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQE 650
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
495-654 |
1.91e-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: 49.68 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 495 AYTKTPQYKANLQQLLDQEKEKNTQLlgtaqqlfSHCQAQKEEIRRLFQQKLDELGVkaltyndliqAQKEISAhnqqLR 574
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKREL--------SSLQSELRRIENRLDELSQELSD----------ASRKIGE----IE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 575 EQSEQLEKDnselrsqsLRLLRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELL 652
Cdd:TIGR02169 723 KEIEQLEQE--------EEKLKERLEELEEDLSSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
|
..
gi 1958790070 653 QL 654
Cdd:TIGR02169 795 EI 796
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
781-1122 |
2.09e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.78 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 781 SQDHTGASKAATSEPHPRPEHAKENSLPYQSPGLSNSMKLSPQDPPLASPATSPLTSERGSEKGVKERAYSSHGetitSL 860
Cdd:PHA03307 99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA----AL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 861 PVSIPLSTVQPnklpVSIPLASVVlPSRAERARSTPSPVPQPRDSSSTLEKQIgASTHGAGGAAAGSRSLTVAPTGFYAG 940
Cdd:PHA03307 175 PLSSPEETARA----PSSPPAEPP-PSTPPAAASPRPPRRSSPISASASSPAP-APGRSAADDAGASSSDSSSSESSGCG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 941 SVAISGALASSPAPLASGMESAVFEESSGPSSLFGTMGSRSTPPQHPPLLPQSRNSGPASPAHQLAASPRLSVTTQGSLP 1020
Cdd:PHA03307 249 WGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1021 DTGKGELPADPAFSDPESEAkrrivfsiSAGASSRQSPSTRHSPltsgtrgdcvqshgqdsRKRSRRKRASAGTPSLTTG 1100
Cdd:PHA03307 329 TSSSSESSRGAAVSPGPSPS--------RSPSPSRPPPPADPSS-----------------PRKRPRPSRAPSSPAASAG 383
|
330 340
....*....|....*....|..
gi 1958790070 1101 VSPKRRALPTVAGLFTQSSGSP 1122
Cdd:PHA03307 384 RPTRRRARAAVAGRARRRDATG 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
536-658 |
2.09e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 536 EEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQ-SLRLLRARCEELR--LDWSTLSLE 612
Cdd:COG4717 71 KELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEaeLAELPERLE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958790070 613 NLRKEKQA---LRSQISEKQRHCLELQISIVELEKTQRQQELLQLKSCV 658
Cdd:COG4717 150 ELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
540-653 |
2.21e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 540 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARcEEL-----RLDWSTLSLENL 614
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958790070 615 RKEKQALRSQISEKQRHCLELQIsivELEKTQRQQELLQ 653
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQE---ELEELQKERQDLE 128
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
512-696 |
2.57e-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: 49.40 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 512 QEKEKNTQLL----GTAQQLFSHCQAQKEEIRRLFQQKLDELgvKALtyndLIQAQKEISAHNQQLREQSEqLEKDNSEL 587
Cdd:pfam01576 204 QELEKAKRKLegesTDLQEQIAELQAQIAELRAQLAKKEEEL--QAA----LARLEEETAQKNNALKKIRE-LEAQISEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 588 RS--QSLRLLRARCEELRLDwstlslenLRKEKQALRSQISEKQRHCLELQisivELeKTQRQQELLQLKSCVPPD---- 661
Cdd:pfam01576 277 QEdlESERAARNKAEKQRRD--------LGEELEALKTELEDTLDTTAAQQ----EL-RSKREQEVTELKKALEEEtrsh 343
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958790070 662 DALSLHLRGKGA-----LGRELESdAGRLRLELDCAKLSL 696
Cdd:pfam01576 344 EAQLQEMRQKHTqaleeLTEQLEQ-AKRNKANLEKAKQAL 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-656 |
3.89e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 506 LQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLfQQKLDELGVKALTY--------NDLIQAQKEISAHNQQLREQS 577
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLrerlesleRRIAATERRLEDLEEQIEELS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 578 EQLEKDNSELRSQSLRL----------------LRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQrhcleLQISI 639
Cdd:TIGR02168 852 EDIESLAAEIEELEELIeeleseleallnerasLEEALALLRSELEELSeeLRELESKRSELRRELEELR-----EKLAQ 926
|
170
....*....|....*..
gi 1958790070 640 VELEKTQRQQELLQLKS 656
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQE 943
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
506-630 |
5.42e-05 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 45.00 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 506 LQQLLD---QEKEKNTQLLGTAQQLFSHCQAQkeeIRRLFQQKlDELGVKALTYNDLIQAQKEISAHNQQLReqseQLEK 582
Cdd:TIGR02473 4 LQKLLDlreKEEEQAKLELAKAQAEFERLETQ---LQQLIKYR-EEYEQQALEKVGAGTSALELSNYQRFIR----QLDQ 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958790070 583 DNSELRsQSLRLLRARCEELRLDWSTL-----SLENLrKEKQALRSQISEKQR 630
Cdd:TIGR02473 76 RIQQQQ-QELALLQQEVEAKRERLLEArrelkALEKL-KEKKQKEYRAEEAKR 126
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
529-690 |
7.90e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 529 SHCQAQKEE-IRRLF--QQKLDELgvkaltyNDLIqaqKEISAHNQQLREQSEQLEKdnselrsqsLRLLRARCEELRLD 605
Cdd:TIGR02168 168 SKYKERRKEtERKLErtRENLDRL-------EDIL---NELERQLKSLERQAEKAER---------YKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 606 WSTLSLENLRKEKQALRSQISEKQRHCLELQisiveLEKTQRQQELLQLKSCVPPDDALSLHLRGK----GALGRELESD 681
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELT-----AELQELEEKLEELRLEVSELEEEIEELQKElyalANEISRLEQQ 303
|
....*....
gi 1958790070 682 AGRLRLELD 690
Cdd:TIGR02168 304 KQILRERLA 312
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
504-653 |
1.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 504 ANLQQLLDQEKEKNTQLLgtaqqlfshCQAQKEEIRRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLREQSEQ 579
Cdd:COG4717 347 EELQELLREAEELEEELQ---------LEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958790070 580 LEkdnSELRSQSLRLLRARceelrldwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQ 653
Cdd:COG4717 418 LE---ELLEALDEEELEEE------------LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
474-651 |
2.13e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 474 PTPPALQKLLESFKIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFSHCQAQKEEIRRL--- 541
Cdd:PRK11281 36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 542 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 611
Cdd:PRK11281 110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958790070 612 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 651
Cdd:PRK11281 177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-696 |
2.41e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 495 AYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFSH---CQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAH-- 569
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAea 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 570 ---------------NQQLREQSEQLEKDNSELRS--QSLRLLRARCEELRLDWSTlSLENLRKEKQALRSQISEKQRHC 632
Cdd:TIGR02168 783 eieeleaqieqlkeeLKALREALDELRAELTLLNEeaANLRERLESLERRIAATER-RLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790070 633 LELQISIVELEKtqRQQELLQLKSCVppDDALSLHLRGKGALG---RELESDAGRLRLELDCAKLSL 696
Cdd:TIGR02168 862 EELEELIEELES--ELEALLNERASL--EEALALLRSELEELSeelRELESKRSELRRELEELREKL 924
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
501-653 |
2.64e-04 |
|
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: 45.66 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 501 QYKANLQQLLDqEKEKNTQLLGTAQQLFSHCQAQKEEIRRL------FQQKLDELG--------VKALTYNDLIQAQKEI 566
Cdd:pfam07888 203 QRDTQVLQLQD-TITTLTQKLTTAHRKEAENEALLEELRSLqerlnaSERKVEGLGeelssmaaQRDRTQAELHQARLQA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 567 SAHNQQL-------RE-------------QSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLEnLRKEKQALRSQIS 626
Cdd:pfam07888 282 AQLTLQLadaslalREgrarwaqeretlqQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE-LGREKDCNRVQLS 360
|
170 180 190
....*....|....*....|....*....|..
gi 1958790070 627 EKQRHCLELQISIVELEKTQRQ-----QELLQ 653
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQlqaekQELLE 392
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
508-653 |
3.05e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.38 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 508 QLLDQE---KEKNTQLLGTAQQLFSHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEKD 583
Cdd:pfam08614 11 RLLDRTallEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQEL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790070 584 NSELRSQS--LRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-QELLQ 653
Cdd:pfam08614 91 EKKLREDErrLAALEAERAQLeeKLKDREEELREKRKLNQDLQDELVA-----LQLQLNMAEekLRKLEKEnRELVE 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
497-700 |
3.89e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 497 TKTPQYKanlqQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQ 576
Cdd:TIGR00618 173 FPLDQYT----QLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 577 SEQLEKDNSelRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRHCLELQISIVEL------EKTQRQQE 650
Cdd:TIGR00618 249 REAQEEQLK--KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhtelqsKMRSRAKL 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958790070 651 LLQLKSCVppddALSLHLRGKGALGRELESDAGRLRLELDCAKLSLPHLS 700
Cdd:TIGR00618 327 LMKRAAHV----KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
508-655 |
4.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 508 QLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLFQQKLDELgvkaltynDLIQAQKEISAHNQQLreqsEQLEKDNSEL 587
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAELEAEL----ERLDASSDDL 687
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 588 RSqslrllrarceelrldwstlslenLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQRQQELLQLK 655
Cdd:COG4913 688 AA------------------------LEEQLEELEAELEelEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
510-656 |
5.76e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 510 LDQEKEKNTQLlgtaQQLFshcqaqKEEIRRLfQQKLDELGVKaltYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRS 589
Cdd:TIGR04523 129 LEKQKKENKKN----IDKF------LTEIKKK-EKELEKLNNK---YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790070 590 QSLRLlrarceELRLdwstLSLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 656
Cdd:TIGR04523 195 KLLKL------ELLL----SNLKKKIQKNKSLESQISE-----LKKQNNQLKDNIEKKQQEINEKTT 246
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
494-653 |
5.93e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 494 LAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQL------FSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEIS 567
Cdd:PRK10246 280 LAALSLAQPARQLRPHWERIQEQSAALAHTRQQIeevntrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFR 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 568 AHNQQL---REQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSL---------------ENLRKEKQALRSQISEKQ 629
Cdd:PRK10246 360 QWNNELagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLtadevaaalaqhaeqRPLRQRLVALHGQIVPQQ 439
|
170 180
....*....|....*....|....*.
gi 1958790070 630 RHCLELQISIVEL--EKTQRQQELLQ 653
Cdd:PRK10246 440 KRLAQLQVAIQNVtqEQTQRNAALNE 465
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
507-655 |
6.25e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 507 QQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIR-RLFQQKLDELGVKaltyNDLIQAQKEI-------SAHNQQLREQSE 578
Cdd:pfam13868 175 REEIEEEKEREIARLRAQQEKAQDEKAERDELRaKLYQEEQERKERQ----KEREEAEKKArqrqelqQAREEQIELKER 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 579 QLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQ-------ALRSQISEKQRHCL-ELQISIVELEKTQRQQE 650
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDEEIE-----QEEAEKRRMkrlehrrELEKQIEEREEQRAaEREEELEEGERLREEEA 325
|
....*
gi 1958790070 651 LLQLK 655
Cdd:pfam13868 326 ERRER 330
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
479-639 |
6.37e-04 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 42.64 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 479 LQKLLESFKIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfshcqaQKEEIRRLFQQKLDELGVKALTynd 558
Cdd:cd16855 27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 559 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 621
Cdd:cd16855 91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151
|
170
....*....|....*...
gi 1958790070 622 RSQISEKQRHCLELQISI 639
Cdd:cd16855 152 RQQIKRAERLKQKLPIPL 169
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
506-627 |
6.49e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 506 LQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRrlfqQKLDELGVKALTYndlIQAQKEIsahnQQLREQSEQLEKDNS 585
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR----ARIKELAARAPAW---LAAQDAL----ERLREQSGEALADSQ 626
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958790070 586 ELRSQSLRLLRarceelRLDWSTLSLENLRKEKQALRSQISE 627
Cdd:COG3096 627 EVTAAMQQLLE------REREATVERDELAARKQALESQIER 662
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
504-627 |
9.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 504 ANLQQLLDQEKEKNTQLLGTAQQlfshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQLreqsEQLEKD 583
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDE-----EELEEELEEL-EEELEEL------EEELEELREELAELEAEL----EQLEED 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790070 584 N--SELRsQSLRLLRARCEELRLDWSTLSL---------ENLRKEKQ-ALRSQISE 627
Cdd:COG4717 469 GelAELL-QELEELKAELRELAEEWAALKLalelleearEEYREERLpPVLERASE 523
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
506-679 |
1.01e-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: 43.96 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 506 LQQLLDQEKEKNTQllgtAQQLFSHCQAQ-----------KEEIRRLFQQKLDELGVKA-----LTYNDLIQAQKEISAH 569
Cdd:pfam05557 137 LQERLDLLKAKASE----AEQLRQNLEKQqsslaeaeqriKELEFEIQSQEQDSEIVKNskselARIPELEKELERLREH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 570 NQQLREQSEQLEKDNSELRSQSLRLlrARCEELRLDWSTLSLENLRKEkQALRSQISEKQRHCLELQISIVELEK-TQRQ 648
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKL--EREEKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRSPEDLSRRiEQLQ 289
|
170 180 190
....*....|....*....|....*....|.
gi 1958790070 649 QELLQLKSCVPPDDALSLHLRgkgALGRELE 679
Cdd:pfam05557 290 QREIVLKEENSSLTSSARQLE---KARRELE 317
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
792-1327 |
1.10e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 792 TSEPHPRP------EHAKENSLPYQS-------------PGLSNSMKLSPQDPPLASPATSPltSERGSEKGVKERAYSS 852
Cdd:PHA03247 2570 PPRPAPRPsepavtSRARRPDAPPQSarprapvddrgdpRGPAPPSPLPPDTHAPDPPPPSP--SPAANEPDPHPPPTVP 2647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 853 HGETITSLP----VSIPLSTVQPNKLPVSI--------PLASVVLPSRAERARS-TPSPVPQPRDSSSTlekqigasthg 919
Cdd:PHA03247 2648 PPERPRDDPapgrVSRPRRARRLGRAAQASsppqrprrRAARPTVGSLTSLADPpPPPPTPEPAPHALV----------- 2716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 920 aggaaagsrSLTVAPTGFYAGSVAiSGALASSPAPLASGMESAVFEESSGPSSLFGTMGSRStppqhppllpqsrnsgPA 999
Cdd:PHA03247 2717 ---------SATPLPPGPAAARQA-SPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA----------------PA 2770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1000 SPAHQLAASPRLSVTTQGSLPDTGKGELPADPAFSDPESEAKRRivfsiSAGASSRQSPSTRHSPLTSGTrgdcvqshgq 1079
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP-----AAALPPAASPAGPLPPPTSAQ---------- 2835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1080 dsrKRSRRKRASAGTPSLTTGVS-----PKRRALPTVAGLFTQSSGSPLNLTSM----VSNINQPLEITAISSPESSLKS 1150
Cdd:PHA03247 2836 ---PTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKPAAPARPPVRRLarpaVSRSTESFALPPDQPERPPQPQ 2912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1151 SPTPYQDHDQPPVLRKERPLGPTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLVGRKPVPS 1230
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1231 GEPVNSSKWKSTFSPISDLGLAKAMDSPLQASSALSHSPlfsfrPSLEEPAAEAKPSTHPRKSFAGSLAAAEGP--SPGT 1308
Cdd:PHA03247 2993 TPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPP-----DDTEDSDADSLFDSDSERSDLEALDPLPPEphDPFA 3067
|
570
....*....|....*....
gi 1958790070 1309 NPPNSLAFSGGLAADLGLH 1327
Cdd:PHA03247 3068 HEPDPATPEAGARESPSSQ 3086
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
507-656 |
1.25e-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: 43.47 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 507 QQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIR---RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKD 583
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 584 NSELRsqslrllrarceelrldwstLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-----QELLQLKS 656
Cdd:TIGR04523 449 DSVKE--------------------LIIKNLDNTRESLETQLKV-----LSRSINKIKqnLEQKQKElkskeKELKKLNE 503
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
536-644 |
1.93e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 536 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 610
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226
|
90 100 110
....*....|....*....|....*....|....
gi 1958790070 611 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 644
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
506-636 |
2.38e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 506 LQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLfQQKLDELGVKAltynDLIQAQK-EISAhnqqLREQSEQLEK-- 582
Cdd:pfam05622 64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLEL-QHRNEELTSLA----EEAQALKdEMDI----LRESSDKVKKle 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790070 583 -----------DNSELRSQsLRLLrarcEELRLDW--STLSLENLRKEKQALRSQISEKQRHCLELQ 636
Cdd:pfam05622 135 atvetykkkleDLGDLRRQ-VKLL----EERNAEYmqRTLQLEEELKKANALRGQLETYKRQVQELH 196
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
156-264 |
2.49e-03 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 39.34 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 156 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 234
Cdd:cd02440 2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69
|
90 100 110
....*....|....*....|....*....|..
gi 1958790070 235 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 264
Cdd:cd02440 70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
478-655 |
3.03e-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: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 478 ALQKLLESFKIQYlqflaYTKTPQYKANLQQLLDQEKEKntqllgtAQQLFSHCQAQKEE--IRRLF-QQKLDELGVKAL 554
Cdd:COG4913 159 ALKARLKKQGVEF-----FDSFSAYLARLRRRLGIGSEK-------ALRLLHKTQSFKPIgdLDDFVrEYMLEEPDTFEA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 555 -------------TYNDLIQAQK------EISAHNQQLREQSEQLEKdNSELRS--------QSLRLLRARCEELRLDWS 607
Cdd:COG4913 227 adalvehfddlerAHEALEDAREqiellePIRELAERYAAARERLAE-LEYLRAalrlwfaqRRLELLEAELEELRAELA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790070 608 TL---------SLENLRKEKQALRSQISE-----KQRhcLELQISIVELEKTQRQQELLQLK 655
Cdd:COG4913 306 RLeaelerleaRLDALREELDELEAQIRGnggdrLEQ--LEREIERLERELEERERRRARLE 365
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
500-649 |
4.03e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.16 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 500 PQYKAnLQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEirrlfQQKLdelgvkaltyndLIQAQKEISAHNQQLREQSEQ 579
Cdd:pfam04849 164 VQLDA-LQEKLRGLEEENLKLRSEASHLKTETDTYEEK-----EQQL------------MSDCVEQLSEANQQMAELSEE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 580 LEKDNSELRSQ-----SLRL----LRARCEELRLDWSTLSLE-NLRKEKQ-ALRSQISE-KQRH--CLELQISIVELEKT 645
Cdd:pfam04849 226 LARKMEENLRQqeeitSLLAqivdLQHKCKELGIENEELQQHlQASKEAQrQLTSELQElQDRYaeCLGMLHEAQEELKE 305
|
....
gi 1958790070 646 QRQQ 649
Cdd:pfam04849 306 LRKK 309
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
503-636 |
4.33e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.16 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 503 KANLQQLLDQEKEKNTQLLGTAQQLFSHCQAQKEEIRRLfQQKldelgvkaltYNDLIQAQKEISAHNQQLREQSEQLEK 582
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-QQN----------YERELVLHAEDIKALQALREELNELKA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958790070 583 DNSELRSQsLRLLRARCEELRLDWStlslenlrKEKQALRSQISEKQRHCLELQ 636
Cdd:pfam07926 72 EIAELKAE-AESAKAELEESEESWE--------EQKKELEKELSELEKRIEDLN 116
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
500-650 |
6.31e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 500 PQYKANLQQLLDQEKEK-------------NTQLLGTAQQLFshcqaqkeEIRRLFQQKLDELGVKALTYNDLIQAQKEI 566
Cdd:PRK10929 78 PKLSAELRQQLNNERDEprsvppnmstdalEQEILQVSSQLL--------EKSRQAQQEQDRAREISDSLSQLPQQQTEA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 567 sahNQQLREQSEQL-----------EKDNSELRSQSLRLlRARCEELRLdwSTLSLENlRKEKQALRSQISEKQRHCLEL 635
Cdd:PRK10929 150 ---RRQLNEIERRLqtlgtpntplaQAQLTALQAESAAL-KALVDELEL--AQLSANN-RQELARLRSELAKKRSQQLDA 222
|
170
....*....|....*.
gi 1958790070 636 QISIVE-LEKTQRQQE 650
Cdd:PRK10929 223 YLQALRnQLNSQRQRE 238
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
796-1311 |
9.12e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 796 HPRPEHAKENSLPYQSPGLSNSMKLSPQDPPLASPATSPLTSERGSEKGVKERAYS-SHG-ETITSLPVSIPlstvqpnk 873
Cdd:PHA03247 2480 YRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMLTwIRGlEELASDDAGDP-------- 2551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 874 lpvSIPLASVVLPSRAERARSTPSPVPQPrdssstLEKQIGASTHGAGGAAAGSRSLT-VAPTGFYAGSVAisgalASSP 952
Cdd:PHA03247 2552 ---PPPLPPAAPPAAPDRSVPPPRPAPRP------SEPAVTSRARRPDAPPQSARPRApVDDRGDPRGPAP-----PSPL 2617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 953 APLASGMESAVFEESSGPSSLFGTMGSRSTPPQHPPLLPQSRNSGPASPAHQLAASPRLSVTTQGSLPDTGKGELPADPA 1032
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1033 FSDPESEAKrrivfsisagassrqSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLT-TGVSPKRRALPTV 1111
Cdd:PHA03247 2698 LADPPPPPP---------------TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPT 2762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1112 aglfTQSSGSPLNLTSMVSNINQPLEITAISSPESSLKSSPTPYQDHDQPPVLRKERPLGPTNGAHYSPLTsdeePGSED 1191
Cdd:PHA03247 2763 ----TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP----PPTSA 2834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 1192 EPSSArierkiatiSLESKSPPKTLENGGGLVGRKPVPSGEPVNSSKWKSTFSP-ISDLGLAKAMDSPLQASSALSHSPL 1270
Cdd:PHA03247 2835 QPTAP---------PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArPPVRRLARPAVSRSTESFALPPDQP 2905
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958790070 1271 fsfrPSLEEPAAEAKPSTHPRKSFAGSLAAAEGPSPGTNPP 1311
Cdd:PHA03247 2906 ----ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
561-655 |
9.21e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790070 561 QAQKEISAHNQ-QLREQSEQLEKDNSELRSQsLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISI 639
Cdd:pfam10473 30 ERELEMSEENQeLAILEAENSKAEVETLKAE-IEEMAQNLRDLELD-----LVTLRSEKENLTKELQKKQERVSELESLN 103
|
90
....*....|....*...
gi 1958790070 640 VELEK--TQRQQELLQLK 655
Cdd:pfam10473 104 SSLENllEEKEQEKVQMK 121
|
|
| |
