|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
17-120 |
8.67e-49 |
|
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: 167.42 E-value: 8.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 17 VIFQNVAKSYLPNAHLECHYTLTPYIHPHPKDWVGIFKVGWSTARDYYTFLWSpmPEHYVEGSAVNCELAFQGYYLPNDD 96
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 528946901 97 GEFYQFCYVTHKGEIRGASTPFQF 120
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
125-460 |
7.21e-36 |
|
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: 142.34 E-value: 7.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 125 PVEELLTME-----DEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAV------------------LEKETTQLREQ 181
Cdd:pfam07888 2 PLDELVTLEeeshgEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAanrqrekekerykrdreqWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 182 VGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKK 261
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 262 AQcereqleCQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQFSLAEKEnlQRTFLL 341
Cdd:pfam07888 162 AG-------AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH--RKEAEN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 342 TTsskedtfiLKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELK-------- 413
Cdd:pfam07888 233 EA--------LLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegrarwaq 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 414 -----LSAVNKDQEKTDTLEHELRREVEDL--------KLRLQMAADhykekfKECQRLQ 460
Cdd:pfam07888 305 eretlQQSAEADKDRIEKLSAELQRLEERLqeermereKLEVELGRE------KDCNRVQ 358
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
150-448 |
5.04e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTS 229
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIEntkLVSEVQTLKNLDG 309
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 310 NKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMA 389
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 528946901 390 DLHTAHLENEKVKKQLTDALAELklsavnkdQEKTDTLEHELRREVEDLKLRLQMAADH 448
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALL--------EAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-468 |
4.19e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 145 TKAGLLELK--IEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKK 222
Cdd:TIGR02168 668 TNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 223 RYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQ 302
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 303 TLKNLDGNKENMITHFKEEISRLQFSLAE-----------KENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEav 371
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESlaaeieeleelIEELESELEALLNERASLEEALALLRSELEELSEELRE-- 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 372 fLAKELSDAVNVRDKTMADLHTAHLENEKVK---KQLTDALAE---LKLSAVNKDQEKTDTLEHELRREVEDLKLRLQ-- 443
Cdd:TIGR02168 906 -LESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKel 984
|
330 340 350
....*....|....*....|....*....|
gi 528946901 444 -----MAADHYKEKFKECQRLQKQINKLSD 468
Cdd:TIGR02168 985 gpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-632 |
3.62e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKAL 206
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 207 TKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCERE-------QLECQLKTEKDE 279
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 280 KELYKVHLKNTEIENTKLVSEVQTLknldgNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEdtfILKEQLRKA 359
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEEL-----LKKLEEAELKELQAELEELEEELEELQEELERLEEALE---ELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 360 EEQIQATRQE--------------------------AVFLAKE--------LSDAVNVRDKTMADLHTA---HL-----E 397
Cdd:TIGR02168 474 EQALDAAERElaqlqarldslerlqenlegfsegvkALLKNQSglsgilgvLSELISVDEGYEAAIEAAlggRLqavvvE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 398 NEKVKKQLTDALAELKLSAVN---KDQEKTDTLEHELRREVEDLKLRLQMAADHykEKFKEcqRLQKQINKLSDQSANSN 474
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDL--VKFDP--KLRKALSYLLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 475 SVftkkigsqQKVNDASINTDPAATASTVDVKPL-PSTAETDFDNLTKGQVSEMTKEIADKTEKYNKCKQLLQDEKTKCN 553
Cdd:TIGR02168 630 DL--------DNALELAKKLRPGYRIVTLDGDLVrPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528946901 554 KYADELAKMElkwkEQVKIAENIKLELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKLEGQNSQ 632
Cdd:TIGR02168 702 ELRKELEELE----EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
783-809 |
8.34e-12 |
|
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: 59.88 E-value: 8.34e-12
10 20
....*....|....*....|....*..
gi 528946901 783 KVCPMCSEQFPPDYDQQVFERHVQTHF 809
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
756-782 |
8.59e-12 |
|
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: 59.97 E-value: 8.59e-12
10 20
....*....|....*....|....*..
gi 528946901 756 KKCPLCELMFPPNYDQSKFEEHVESHW 782
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
758-781 |
3.40e-11 |
|
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: 58.20 E-value: 3.40e-11
10 20
....*....|....*....|....
gi 528946901 758 CPLCELMFPPNYDQSKFEEHVESH 781
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
155-639 |
3.99e-10 |
|
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: 63.59 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 155 EKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKryndvtskalql 234
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 235 eediVSVTHKAIEKEteldslkdkLKKAQCEREQLecqLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGNKEnm 314
Cdd:pfam05483 343 ----AKAAHSFVVTE---------FEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE-- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 315 ithfkEEISRLQFSLAEKENLqrtfllttsskedtFILKEQLRKAEEQIQATRQEAVFLakelsdaVNVRDKTMADLHTA 394
Cdd:pfam05483 405 -----VELEELKKILAEDEKL--------------LDEKKQFEKIAEELKGKEQELIFL-------LQAREKEIHDLEIQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 395 HLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEH---------ELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINK 465
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdklllenkELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 466 LSDQSAN----SNSVFTKKIGSQQKVN---DASINTDPAATASTVDVKPLPSTAETDFDNLTKgQVSEMTKEIADKTEKY 538
Cdd:pfam05483 539 LEEKEMNlrdeLESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKK-QIENKNKNIEELHQEN 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 539 NKCKQLLQDEKTKCNKYADELAKMELKwkeqvkiAENIKLELAEVVDNYklqlaEKEKEISGLTSywENLSREKEHKRSV 618
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELE-------LASAKQKFEEIIDNY-----QKEIEDKKISE--EKLLEEVEKAKAI 683
|
490 500
....*....|....*....|.
gi 528946901 619 ENQAERKLEGQNSQSPHQISQ 639
Cdd:pfam05483 684 ADEAVKLQKEIDKRCQHKIAE 704
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
158-473 |
4.99e-09 |
|
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: 59.99 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 158 MKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERgdqlQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEED 237
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA----KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 238 ivsvthKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGNKENMITH 317
Cdd:pfam02463 245 ------LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 318 FKEEISRLQfslaEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKElsdavnvRDKTMADLHTAHLE 397
Cdd:pfam02463 319 SEKEKKKAE----KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE-------ELLAKKKLESERLS 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528946901 398 NEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQMaadhyKEKFKECQRLQKQINKLSDQSANS 473
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE-----EEESIELKQGKLTEEKEELEKQEL 458
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
157-563 |
5.80e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 157 TMKEKEellKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKAltkvSQSLKMENEEfkkryndvtskalqlEE 236
Cdd:pfam15921 504 SLQEKE---RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE----CEALKLQMAE---------------KD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 237 DIVSVTHKAIEKETELDSLKDK------LKKAQCERE----QLECQ----LKTEKDEK--ELyKVHLKNTEIENTKLVS- 299
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagamqVEKAQLEKEindrRLELQefkiLKDKKDAKirEL-EARVSDLELEKVKLVNa 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 300 ---EVQTLKNLDGNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTF-ILKEQLRKAEEQIQATRQE------ 369
Cdd:pfam15921 641 gseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTnKLKMQLKSAQSELEQTRNTlksmeg 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 370 --------AVFLAKELS------DAVNVRDKTMADLHT-AHLENEKVKKQLTDALAELKLSAVNKDQE--KTDTLEHELR 432
Cdd:pfam15921 721 sdghamkvAMGMQKQITakrgqiDALQSKIQFLEEAMTnANKEKHFLKEEKNKLSQELSTVATEKNKMagELEVLRSQER 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 433 REVEDLKlRLQMAADHYKEKFKECQRLqkqINKLSDQSANSNSVFTKKIGSQQkvndasintDPAATASTvDVKPL---P 509
Cdd:pfam15921 801 RLKEKVA-NMEVALDKASLQFAECQDI---IQRQEQESVRLKLQHTLDVKELQ---------GPGYTSNS-SMKPRllqP 866
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528946901 510 STAETDFDNLTKGQVS------EMTKEIADKTEKYNKCKQLLQDEKTKCNKY-ADELAKME 563
Cdd:pfam15921 867 ASFTRTHSNVPSSQSTasflshHSRKTNALKEDPTRDLKQLLQELRSVINEEpTVQLSKAE 927
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-380 |
6.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKAL 206
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 207 TKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVH 286
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 287 LKNTEIENTKLVSEVQTLKnldgnkenmithfKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQAT 366
Cdd:COG1196 402 LEELEEAEEALLERLERLE-------------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250
....*....|....
gi 528946901 367 RQEAVFLAKELSDA 380
Cdd:COG1196 469 LEEAALLEAALAEL 482
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
783-809 |
8.41e-09 |
|
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: 51.49 E-value: 8.41e-09
10 20
....*....|....*....|....*..
gi 528946901 783 KVCPMCSEQFPPDYDQQVFERHVQTHF 809
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
785-808 |
9.85e-09 |
|
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: 51.03 E-value: 9.85e-09
10 20
....*....|....*....|....
gi 528946901 785 CPMCSEQFPPDYDQQVFERHVQTH 808
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
151-443 |
2.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 151 ELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVsqsLKMENEEFKK----RYND 226
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDlgeeEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 227 VTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCER-------EQLECQLKTEKDEKELYKVHLKNTEIENTKLVS 299
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 300 EVQTLKNLDGNKENMITHFKEEISRLQFSLAE-KENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELS 378
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINElKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528946901 379 DAVNVRDKTMADLhtahlenEKVKKQLTDALAElkLSAVNKDQektdtleHELRREVEDLKLRLQ 443
Cdd:TIGR02169 452 KQEWKLEQLAADL-------SKYEQELYDLKEE--YDRVEKEL-------SKLQRELAEAEAQAR 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-627 |
2.23e-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: 57.72 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKErgdQLQAEQKALTKVsQSLKMENEEFKKRYNDVTS 229
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN---KLLKLELLLSNL-KKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNldG 309
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--Q 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 310 NKENMITHFKEEIsrlqfslaekenlqrtflltTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNvrdktma 389
Cdd:TIGR04523 304 KEQDWNKELKSEL--------------------KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 390 dlhtahlENEKVKKQLTDALAELKlSAVNKDQEKTDTLEhELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:TIGR04523 357 -------ENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 470 SANSNSVFTKKigsqqkvndasintdpaatastvdvkplpstaetdfdnltKGQVSEMTKEIADKTEKYNKCKQLLQDEK 549
Cdd:TIGR04523 428 IERLKETIIKN----------------------------------------NSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 550 TKCNKYADELAKMELKWKE---QVKIAENIKLELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKL 626
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
.
gi 528946901 627 E 627
Cdd:TIGR04523 548 N 548
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
149-475 |
2.51e-08 |
|
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: 57.67 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 149 LLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLK------MENEEFKK 222
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKqeiekeEEKLAQVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 223 RYNDVTSKALQLEEDIVSVTHKAIEKEtELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQ 302
Cdd:pfam02463 272 KENKEEEKEKKLQEEELKLLAKEEEEL-KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 303 TLKNLDGNKENMithfkeeiSRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVN 382
Cdd:pfam02463 351 REAEEEEEEELE--------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 383 VRDKTMADlhtahLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKfKECQRLQKQ 462
Cdd:pfam02463 423 EEKKEELE-----ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE-LLLSRQKLE 496
|
330
....*....|...
gi 528946901 463 INKLSDQSANSNS 475
Cdd:pfam02463 497 ERSQKESKARSGL 509
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
785-808 |
4.01e-08 |
|
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: 49.34 E-value: 4.01e-08
10 20
....*....|....*....|....
gi 528946901 785 CPMCSEQFPPDYDQQVFERHVQTH 808
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-469 |
6.17e-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: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHeKERGDQLQAEQ-------------------KALTKVSQSL 213
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKreyegyellkekealerqkEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 214 KMENEEFKKRYNDVTSKALQLEEDIVSVTHKaIEKETELDSL--KDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTE 291
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKK-IKDLGEEEQLrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 292 IENTKLVSEvqtlknldgnkenmITHFKEEISRLQfslAEKENLQRTFlltTSSKEDTFILKEQLRKAEEQIQATRQEAV 371
Cdd:TIGR02169 329 AEIDKLLAE--------------IEELEREIEEER---KRRDKLTEEY---AELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 372 FLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELK--LSAVNKDQEKTDTLEHELRREVEDLKLRLQMAADHY 449
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340
....*....|....*....|...
gi 528946901 450 KEKFK---ECQRLQKQINKLSDQ 469
Cdd:TIGR02169 469 QELYDlkeEYDRVEKELSKLQRE 491
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
758-781 |
6.56e-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: 48.72 E-value: 6.56e-08
10 20
....*....|....*....|....
gi 528946901 758 CPLCELMFPPNYDQSKFEEHVESH 781
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-596 |
1.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 145 TKAGLLELKIEKTMKEKEELLK----LIAVLEKETTQLREQVGRMErELNHEKERGDQLQAEQKALTKVSQslkmeneEF 220
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIReleeRIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR-------EI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 221 KKRYNDVTSKALQLEEDIvsvtHKAIEKETELDSLKDKLKKAQCEREQLEC------QLKTEKDEKELYKVHLKNTEIEN 294
Cdd:PRK03918 313 EKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 295 ------------TKLVSEVQTLKNLDGNKENMITHFKEEISRLQ------------FSLAEKENLQRTFLLTTSSkedtf 350
Cdd:PRK03918 389 lekeleelekakEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLEEYTAELKR----- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 351 iLKEQLRKAEEQIQATRQEAVFLAKELSdavnvRDKTMADLHTAHLENEKVKKQLTDALAElKLSAVNKDQEKTDTLEHE 430
Cdd:PRK03918 464 -IEKELKEIEEKERKLRKELRELEKVLK-----KESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 431 LRREVEDLKLRLQMAADHYKE------KFKECQ-RLQKQINKLSDQSANSNSVFTKKIGSQQKVNDASINTDPAAT---A 500
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKlaelekKLDELEeELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKeleR 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 501 STVDVKPLPSTAETDFDNL--TKGQVSEMTKEIADKTEKYNKckqllQDEKTKCNKYAdELAKMELKWKEQVKIAENIKL 578
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELaeTEKRLEELRKELEELEKKYSE-----EEYEELREEYL-ELSRELAGLRAELEELEKRRE 690
|
490
....*....|....*...
gi 528946901 579 ELAEVVDNYKLQLAEKEK 596
Cdd:PRK03918 691 EIKKTLEKLKEELEEREK 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-463 |
1.37e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKAL 232
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 233 QLEEDIVSVTHKAIEKetELDSLKDKLKKAQCEREQLECQLKTEKDEKELYK---------VHLKNTEIEntKLVSEVQT 303
Cdd:TIGR02169 797 QAELSKLEEEVSRIEA--RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqiksiekeIENLNGKKE--ELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 304 LKNLDGNKENMITHFKEEISRLQfslAEKENLQRtfllttsSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVnv 383
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELE---AQLRELER-------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK-- 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 384 rdKTMADLHTAHLENEKVKKQLTDALAEL-KLSAVNKDQEktDTLEHELRR--EVEDLKLRLQMAADHYKEKFKECQRLQ 460
Cdd:TIGR02169 941 --GEDEEIPEEELSLEDVQAELQRVEEEIrALEPVNMLAI--QEYEEVLKRldELKEKRAKLEEERKAILERIEEYEKKK 1016
|
...
gi 528946901 461 KQI 463
Cdd:TIGR02169 1017 REV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
153-582 |
1.43e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKEELLKLIAVLEKETTQLREQVGRMErELNHEKERGDQLQAEQKALTKvsqslkmenEEFKKRYNDVTSKAL 232
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTP---------EKLEKELEELEKAKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 233 QLEEDIVSVTHKAIEKETELDSLKD---KLKKAQ-----CEREQlecqlkTEKDEKEL---YKVHLKNTEIENTKLVSEV 301
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKaieELKKAKgkcpvCGREL------TEEHRKELleeYTAELKRIEKELKEIEEKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 302 QTLKNLDGNKENMITHfKEEISRLQFSLAEKENLQRTflLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAv 381
Cdd:PRK03918 476 RKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 382 NVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEH------ELR---REVEDLKLRLQMAADHYKEK 452
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyneylELKdaeKELEREEKELKKLEEELDKA 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 453 FKECQRLQKQINKLSDQSANSNSVFTKKigSQQKVNDASINTDPAATASTVDVKPLPS---TAETDFDNLtKGQVSEMtK 529
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKrreEIKKTLEKL-KEELEER-E 707
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 528946901 530 EIADKTEKYNKCKQLLQDEKTKCNKYADELAKMELkwKEQVKIAENIKLELAE 582
Cdd:PRK03918 708 KAKKELEKLEKALERVEELREKVKKYKALLKERAL--SKVGEIASEIFEELTE 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-468 |
1.76e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 171 LEKETTQLREQVGRMERELNhekergdQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKET 250
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELS-------SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 251 ELDSLKDKLKKAQCEREQLECQLktEKDEKELYKVHLKNTEIENTKLVSEVQtlknldgNKENMITHFKEEISRLQFSLA 330
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLSHSRIP-------EIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 331 EKE-NLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFL----------AKELSDAVNVRDKTMADL------HT 393
Cdd:TIGR02169 816 EIEqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLngkkeeleeeLEELEAALRDLESRLGDLkkerdeLE 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528946901 394 AHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELrREVEDLKLRLQ--MAADHYKEKFK-ECQRLQKQINKLSD 468
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKGEDEeiPEEELSLEDVQaELQRVEEEIRALEP 972
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-627 |
1.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENE---EFKKRYND 226
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkirELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 227 VTSKALQLEEDIVSVthKAIEKETE--------LDSLKDKLKKAQCEREQLECQLKT--------EKDEKELYKVHLKNT 290
Cdd:PRK03918 271 LKKEIEELEEKVKEL--KELKEKAEeyiklsefYEEYLDELREIEKRLSRLEEEINGieerikelEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 291 EIEN-----TKLVSEVQTLKNLDGNKENMITHFK----EEISR-LQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAE 360
Cdd:PRK03918 349 ELEKrleelEERHELYEEAKAKKEELERLKKRLTgltpEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 361 EQIQATRQEAVFLAKELSDavNVRDKTMADlHTAHLEN-EKVKKQLTDALAELKLSAVNKD----QEKTDTLEHELRREV 435
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTE--EHRKELLEE-YTAELKRiEKELKEIEEKERKLRKELRELEkvlkKESELIKLKELAEQL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 436 EDLKLRLQ-MAADHYKEKFKECQRLQKQINKLSDQSANSNSVFTKKIGSQQKVNDASINTDpaatastvDVKPLPSTAET 514
Cdd:PRK03918 506 KELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD--------ELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 515 DFDNLTKGQVSEMTKEIADKTEKYNK------CKQLLQDEKTKCNKYADELAKMELKWKEQVKIAENIKLELAEVVDNY- 587
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYs 657
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 528946901 588 -------KLQLAEKEKEISGLTSYWENL-SREKEHKRSVENQAERKLE 627
Cdd:PRK03918 658 eeeyeelREEYLELSRELAGLRAELEELeKRREEIKKTLEKLKEELEE 705
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-630 |
1.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 151 ELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQkalTKVSQSLKMENEEFKKRYNDVTSK 230
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE---AKKKAEEAKKADEAKKKAEEAKKK 1498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 231 ALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKvhlKNTEIENTKLVSEVQTLKNLDGN 310
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK---KAEELKKAEEKKKAEEAKKAEED 1575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 311 KENMITHFKE----EISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDK 386
Cdd:PTZ00121 1576 KNMALRKAEEakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 387 TMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQ---MAADHYKEKFKECQRLQKQI 463
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekKKAEELKKAEEENKIKAEEA 1735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 464 NKLSDQSANSNSVFTKKIGSQQKVNDASINTDPAATASTVDVKPLPSTAETDFDNLTKGQVSEMTKEIADKTEkynkckq 543
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA------- 1808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 544 LLQDEKTKCNKYADELAKMELKWKEQVKIAENIKLELAEVVDNYKLQL-----------AEKEKEISGLTSYWENLSREK 612
Cdd:PTZ00121 1809 NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKnnengedgnkeADFNKEKDLKEDDEEEIEEAD 1888
|
490
....*....|....*...
gi 528946901 613 EHKRSVENQAERKLEGQN 630
Cdd:PTZ00121 1889 EIEKIDKDDIEREIPNNN 1906
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-469 |
5.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLE--KETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDV 227
Cdd:COG4717 107 LEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 228 TSKAL----QLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYK------------------- 284
Cdd:COG4717 187 SLATEeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglgg 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 285 ------------------------VHLKNTEIENTKLVSEVQTLKNLDGNKENMITHFKEEisrlqfsLAEKENLQRTFL 340
Cdd:COG4717 267 sllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAA-------LGLPPDLSPEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 341 LTTSSK-EDTFILKEQLRKAEEQIQATRQEAVFlaKELSDAVNVRDKTM-ADLHTAHLENEKVKKQLTDALAELKLSAVN 418
Cdd:COG4717 340 LELLDRiEELQELLREAEELEEELQLEELEQEI--AALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528946901 419 KDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:COG4717 418 LEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-648 |
2.22e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 149 LLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNhekergdQLQAEQKALTKVSQSLKMENEEFKKRYNDVT 228
Cdd:TIGR04523 201 LLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN-------EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 229 SKALQLEEDIvsvthkaIEKETELDSLKDKLKKAQCEREQ-LECQLKTEKDEKELYKVHLKNTEIENTKLVSEvqtLKNL 307
Cdd:TIGR04523 274 KELEQNNKKI-------KELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQ---LNEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 308 DGNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFI-LKEQLRKAEEQIQATRQEAVFLA---KELSDAVNV 383
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnLESQINDLESKIQNQEKLNQQKDeqiKKLQQEKEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 384 RDKTMADLHTAHLENEKVKKQLTDALAELKLSAvnkdqEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQI 463
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELII-----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 464 NKLSDQ---SANSNSVFTKKIgSQQKVNDASINTDPAATAStvDVKPLPSTAETDFDNLTKgqvSEMTKEIADKTEKYNK 540
Cdd:TIGR04523 499 KKLNEEkkeLEEKVKDLTKKI-SSLKEKIEKLESEKKEKES--KISDLEDELNKDDFELKK---ENLEKEIDEKNKEIEE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 541 CKQlLQDEKTKCNKYADELAKmelkwkeqvkiaeniklELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVEN 620
Cdd:TIGR04523 573 LKQ-TQKSLKKKQEEKQELID-----------------QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
490 500
....*....|....*....|....*...
gi 528946901 621 QAERKLEGQNsQSPHQISQCLKTSSEKS 648
Cdd:TIGR04523 635 NIKSKKNKLK-QEVKQIKETIKEIRNKW 661
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
151-610 |
2.31e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 151 ELKIEKTMKEKeellkliaVLEKETTQLrEQVGRMEreLNHE----KERGDQLQAEQKALTKVSQSLKMENEEFKKRYND 226
Cdd:pfam15921 153 ELEAAKCLKED--------MLEDSNTQI-EQLRKMM--LSHEgvlqEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 227 VTSKALQLEEDIVSVTHKAIEKETELDSLKDKlkkaqcEREQLECQLKTEKDEKELYkvhLKNTEIENTKLVSEVQTLKN 306
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSE------SQNKIELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 307 ldgnKENMIThfkeeiSRLQFSLAEKENLQRTFLLTTSSKEDTFI-LKEQLRKA----EEQIQATRQEAVFLAKELSDAV 381
Cdd:pfam15921 293 ----QANSIQ------SQLEIIQEQARNQNSMYMRQLSDLESTVSqLRSELREAkrmyEDKIEELEKQLVLANSELTEAR 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 382 NVRD--------------KTMADLHTAH----LENEKvKKQLTDalaelklsavnKDQEKTDTLEHeLRREVEDLKLRLQ 443
Cdd:pfam15921 363 TERDqfsqesgnlddqlqKLLADLHKREkelsLEKEQ-NKRLWD-----------RDTGNSITIDH-LRRELDDRNMEVQ 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 444 MAADHYKEKFKECQ-RLQKQINKLS--DQSANSNSVFTKKIGSQQKVNDASINTDPAATAStvdvkpLPSTAETdfdnlt 520
Cdd:pfam15921 430 RLEALLKAMKSECQgQMERQMAAIQgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT------LESSERT------ 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 521 kgqVSEMTKEIADKtekyNKCKQLLQDEKTKCNKYADelakMELKWKEQVKIAENIKLELAEVVDNYKLQLAEKEKEISG 600
Cdd:pfam15921 498 ---VSDLTASLQEK----ERAIEATNAEITKLRSRVD----LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
490
....*....|
gi 528946901 601 LTSYWENLSR 610
Cdd:pfam15921 567 LRQQIENMTQ 576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-416 |
2.76e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 194 ERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQL 273
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 274 KTEKDE-KELYKVHLKNTEIENTKLV----SEVQTLKNLDGNKEnMITHFKEEISRLQfslAEKENLQRtfllttssked 348
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKY-LAPARREQAEELR---ADLAELAA----------- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528946901 349 tfiLKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLhtahlenEKVKKQLTDALAELKLSA 416
Cdd:COG4942 165 ---LRAELEAERAELEALLAELEEERAALEALKAERQKLLARL-------EKELAELAAELAELQQEA 222
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-627 |
2.77e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTS 229
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 230 KalQLEEDIVSVTHKAIEKETELD-------SLKDKLKKAQCEREQLEC--------------QLKTEKDEKELYKVHLK 288
Cdd:TIGR04523 310 K--ELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESensekqreleekqnEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 289 NTEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQfslAEKENLqrtfllttssKEDTFILKEQLRKAEEQIQATRQ 368
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---KEIERL----------KETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 369 EAVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELK-LSAVNKDQEKTDTlehELRREVEDLKLRLQMAAD 447
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKkLNEEKKELEEKVK---DLTKKISSLKEKIEKLES 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 448 HYKEKFKECQRLQKQINKlsDQSANSNSVFTKKIGSQQKVNDASINTDPAATASTVDVKPLPSTAETDFDNLTKG----- 522
Cdd:TIGR04523 532 EKKEKESKISDLEDELNK--DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEieeke 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 523 -QVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADELAKMelkwKEQVKiaeNIKLELAEVVDNYKlQLAEKEKEISGL 601
Cdd:TIGR04523 610 kKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI----KETIK---EIRNKWPEIIKKIK-ESKTKIDDIIEL 681
|
490 500
....*....|....*....|....*....
gi 528946901 602 TSYWEN---LSREKEHKRSVENQAERKLE 627
Cdd:TIGR04523 682 MKDWLKelsLHYKKYITRMIRIKDLPKLE 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
160-648 |
6.45e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 160 EKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIV 239
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 240 SVTHKAIEKETELDSLKDKLKKaqcereqlecqlktekDEKELYKV--HLKNTEIENTKLVSEVQTLKNLDGNKENMITH 317
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKE----------------NKKNIDKFltEIKKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 318 FKEEISRLQFSLAeKENLQRTFLLTTSSKEDTFI-----LKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLH 392
Cdd:TIGR04523 178 LEKEKLNIQKNID-KIKNKLLKLELLLSNLKKKIqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 393 TAHLENEKVKKQLTDalaelKLSAVNKDQEKTDTLEHELRR-EVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSA 471
Cdd:TIGR04523 257 QLKDEQNKIKKQLSE-----KQKELEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 472 NSN---SVFTKKIGSQQKVNDASINT----DPAATASTVDVKPLPSTAETDFDNLT--KGQVSEMTKEIaDKTEKYNKCK 542
Cdd:TIGR04523 332 QNNkiiSQLNEQISQLKKELTNSESEnsekQRELEEKQNEIEKLKKENQSYKQEIKnlESQINDLESKI-QNQEKLNQQK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 543 Q----LLQDEKTKCNKYADELAKMELKWKEQVKIAENIKLELAEVVDN-------YKLQLAEKEKEISGLTSYWENLSRE 611
Cdd:TIGR04523 411 DeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntresLETQLKVLSRSINKIKQNLEQKQKE 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 528946901 612 ---KEHKRSVENQAERKLEGQNSQSPHQISQCLKT----SSEKS 648
Cdd:TIGR04523 491 lksKEKELKKLNEEKKELEEKVKDLTKKISSLKEKieklESEKK 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-640 |
6.92e-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: 50.06 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQS-----LKMENEEFKKRY 224
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEEL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 225 NDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLEcQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTL 304
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE-RLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 305 KNLD------------GNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSK------EDTFILKEQ---------LR 357
Cdd:TIGR02168 529 ISVDegyeaaieaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgteiqgNDREILKNIegflgvakdLV 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 358 KAEEQIQATRQEA---VFLAKELSDAVNVRDKTMA---------DLHTAH---------------------LENEKVKKQ 404
Cdd:TIGR02168 609 KFDPKLRKALSYLlggVLVVDDLDNALELAKKLRPgyrivtldgDLVRPGgvitggsaktnssilerrreiEELEEKIEE 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 405 LTDALAELK--LSAVNKDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANSNSvftKKIG 482
Cdd:TIGR02168 689 LEEKIAELEkaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEE 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 483 SQQKVNDASintdPAATASTVDVKPLPSTAETDfdnltKGQVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADELAKM 562
Cdd:TIGR02168 766 LEERLEEAE----EELAEAEAEIEELEAQIEQL-----KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 563 ELKWKEQVKIAENIKLELAEV---VDNYKLQLAEKEKEISGLT----SYWENLSREKEHKRSVENQaERKLEGQNSQSPH 635
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLneraSLEEALALLRSELEELSEE-LRELESKRSELRR 915
|
....*
gi 528946901 636 QISQC 640
Cdd:TIGR02168 916 ELEEL 920
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
158-627 |
1.41e-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: 48.95 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 158 MKEKEELLKLIAVLEKETTQLREQVGRMERELnheKERGDQLQAEQK---ALTKVSQSLKMENEEFkkryndvtskALQL 234
Cdd:pfam05483 70 FENSEGLSRLYSKLYKEAEKIKKWKVSIEAEL---KQKENKLQENRKiieAQRKAIQELQFENEKV----------SLKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 235 EEDIVSvtHKAIEKETELDSLKDKLKKAQCEREqlecqlkTEKDEKELYkvhlkntEIENTKlvsevQTLKNLDGNKENM 314
Cdd:pfam05483 137 EEEIQE--NKDLIKENNATRHLCNLLKETCARS-------AEKTKKYEY-------EREETR-----QVYMDLNNNIEKM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 315 ITHFKEeiSRLQfslAEKENLQRTFllttsskedtfilkeQLRKAEEQIQatrqeavFLAKELSDAVNVRDKTMADLHTA 394
Cdd:pfam05483 196 ILAFEE--LRVQ---AENARLEMHF---------------KLKEDHEKIQ-------HLEEEYKKEINDKEKQVSLLLIQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 395 HLENEKVKKQLTDALAELKlSAVNKDQEKT----------DTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQIN 464
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESR-DKANQLEEKTklqdenlkelIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 465 KLSDQSANSNSVFTKKigsqqKVNDASINTDPAATASTVDvkPLPSTAETDFDNlTKGQVSEMTKEIADKTEKYNKCKQL 544
Cdd:pfam05483 328 QLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLE--ELLRTEQQRLEK-NEDQLKIITMELQKKSSELEEMTKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 545 LQDEKTKCNKYADELAKME--LKWKEQV-KIAENIK---LELAEVVDNYKLQLAEKEKEISGLTSYWENLSRE-KEHKRS 617
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEklLDEKKQFeKIAEELKgkeQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEvEDLKTE 479
|
490
....*....|
gi 528946901 618 VENQAERKLE 627
Cdd:pfam05483 480 LEKEKLKNIE 489
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
150-282 |
1.65e-05 |
|
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: 47.70 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMEREL----NHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYN 225
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELrqlkQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 528946901 226 DVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKkaqcereqlECQLKTEKDEKEL 282
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLE---------QCRGFTFKEIEKL 276
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-621 |
1.83e-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: 48.63 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 169 AVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEfkkryNDVTSKALQLEEdiVSVTHKAIEK 248
Cdd:pfam01576 64 ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-----EEAARQKLQLEK--VTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 249 ETELDSLKDKLKKAQCEREQLECQLK------TEKDE--KELYKVHLKN----TEIENtKLVSEVQTLKNLDGNKENM-- 314
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLEERISeftsnlAEEEEkaKSLSKLKNKHeamiSDLEE-RLKKEEKGRQELEKAKRKLeg 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 315 -ITHFKEEISRLQFSLAEkenlqrtfllttsskedtfiLKEQLRKAEEQIQAT----------RQEAVFLAKELSDAVNV 383
Cdd:pfam01576 216 eSTDLQEQIAELQAQIAE--------------------LRAQLAKKEEELQAAlarleeetaqKNNALKKIRELEAQISE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 384 RDKTMADLHTAHLENEKVKKQLTDALAELKLSAvnKDQEKTDTLEHELR----REVEDLKLRLQMAADHYKEKFKEC-QR 458
Cdd:pfam01576 276 LQEDLESERAARNKAEKQRRDLGEELEALKTEL--EDTLDTTAAQQELRskreQEVTELKKALEEETRSHEAQLQEMrQK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 459 LQKQINKLSDQ----SANSNSVFTKKIGSQQKVNDASINTDPAATASTvDVKPLPSTAETDFDNLtKGQVSEMTKEIADK 534
Cdd:pfam01576 354 HTQALEELTEQleqaKRNKANLEKAKQALESENAELQAELRTLQQAKQ-DSEHKRKKLEGQLQEL-QARLSESERQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 535 TEKYNKCK-------QLLQDEKTKCNKYADELAKMElkwkEQVKIAENIKLELAEVVDNYKLQLAEKEKEISGLTsywEN 607
Cdd:pfam01576 432 AEKLSKLQselesvsSLLNEAEGKNIKLSKDVSSLE----SQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ---EQ 504
|
490
....*....|....
gi 528946901 608 LSREKEHKRSVENQ 621
Cdd:pfam01576 505 LEEEEEAKRNVERQ 518
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-488 |
1.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 149 LLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVT 228
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 229 SKALQLEEDIVSVT---HKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKD--EKELYKVHLKNTEIENTKLVSEVQT 303
Cdd:COG4372 108 EEAEELQEELEELQkerQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 304 LKNlDGNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNV 383
Cdd:COG4372 188 LLK-EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 384 RDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEktdtLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQI 463
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA----ALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
330 340
....*....|....*....|....*
gi 528946901 464 NKLSDQSANSNSVFTKKIGSQQKVN 488
Cdd:COG4372 343 LQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
152-537 |
2.08e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 152 LKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKE-------RGDQLQAEQKALTKVSQSL--KMENEEFKK 222
Cdd:COG5022 803 LSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliqkfgRSLKAKKRFSLLKKETIYLqsAQRVELAER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 223 RYNDvtskalqLEEDIVSVTHKAiEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKelYKVHLKNTEIENT------- 295
Cdd:COG5022 883 QLQE-------LKIDVKSISSLK-LVNLELESEIIELKKSLSSDLIENLEFKTELIAR--LKKLLNNIDLEEGpsieyvk 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 296 -----KLVSEVQTLKNLDGNKENMITHFKEEISRLQFSLAEKENLQRTfLLTTSSKEDTFILKEQLRKAEEQIQATRQEA 370
Cdd:COG5022 953 lpelnKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKE-LAELSKQYGALQESTKQLKELPVEVAELQSA 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 371 VFLAKELSDAVNVRdKTMADLHTAH-LENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQmAADHY 449
Cdd:COG5022 1032 SKIISSESTELSIL-KPLQKLKGLLlLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVT-NRNLV 1109
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 450 KEKFKeCQRLQKQINKL-----SDQSANSNSVFTKKIGSQQKVND--ASINTDPAATASTVDVKPLPSTAETD------F 516
Cdd:COG5022 1110 KPANV-LQFIVAQMIKLnllqeISKFLSQLVNTLEPVFQKLSVLQleLDGLFWEANLEALPSPPPFAALSEKRlyqsalY 1188
|
410 420
....*....|....*....|.
gi 528946901 517 DNLTKGQVSEMtKEIADKTEK 537
Cdd:COG5022 1189 DEKSKLSSSEV-NDLKNELIA 1208
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-596 |
2.22e-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: 48.13 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 288 KNTEIENtkLVSEVQTLKNLDGNKENMITHFKEEISRLQFSLAEKEnlQRTFLLTTSSKEdtfiLKEQLRKAEEQIQATR 367
Cdd:TIGR02168 675 RRREIEE--LEEKIEELEEKIAELEKALAELRKELEELEEELEQLR--KELEELSRQISA----LRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 368 QEAVFLAKELSDAVNVRDKTMADLH---TAHLENEKVKKQLTDALAELK--LSAVNKDQEKTDTLEHELRREVEDLKLRL 442
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEeaeEELAEAEAEIEELEAQIEQLKeeLKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 443 QMAADHYKEKFKECQRLQKQINKLSDQSANSNSVFTKkigSQQKVNDASINTDpAATASTVDVKPLPSTAETDFDNLTKg 522
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELE-ALLNERASLEEALALLRSELEELSE- 901
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528946901 523 QVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKyadelAKMELKWKEQvKIAENIKLELAEVVDNYKLQLAEKEK 596
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEG-----LEVRIDNLQE-RLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-442 |
2.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 168 IAVLEKETTQLreqvgrmERELNHEKERGDQLQAEQKALTKVSQSLkmeneefkkryndvtSKALQLEEDIVSV--THKA 245
Cdd:COG4913 612 LAALEAELAEL-------EEELAEAEERLEALEAELDALQERREAL---------------QRLAEYSWDEIDVasAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 246 I-EKETELDSLK---DKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGNKENMITHFKEE 321
Cdd:COG4913 670 IaELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 322 ISRLQFSLAEKENLQRTFLLTTSSKEDTfiLKEQLRKAEEQIQATRQEavFLAKELSDAVNVRDkTMADLHT-----AHL 396
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDA--LRARLNRAEEELERAMRA--FNREWPAETADLDA-DLESLPEylallDRL 824
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 528946901 397 ENE---KVKKQLTDALAElklsavNKDQEKTDtLEHELRREVEDLKLRL 442
Cdd:COG4913 825 EEDglpEYEERFKELLNE------NSIEFVAD-LLSKLRRAIREIKERI 866
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
245-632 |
4.15e-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: 47.32 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 245 AIEKETELDSLKDKLKKAQCEREQLECQLKT-----EKDEKelyKVHLKNTEIENTKlvSEVQTLKNLDGNKENMITHFK 319
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNldknlNKDEE---KINNSNNKIKILE--QQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 320 EEISRLQFSLAEKenlqrtfllttssKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDavnvRDKTMADLHTAHLENE 399
Cdd:TIGR04523 103 SDLSKINSEIKND-------------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK----KEKELEKLNNKYNDLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 400 KVKKQLTDALAELKLSAVNKdQEKTDTLEHELRRevedLKLRLqMAADHYKEKFKEcqrLQKQINKLSDQSANSNSVFTK 479
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNI-QKNIDKIKNKLLK----LELLL-SNLKKKIQKNKS---LESQISELKKQNNQLKDNIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 480 KigsQQKVNdasintdpaatastvDVKPLPSTAETDFDNLTKGQvSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADEL 559
Cdd:TIGR04523 237 K---QQEIN---------------EKTTEISNTQTQLNQLKDEQ-NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528946901 560 AkmELKWKEQVKIAENIKLELAEV---VDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKLEGQNSQ 632
Cdd:TIGR04523 298 S--DLNNQKEQDWNKELKSELKNQekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-482 |
4.23e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 172 EKETTQLREQVGRMERElnheKERGDQLQAEQKALT----------KVSQS----LKMENEEFKKRYNDVTSKALQLEED 237
Cdd:TIGR02168 221 ELRELELALLVLRLEEL----REELEELQEELKEAEeeleeltaelQELEEkleeLRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 238 IVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQ-------LKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGN 310
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKldelaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 311 KENMITHFKEEISRLQFSLAEKENLQRTfllttsskedtfiLKEQLRKAEEQIQATRQEAVFLAKELSDavnvrdktmAD 390
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIER-------------LEARLERLEDRRERLQQEIEELLKKLEE---------AE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 391 LHTAHLENEKVKKQLTDALAELklsavnkdqEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQS 470
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEEL---------ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
330
....*....|..
gi 528946901 471 ANSNSVFTKKIG 482
Cdd:TIGR02168 506 EGVKALLKNQSG 517
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
155-646 |
5.17e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 155 EKTMKEKEELLKLIAV----LEKETTQLREQVGRMERELNHEKERgdqlqaeqkaltkvsqsLKMENEEFKKRYNDVTSk 230
Cdd:pfam12128 397 DKLAKIREARDRQLAVaeddLQALESELREQLEAGKLEFNEEEYR-----------------LKSRLGELKLRLNQATA- 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 231 alqlEEDIvsVTHKAIeKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGN 310
Cdd:pfam12128 459 ----TPEL--LLQLEN-FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFP 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 311 KENMITHF--------KEEISRlqfsLAEKENLQRTFL-----LTTSSKEDTFI--------------------LKEQLR 357
Cdd:pfam12128 532 QAGTLLHFlrkeapdwEQSIGK----VISPELLHRTDLdpevwDGSVGGELNLYgvkldlkridvpewaaseeeLRERLD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 358 KAEEQIQATRQEAVFLAKELSDA---VNVRDKTMADLHTAHLENEKVKKQLTDALAELKL-------SAVNKDQEKTDTL 427
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQAngeLEKASREETFARTALKNARLDLRRLFDEKQSEKDkknkalaERKDSANERLNSL 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 428 EHELRRevedLKLRLQMAADHYKEKFKEcQRLQKQINKLSDQSANSNSVftkkigsqqkvndASINTDPAATASTVDVKp 507
Cdd:pfam12128 688 EAQLKQ----LDKKHQAWLEEQKEQKRE-ARTEKQAYWQVVEGALDAQL-------------ALLKAAIAARRSGAKAE- 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 508 lPSTAETDFDNLTKG------QVSEMTKEIADKTEKYNKCKQLLQDEKT-----------KCNKYADELAKMELKwkeqv 570
Cdd:pfam12128 749 -LKALETWYKRDLASlgvdpdVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERA----- 822
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528946901 571 kiAENIKLELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSV-ENQAERKLEGQNSQSPHQISQCLKTSSE 646
Cdd:pfam12128 823 --ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLKEDANSEQAQGSIGERLAQLED 897
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
150-306 |
5.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKER-GDQLQAEQK------------------------ 204
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARALYRsggsvsyldvllgsesfsdfldrl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 205 -ALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELY 283
Cdd:COG3883 122 sALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
170 180
....*....|....*....|...
gi 528946901 284 KVHLKNTEIENTKLVSEVQTLKN 306
Cdd:COG3883 202 EAELAAAEAAAAAAAAAAAAAAA 224
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
127-455 |
5.57e-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: 46.61 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 127 EELLTMEDEGNS-----DMLVVTT-KAGLLELKIE---KTMKEKEELLKLIAVLEKETTQLREQVGRMERELnhekergd 197
Cdd:pfam05622 104 EELTSLAEEAQAlkdemDILRESSdKVKKLEATVEtykKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEEL-------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 198 qlqaeqkaltKVSQSLKMENEEFKKRYNDVTSKaLQLEedivsvTHKAIEKETELDSLKDKLKKAQCEREQL--ECQLKT 275
Cdd:pfam05622 176 ----------KKANALRGQLETYKRQVQELHGK-LSEE------SKKADKLEFEYKKLEEKLEALQKEKERLiiERDTLR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 276 EKDEkELYKVHLKNTEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQFS---LAEKENLQRTFLLTTS------SK 346
Cdd:pfam05622 239 ETNE-ELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHEnkmLRLGQEGSYRERLTELqqlledAN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 347 EDTFILKEQLRKAEEQIQATRQEAVFLAKELS-------DAVNVRDKT---MADLHTAHLENEKVKKQLtdalAELKLSA 416
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKALQeqgskaeDSSLLKQKLeehLEKLHEAQSELQKKKEQI----EELEPKQ 393
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 528946901 417 VNKDQEKTDTLEHELRREVEDLKlrlqMAADHYK---EKFKE 455
Cdd:pfam05622 394 DSNLAQKIDELQEALRKKDEDMK----AMEERYKkyvEKAKS 431
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
149-469 |
7.51e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 149 LLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVsQSLKMEN-----EEFKKR 223
Cdd:pfam07111 85 LRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEI-QRLHQEQlssltQAHEEA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 224 YNDVTSKALQLEEDIVSVTHK---------AIEKETELdsLKDKLKKAQcerEQLECQ------LKTEKDEKELYKVHLK 288
Cdd:pfam07111 164 LSSLTSKAEGLEKSLNSLETKrageakqlaEAQKEAEL--LRKQLSKTQ---EELEAQvtlvesLRKYVGEQVPPEVHSQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 289 NTEIENTKLVSEVQtlknldgnkenmitHFKEEISRLQFSLAekenlqrtfLLTTSSKEDTFILKEQLRKAEEQIQATRQ 368
Cdd:pfam07111 239 TWELERQELLDTMQ--------------HLQEDRADLQATVE---------LLQVRVQSLTHMLALQEEELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 369 -EAVFLAKELSDAVNVRDKT---MADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTdTLEHELRR-----EVEDLK 439
Cdd:pfam07111 296 lEPEFPKKCRSLLNRWREKVfalMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQA-ILQRALQDkaaevEVERMS 374
|
330 340 350
....*....|....*....|....*....|.
gi 528946901 440 LR-LQMAADHYKEKFKecqRLQKQINKLSDQ 469
Cdd:pfam07111 375 AKgLQMELSRAQEARR---RQQQQTASAEEQ 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-307 |
7.89e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKvsqSLKMENEEFKKR------ 223
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 224 -------------------------YNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKD 278
Cdd:COG4942 116 lgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190
....*....|....*....|....*....|...
gi 528946901 279 EKELY----KVHLKNTEIENTKLVSEVQTLKNL 307
Cdd:COG4942 196 ERQKLlarlEKELAELAAELAELQQEAEELEAL 228
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
153-454 |
1.06e-04 |
|
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: 45.87 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKE-ELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQK-------ALTKVSQSLKMENEEFKKRY 224
Cdd:pfam05483 429 KIAEELKGKEqELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklkniELTAHCDKLLLENKELTQEA 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 225 NDVTSKALQLEEDIV--------------SVTHKAIEKETELDSLKDKLKKaqcEREQLECQLKTEKDEKELYKVHLKNT 290
Cdd:pfam05483 509 SDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKK 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 291 EIENTKLVSEVQTLKNLDGNKENMITHFKEE---------------------ISRLQFSLAE-KENLQRTFLLTTSSKED 348
Cdd:pfam05483 586 EKQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgsaenkqlnayeikVNKLELELASaKQKFEEIIDNYQKEIED 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 349 TFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLHTAHleNEKVKKQLTDALAELKLSAvNKDQEKTD--- 425
Cdd:pfam05483 666 KKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH--KHQYDKIIEERDSELGLYK-NKEQEQSSaka 742
|
330 340 350
....*....|....*....|....*....|..
gi 528946901 426 TLEHEL---RREVEDLKLRLQMAADHyKEKFK 454
Cdd:pfam05483 743 ALEIELsniKAELLSLKKQLEIEKEE-KEKLK 773
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
131-261 |
1.10e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 43.07 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 131 TMEDEGNSDMLVVTTKAGLLeLKIEKTMKEKEELLKLIAVLE-------KETTQLREQVGRMERELNHEKERGDQLQAEQ 203
Cdd:pfam11559 25 TAEGVEENIARIINVIYELL-QQRDRDLEFRESLNETIRTLEaeierlqSKIERLKTQLEDLERELALLQAKERQLEKKL 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528946901 204 KALTkvsQSLKMENEEFKKRYNDVTSKALQLeedivsvTHKAIEKETELDSLKDKLKK 261
Cdd:pfam11559 104 KTLE---QKLKNEKEELQRLKNALQQIKTQF-------AHEVKKRDREIEKLKERLAQ 151
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-585 |
1.23e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 352 LKEQLRKAEEQIQATRQE--AVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEH 429
Cdd:COG3206 187 LRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 430 ELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQsansnsvftkkIGSQQKVNDASINTDPAATASTVDVkplp 509
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ-----------LQQEAQRILASLEAELEALQAREAS---- 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528946901 510 staetdfdnlTKGQVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADELAKMelkwkEQVKIAENIKLELAEVVD 585
Cdd:COG3206 332 ----------LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL-----EEARLAEALTVGNVRVID 392
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
110-469 |
1.29e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 110 EIRGASTPFQFRAASP----VEELLTMEDEGNSDMLvvttkAGLLELKI--EKTMKEKEELLKLI-----AVLEKETT-- 176
Cdd:PRK04778 90 EAEELNDKFRFRKAKHeineIESLLDLIEEDIEQIL-----EELQELLEseEKNREEVEQLKDLYrelrkSLLANRFSfg 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 177 ----QLREQVGRMERELNH---EKERGDQLQAEqkaltKVSQSLKMENEEFKKRYNDVtsKAL----------------- 232
Cdd:PRK04778 165 paldELEKQLENLEEEFSQfveLTESGDYVEAR-----EILDQLEEELAALEQIMEEI--PELlkelqtelpdqlqelka 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 233 ---QLEEDIVSVTHKAIEKEteLDSLKDKLKKAQCEREQLEC--------QLKTEKDEkeLYKVhlknteIENtklvsEV 301
Cdd:PRK04778 238 gyrELVEEGYHLDHLDIEKE--IQDLKEQIDENLALLEELDLdeaeekneEIQERIDQ--LYDI------LER-----EV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 302 QTLKNLDGNKENM---ITHFKEEISRLQfslAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELS 378
Cdd:PRK04778 303 KARKYVEKNSDTLpdfLEHAKEQNKELK---EEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 379 DAVNVRDKTMADLHTAHLENEKVKKQLtDALAELKLSAVNKDQEKTDTLeHELRREVEdlKLRLQMAADHYKEKFKEcqr 458
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEML-QGLRKDELEAREKLERYRNKL-HEIKRYLE--KSNLPGLPEDYLEMFFE--- 452
|
410
....*....|.
gi 528946901 459 LQKQINKLSDQ 469
Cdd:PRK04778 453 VSDEIEALAEE 463
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
783-810 |
1.32e-04 |
|
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: 39.74 E-value: 1.32e-04
10 20
....*....|....*....|....*...
gi 528946901 783 KVCPMCSEQFPpDYDQQVFERHVQTHFD 810
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-623 |
1.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 146 KAGLLELKIEKTMKEkEELLKLIAVLEKETTQlREQVGRMEREL-NHEKERGDQLQAEQKALTKVSQS---LKMENEEFK 221
Cdd:pfam01576 228 QAQIAELRAQLAKKE-EELQAALARLEEETAQ-KNNALKKIRELeAQISELQEDLESERAARNKAEKQrrdLGEELEALK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 222 KRYND-VTSKALQLE-----EDIVSVTHKAIEKETE----------------LDSLKDKLKKAQCEREQLE-CQLKTEKD 278
Cdd:pfam01576 306 TELEDtLDTTAAQQElrskrEQEVTELKKALEEETRsheaqlqemrqkhtqaLEELTEQLEQAKRNKANLEkAKQALESE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 279 EKELyKVHLK-------NTEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQfslAEKENLQrTFLLTTSSK----- 346
Cdd:pfam01576 386 NAEL-QAELRtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ---SELESVS-SLLNEAEGKnikls 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 347 EDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQ---LTDALAELKlsavNKDQEK 423
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMK----KKLEED 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 424 TDTLE------HELRREVEDLKLRlqmaadhYKEKFKECQRLQKQINKLsdqsansnsvftkkigsQQKVNDASINTDPa 497
Cdd:pfam01576 537 AGTLEaleegkKRLQRELEALTQQ-------LEEKAAAYDKLEKTKNRL-----------------QQELDDLLVDLDH- 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 498 atastvdvkplpstaetdfdnlTKGQVSEMTKeiadkteKYNKCKQLLQDEKTKCNKYADELAKMELKWKEQVKIAENIK 577
Cdd:pfam01576 592 ----------------------QRQLVSNLEK-------KQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 528946901 578 LELAEVVD-------NYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAE 623
Cdd:pfam01576 643 RALEEALEakeelerTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE 695
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
783-810 |
1.58e-04 |
|
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar proteins; spn-F is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. It acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F is a coil-coiled protein containing a C2H2-type zinc binding domain.
Pssm-ID: 412017 Cd Length: 30 Bit Score: 39.43 E-value: 1.58e-04
10 20
....*....|....*....|....*...
gi 528946901 783 KVCPMCSEQFPPDYDQQVFERHVQTHFD 810
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
157-322 |
1.58e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 157 TMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEE 236
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 237 DIVSVT----HKAIEKE-----TELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQT-LKN 306
Cdd:COG1579 81 QLGNVRnnkeYEALQKEieslkRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAeLEE 160
|
170
....*....|....*.
gi 528946901 307 LDGNKENMITHFKEEI 322
Cdd:COG1579 161 LEAEREELAAKIPPEL 176
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-447 |
1.84e-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: 45.11 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 152 LKIEKTMKEKE------ELLKLIAVLEKETTQLREQVGRMErELNHEKERGDQLQAEQ-KALTKVSQSLKMENEEFKKRY 224
Cdd:pfam15921 588 MQVEKAQLEKEindrrlELQEFKILKDKKDAKIRELEARVS-DLELEKVKLVNAGSERlRAVKDIKQERDQLLNEVKTSR 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 225 NDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKT-EKDEKELYKVHLknteientklvsevqt 303
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmEGSDGHAMKVAM---------------- 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 304 lknldgNKENMITHFKEEISRLQFSLAEKENlqrtfLLTTSSKEDTFiLKEQLRKaeeqiqatrqeavfLAKELSDAVNV 383
Cdd:pfam15921 731 ------GMQKQITAKRGQIDALQSKIQFLEE-----AMTNANKEKHF-LKEEKNK--------------LSQELSTVATE 784
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528946901 384 RDKTMADLHTAHLENEKVKKQLTDALAELKLSAVnKDQEKTDTLEhelRREVEDLKLRLQMAAD 447
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASL-QFAECQDIIQ---RQEQESVRLKLQHTLD 844
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-601 |
2.01e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 146 KAGLLELKIEKTMKEKEELLKLIA--VLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKR 223
Cdd:PRK02224 170 RASDARLGVERVLSDQRGSLDQLKaqIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 224 YNDVTSkalqLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQL-----KTEKDEKELYKVHLKNTEIENTK-- 296
Cdd:PRK02224 250 REELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERddllaEAGLDDADAEAVEARREELEDRDee 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 297 LVSEVQTLKNLDGNKENMITHFKEEISRLQFSLAEKENLQRTFlltTSSKEDTfilKEQLRKAEEQIQATRQEAVFLAKE 376
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL---ESELEEA---REAVEDRREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 377 LSDAVNVRDKtMADLHTAHLEN-EKVKKQLTDALAELK------------------------------LSAVNKDQEKTD 425
Cdd:PRK02224 400 FGDAPVDLGN-AEDFLEELREErDELREREAELEATLRtarerveeaealleagkcpecgqpvegsphVETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 426 TLEHEL---RREVEDLKLRLqmaadhykEKFKECQRLQKQINKLSDQSANSNSVFTKKigsqqkvnDASINTDP-AATAS 501
Cdd:PRK02224 479 ELEAELedlEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEELIAER--------RETIEEKReRAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 502 TVDVKPLPSTAETDFDNLTKgqVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADELAKMELKWKEQVKIAENIKlELA 581
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAE--AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE-ALA 619
|
490 500
....*....|....*....|
gi 528946901 582 EVVDNYKLQLAEKEKEISGL 601
Cdd:PRK02224 620 ELNDERRERLAEKRERKREL 639
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
150-279 |
2.14e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQA----------------EQKALTKVSQSL 213
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyeeqlgnvrnnkEYEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528946901 214 KMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDE 279
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
134-325 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 134 DEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKER--GDQLQAEQKALTKVSQ 211
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 212 SLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYK--VHLKN 289
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKqeVKQIK 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528946901 290 TEIENTK-----LVSEVQTLKNL---------DGNKENMItHFKEEISRL 325
Cdd:TIGR04523 652 ETIKEIRnkwpeIIKKIKESKTKiddiielmkDWLKELSL-HYKKYITRM 700
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
783-809 |
2.94e-04 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 38.63 E-value: 2.94e-04
10 20
....*....|....*....|....*..
gi 528946901 783 KVCPMCSEQFPPDYDQQVFERHVQTHF 809
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
110-610 |
3.32e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 110 EIRGASTPFQFRAA-SPVEELLTMEDEGNSDM-LVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMER 187
Cdd:pfam12128 257 ELRLSHLHFGYKSDeTLIASRQEERQETSAELnQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 188 E----LNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETEldsLKDKLK--- 260
Cdd:pfam12128 337 AdietAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIRE---ARDRQLava 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 261 ----KAQCE--REQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDgNKENMITHFKEEisrLQFSLAEKEN 334
Cdd:pfam12128 414 eddlQALESelREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLE-NFDERIERAREE---QEAANAEVER 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 335 LQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAV------------FLAKELSDAVNVRDKTMAD--LHTAHLENEK 400
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpqagtllhFLRKEAPDWEQSIGKVISPelLHRTDLDPEV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 401 VKKQLTDalaELKLSAVNKDQEKTDT-----LEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANSNS 475
Cdd:pfam12128 570 WDGSVGG---ELNLYGVKLDLKRIDVpewaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 476 VFTKKIGSQQKVNDASINTDPAATASTVDVKPLPSTAETDFD---NLTKGQVSEMTKEIAD-----KTEKYNKCKQLLQD 547
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEaqlKQLDKKHQAWLEEQKEqkreaRTEKQAYWQVVEGA 726
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528946901 548 EKTKCNKYADELAKMELKWKEQVK-IAENIKLELAEV-VDNYKlqLAEKEKEISGLTSYWENLSR 610
Cdd:pfam12128 727 LDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLgVDPDV--IAKLKREIRTLERKIERIAV 789
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
180-411 |
3.60e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 180 EQVGRMERELNHEKERGDQL-QAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDk 258
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 259 lkkaqcEREQLECQLKTEKDEKELYK--------VHLKNTEIENTKLVSEVQTLKNLDGNKENMITHF--KEEISRLQFS 328
Cdd:PRK05771 122 ------EIERLEPWGNFDLDLSLLLGfkyvsvfvGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVvvLKELSDEVEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 329 LAEKENLQRtflLTTSSKEdtfILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLHtAHLENEKVKKQLTDA 408
Cdd:PRK05771 196 ELKKLGFER---LELEEEG---TPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALY-EYLEIELERAEALSK 268
|
...
gi 528946901 409 LAE 411
Cdd:PRK05771 269 FLK 271
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
150-608 |
3.99e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKE-ELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKmeneEFKKRYNDVT 228
Cdd:TIGR00606 207 MELKYLKQYKEKAcEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK----ALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 229 SKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQcEREQLECQLKTEKDEKELYKVHLKNTEIENtklvsevqtlknld 308
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREK-ERELVDCQRELEKLNKERRLLNQEKTELLV-------------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 309 gnkenmithfkeEISRLQfslaekenLQRTFLLTTSSKEDTFILKEQLR------KAEEQIQATRQEAVFLAKE-LSDAV 381
Cdd:TIGR00606 348 ------------EQGRLQ--------LQADRHQEHIRARDSLIQSLATRleldgfERGPFSERQIKNFHTLVIErQEDEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 382 NVRDKTMADLHtahlENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHElRREVEDLKLRLQMAADHYKEKFKECQRLQK 461
Cdd:TIGR00606 408 KTAAQLCADLQ----SKERLKQEQADEIRDEKKGLGRTIELKKEILEKK-QEELKFVIKELQQLEGSSDRILELDQELRK 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 462 QINKLSDQSANSNSVFTKKIGSQQKVNDASINTDPAATAStvdvkplpSTAETDFDNLTKGQVSEMTKEIADKTEKYNKC 541
Cdd:TIGR00606 483 AERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ--------EMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528946901 542 KQLLQDEKTKCNKY---ADELAKMELKWKEQVKIAEN----IKLELAEVVDNYKLQLAEKEKEISGLTSYWENL 608
Cdd:TIGR00606 555 KSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDrlakLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
152-281 |
4.46e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 152 LKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTS-- 229
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528946901 230 --KALQ-----LEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKE 281
Cdd:COG1579 90 eyEALQkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
121-436 |
4.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 121 RAASPVEELLTMEDEGNSDMLVVTTKAG-----------LLELKIEKTMKEK-EELLKLIAVLEKETTQLREQVGRMERE 188
Cdd:COG3206 118 AAIERLRKNLTVEPVKGSNVIEISYTSPdpelaaavanaLAEAYLEQNLELRrEEARKALEFLEEQLPELRKELEEAEAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 189 LnhekergdqlqaeqkaltkvsqslkmenEEFKKRYN--DVTSKALQLEEDIVSVthkaiekETELDSLKDKLKKAQCER 266
Cdd:COG3206 198 L----------------------------EEFRQKNGlvDLSEEAKLLLQQLSEL-------ESQLAEARAELAEAEARL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 267 EQLECQLKTEKDEkelykvhlknteienTKLVSEVQTLKNLdgnkenmithfKEEISRLQFSLAEkenlqrtfLLTTSSK 346
Cdd:COG3206 243 AALRAQLGSGPDA---------------LPELLQSPVIQQL-----------RAQLAELEAELAE--------LSARYTP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 347 EDtfilkEQLRKAEEQIQATRQEavfLAKELsdavnvrDKTMADLHTAHLENEKVKKQLTDALAELKlSAVNKDQEKTDT 426
Cdd:COG3206 289 NH-----PDVIALRAQIAALRAQ---LQQEA-------QRILASLEAELEALQAREASLQAQLAQLE-ARLAELPELEAE 352
|
330
....*....|
gi 528946901 427 LEhELRREVE 436
Cdd:COG3206 353 LR-RLEREVE 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-279 |
5.58e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALtkvsqslkmeNEEFKKRyndvTS 229
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----------ALEIKKQ----EW 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 528946901 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDE 279
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
210-627 |
5.82e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 210 SQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELykvhLKN 289
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 290 TEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQE 369
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 370 AVFLAKELSDAVNVRDKTMadlhtahlENEKVKKQLTDALAELKLSAvnKDQEKTDTLEHELRREVEDLK-LRLQMAADH 448
Cdd:PRK03918 323 INGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 449 YKEKFKECQRLQKQINKLSDQSANsnsvfTKKIGSQQKvnDASINTDPAATASTVDVKPLPSTAETDFDNLTKGQVSEMT 528
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGE-----LKKEIKELK--KAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 529 KEIADKTEKYNKCKQLL---------QDEKTKCNKYADELAKMELKWKEQVKiaENIKlELAEVVDNYKLQLAEKEKEIS 599
Cdd:PRK03918 466 KELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKKYNL--EELE-KKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430
....*....|....*....|....*....|.
gi 528946901 600 GLTSYWENLSREKEHKRSVENQ---AERKLE 627
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKldeLEEELA 573
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-624 |
6.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKA--LTKVSQSLKMENEEFKKRYNDVTSK 230
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 231 ALQLEedivsvthkaiEKETELDSLKDKLKKAQCEREQLECQLKTEKDEkelykvHLKNTEIENTKLVSEVQTLKNLdgn 310
Cdd:COG4717 155 LEELR-----------ELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEE--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 311 kenmITHFKEEISRLQfslAEKENLQRTFLLTTsskedtfiLKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKT--- 387
Cdd:COG4717 215 ----LEEAQEELEELE---EELEQLENELEAAA--------LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 388 ---MADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEktdtlEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQIN 464
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 465 KLSDQsansnsvftkkigsqqkvnDASINTDPAATASTVDVKPLPSTAETDFDnltkgQVSEMTKEIADKTEKYNKCKQL 544
Cdd:COG4717 355 EAEEL-------------------EEELQLEELEQEIAALLAEAGVEDEEELR-----AALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 545 LQDEKTKCNKYADELAKMELKWKEQvKIAENIKlELAEVVDNYKLQLAEKEKEISGL---TSYWENLSREKEHKRSVENQ 621
Cdd:COG4717 411 LEELLGELEELLEALDEEELEEELE-ELEEELE-ELEEELEELREELAELEAELEQLeedGELAELLQELEELKAELREL 488
|
...
gi 528946901 622 AER 624
Cdd:COG4717 489 AEE 491
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
756-781 |
1.04e-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: 37.15 E-value: 1.04e-03
10 20
....*....|....*....|....*.
gi 528946901 756 KKCPLCELMFPPNYDQSKFEEHVESH 781
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
216-423 |
1.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 216 ENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQL-KTEKDEKELYKVhLKnteien 294
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaEAEAEIEERREE-LG------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 295 tKLVSEVQTlknlDGNKENMI------THFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQ 368
Cdd:COG3883 90 -ERARALYR----SGGSVSYLdvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528946901 369 EAVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEK 423
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
119-627 |
1.11e-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: 42.65 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 119 QFRAASPVEELLTMEDEGNSDMLvvtTKAGLLELKIEKTMKEKEELLKL-------------------IAVLEKETTQLR 179
Cdd:TIGR00618 156 QFLKAKSKEKKELLMNLFPLDQY---TQLALMEFAKKKSLHGKAELLTLrsqlltlctpcmpdtyherKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 180 EQVG---------RMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNdVTSKALQLEEDIVSVTH---KAIE 247
Cdd:TIGR00618 233 EALQqtqqshaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN-RARKAAPLAAHIKAVTQieqQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 248 KETELDSLKDKLKKAQCEREQLECQlKTEKDEKELYKVHLKNTEIENtKLVSEVQTLknldgnkenMITHFKEEISRLQF 327
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHI-RDAHEVATS---------IREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 328 SLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKelSDAVNVRDKTMADLHTAHLENEKVKKQLTD 407
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAH--AKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 408 ALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQMAADHYKEK--FKECQRLQKQINKLSDQSANSNSVFTKKIGSQQ 485
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcpLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 486 KVNDASINTDPAATASTVDVKPLPSTAETDFDNLTKgqvseMTKEIADKTEKYNKCKQLLQDektkCNKYADELAKMELK 565
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI-----LTQCDNRSKEDIPNLQNITVR----LQDLTEKLSEAEDM 609
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 566 WKEQVKIaenIKLELAEVVDNYKLQLAEKE------KEISGLTSYWENLSREK--EHKRSVENQAERKLE 627
Cdd:TIGR00618 610 LACEQHA---LLRKLQPEQDLQDVRLHLQQcsqelaLKLTALHALQLTLTQERvrEHALSIRVLPKELLA 676
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-281 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 145 TKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMEREL-NHEKERGDQLQAEQKALTKVSQSLKMENEEFKKR 223
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528946901 224 YNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKE 281
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
294-485 |
1.35e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 294 NTKLVSEVQTLKNLDGNKENMITHFKEEISRLQF-SLAEKENLQRTfllttSSKEDTFILK-EQLRKAEEQIQATRQEAV 371
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKkASALKRQLDRE-----SDRNQELQKRiRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 372 FLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTdtlehELRREVEDLKLRLQMAADHYKE 451
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQ-----STNSELEELQERLDLLKAKASE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528946901 452 KFKECQRLQKQINKLSD------------QSANSNSVFTKKIGSQQ 485
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEaeqrikelefeiQSQEQDSEIVKNSKSEL 196
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
162-371 |
1.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 162 EELLKLIAVLEKETTQLREQVGRMERELNHEKERgdQLQAEQKALTKVSQ-------------SLKMENEEFKKRYNDVT 228
Cdd:PRK04863 878 NRLLPRLNLLADETLADRVEEIREQLDEAEEAKR--FVQQHGNALAQLEPivsvlqsdpeqfeQLKQDYQQAQQTQRDAK 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 229 SKALQLEEDIVSVTH-------KAIEKETEL-DSLKDKLKKAQCEREQLECQLKTEKDEKELY-KVHlknteienTKLVS 299
Cdd:PRK04863 956 QQAFALTEVVQRRAHfsyedaaEMLAKNSDLnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYnQVL--------ASLKS 1027
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 300 EVQTlknldgnKENMITHFKEEIS----RLQFSLAEK---------ENL-----QRTFLLTTSSKEDTFI--LKEQLRKA 359
Cdd:PRK04863 1028 SYDA-------KRQMLQELKQELQdlgvPADSGAEERararrdelhARLsanrsRRNQLEKQLTFCEAEMdnLTKKLRKL 1100
|
250
....*....|..
gi 528946901 360 EEQIQATRQEAV 371
Cdd:PRK04863 1101 ERDYHEMREQVV 1112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-676 |
1.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 408 ALAELKLSAVNKD----QEKTDTLEHELRR---EVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANSNSVFTKK 480
Cdd:COG3883 12 AFADPQIQAKQKElselQAELEAAQAELDAlqaELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 481 IGSQQKvNDASIntdpaataSTVDVKpLPSTAETDF-DNLTkgQVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADEL 559
Cdd:COG3883 92 ARALYR-SGGSV--------SYLDVL-LGSESFSDFlDRLS--ALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 560 AKMelkwkeqvkiaeniKLELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKLEGQNSQSPHQISQ 639
Cdd:COG3883 160 EAL--------------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 528946901 640 CLKTSSEKSGHVPAVSNTQPVLQYGNPYATPETRDGA 676
Cdd:COG3883 226 AAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-300 |
1.60e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 150 LELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEqkaltkvSQSLKMENEEFKKRYNDVTS 229
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE-------LQRLSEELADLNAAIAGIEA 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528946901 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLktEKDEKELYKVHLKNTEIENTKLVSE 300
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY--DRVEKELSKLQRELAEAEAQARASE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
151-303 |
2.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 151 ELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAE----QKALTKVSQSLKMENEEFKKR--- 223
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 224 -------------------YNDVTSKALQLeEDIVSVTHKAIEketELDSLKDKLKKAQCEREQLECQLKTEKDEKELYK 284
Cdd:COG3883 95 lyrsggsvsyldvllgsesFSDFLDRLSAL-SKIADADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170
....*....|....*....
gi 528946901 285 VHLKNTEIENTKLVSEVQT 303
Cdd:COG3883 171 AELEAQQAEQEALLAQLSA 189
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
756-782 |
2.18e-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: 2.18e-03
10 20
....*....|....*....|....*..
gi 528946901 756 KKCPLCELMFPPNYDQSKFEEHVESHW 782
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
169-444 |
2.31e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 169 AVLEKETTQLREQVGR--------MERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVS 240
Cdd:pfam00038 28 KLLETKISELRQKKGAepsrlyslYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 241 ---VTHKA----IEKETELDSLKdklkkaqcerEQLECQLKTEKDE-KELYKVHLKNT---EIENTKLVSEVQTLKNLDG 309
Cdd:pfam00038 108 lrkDLDEAtlarVDLEAKIESLK----------EELAFLKKNHEEEvRELQAQVSDTQvnvEMDAARKLDLTSALAEIRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 310 NKENMITHFKEEisrlqfslAEKENLQRTFLLTTSSKEDTfilkEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMA 389
Cdd:pfam00038 178 QYEEIAAKNREE--------AEEWYQSKLEELQQAAARNG----DALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528946901 390 DLHTAHLENEKVKKQLTDALAELKlsavNKDQEKTDTLEHELrREVEDL---KLRLQM 444
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELE----AELQETRQEMARQL-REYQELlnvKLALDI 298
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-647 |
2.45e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 146 KAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKvSQSLKMENEEFKKRYN 225
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAKKKAEEDKKKAD 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 226 DVTSKALqlEEDIVSVTHKAIEKETELDSLKDKL----------KKAQCEREQLECQLKTEKDEK--ELYKVHLKNTEIE 293
Cdd:PTZ00121 1409 ELKKAAA--AKKKADEAKKKAEEKKKADEAKKKAeeakkadeakKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKAD 1486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 294 NTKLVSEVQTLKNLDGNKenmithfKEEISRLQFSLAEKENLQRTFLLTTSSKEDTfilKEQLRKAEEQIQAtrqEAVFL 373
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKK-------AAEAKKKADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKA---DELKK 1553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 374 AKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRlqmaadhyKEKF 453
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--------AEEL 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 454 KECQRLQKQINKLSDQSANSnsvftKKIGSQQKvndasintdPAATASTVDVKPLPSTAETDfdnltKGQVSEMTKEiad 533
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEE-----KKKAEELK---------KAEEENKIKAAEEAKKAEED-----KKKAEEAKKA--- 1683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 534 KTEKYNKCKQLLQDEKTKcnKYADELAKMElkwKEQVKIAENIKLElaEVVDNYKLQLAEKEKEISGLTSywENLSREKE 613
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEA--KKAEELKKKE---AEEKKKAEELKKA--EEENKIKAEEAKKEAEEDKKKA--EEAKKDEE 1754
|
490 500 510
....*....|....*....|....*....|....*..
gi 528946901 614 HKRSVEN---QAERKLEGQNSQSPHQISQCLKTSSEK 647
Cdd:PTZ00121 1755 EKKKIAHlkkEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-365 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 146 KAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEqkaltkvsqslkMENEEFKKRYn 225
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE------------IQELQEQRID- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 226 dvtskalqLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLK 305
Cdd:TIGR02169 845 --------LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 306 NLDGNkenmithFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQA 365
Cdd:TIGR02169 917 KRLSE-------LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
155-505 |
3.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 155 EKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQL 234
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 235 EEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKElykvhlknteientKLVSEVQTLKNLDGNKENM 314
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK--------------QLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 315 ITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEdtfiLKEQLRKAEEQIQATRQEAVFLAKELSDAVNVrdktmADLHTA 394
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQA----LDELLKEANRNAEKEEELAEAEKLIESLPREL-----AEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 395 HLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLR-LQMAADHYKEKFKECQRLQKQINKLSDQSANS 473
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVeKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340 350
....*....|....*....|....*....|..
gi 528946901 474 NSVFTKKIGSQQKVNDASINTDPAATASTVDV 505
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-632 |
3.21e-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: 41.20 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 403 KQLTDALAELKlSAVNKDQEKTDTLE--HELRREVEDLKLRLqmAADHYKEKFKECQRLQKQINKLSDQsansnsvfTKK 480
Cdd:TIGR02168 189 DRLEDILNELE-RQLKSLERQAEKAEryKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEE--------LEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 481 IGSQQKVNDASINTdpaatastvdvkplpstaetdfdnlTKGQVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADELA 560
Cdd:TIGR02168 258 LTAELQELEEKLEE-------------------------LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528946901 561 KMELKWKEqvkiAENIKLELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKLEGQNSQ 632
Cdd:TIGR02168 313 NLERQLEE----LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-630 |
3.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENeefkKRYNDVTSKAL 232
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED----AKKAEAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 233 QLEedivsvthKAIEKETELDSLK-DKLKKAQCEREQLEC-QLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGN 310
Cdd:PTZ00121 1186 EVR--------KAEELRKAEDARKaEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 311 KENMITHFKEEISRLQFSLAEKENLQRTflLTTSSKEDTFILKEQLRKAEEQIQAT--RQEAVFLAKELSDAVNVRDKTM 388
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 389 ADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSD 468
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 469 QSANSNSVfTKKIGSQQKVNDASINTDPAATASTVDVKPLPS-TAETDFDNLTKGQVSEMTKEIADKTEKYNKCKQLLQD 547
Cdd:PTZ00121 1416 AKKKADEA-KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 548 EKTKCN---------KYADELAKMElkwkEQVKIAENIKLELAEVVDnyKLQLAEKEKEISGLTSYWEnlSREKEHKRSV 618
Cdd:PTZ00121 1495 AKKKADeakkaaeakKKADEAKKAE----EAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEE--LKKAEEKKKA 1566
|
490
....*....|..
gi 528946901 619 EnQAERKLEGQN 630
Cdd:PTZ00121 1567 E-EAKKAEEDKN 1577
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
171-453 |
3.61e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 171 LEKETTQ---LREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEdivsvTHKAIE 247
Cdd:pfam01576 477 LQEETRQklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE-----GKKRLQ 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 248 KETELDSLKDKLKKAQCEReqLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQF 327
Cdd:pfam01576 552 RELEALTQQLEEKAAAYDK--LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 328 SLAEKENlqrTFLLTTSSKEDTFILKEQLRKAEEQIQAtrqeavflakELSDAVNVRDKTMADLHtahlENEKVKKQLTD 407
Cdd:pfam01576 630 EAREKET---RALSLARALEEALEAKEELERTNKQLRA----------EMEDLVSSKDDVGKNVH----ELERSKRALEQ 692
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 528946901 408 ALAELKlsavnkdqEKTDTLEHELrREVEDLKLRLQMAADHYKEKF 453
Cdd:pfam01576 693 QVEEMK--------TQLEELEDEL-QATEDAKLRLEVNMQALKAQF 729
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
153-459 |
3.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 153 KIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKAltkvsqsLKMENEEFKKRYNDVTSKAL 232
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 233 QLEEdivsvthKAIEKETELDSLKDKLKKAQCEREQLEcqlKTEKDEKELYKvhlkntEIEntKLVSEVQTlKNLDGNKE 312
Cdd:COG1340 75 ELKE-------ERDELNEKLNELREELDELRKELAELN---KAGGSIDKLRK------EIE--RLEWRQQT-EVLSPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 313 NMIThfkEEISRLQFSL--AEKENLQRTFLLTTSSKEDTfiLKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMAD 390
Cdd:COG1340 136 KELV---EKIKELEKELekAKKALEKNEKLKELRAELKE--LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528946901 391 LHTAHLENEKVKKQLtDALAElKLSAVNKDQEKTDTLEHELRREVEDLKLR-----LQMAADHYKEKFKECQRL 459
Cdd:COG1340 211 ADELHKEIVEAQEKA-DELHE-EIIELQKELRELRKELKKLRKKQRALKREkekeeLEEKAEEIFEKLKKGEKL 282
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
177-465 |
4.09e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 177 QLREQVGRMERELNHEKERGDQLQAE-QKALTKVSQSLK-MENEEFKKRYNDVTSKALQLEEDIVSVThKAIEkETELDS 254
Cdd:pfam06160 183 KLEEETDALEELMEDIPPLYEELKTElPDQLEELKEGYReMEEEGYALEHLNVDKEIQQLEEQLEENL-ALLE-NLELDE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 255 LKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLknldgnkenmithfKEEISRLQ--FSLAEK 332
Cdd:pfam06160 261 AEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKEL--------------KEELERVQqsYTLNEN 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 333 EnLQRTFLLTTSSKEdtfiLKEQLRKAEEQIQAtrQEAVFlaKELSDAVNVRDKTMADLHTAHlenEKVKKQLTDalael 412
Cdd:pfam06160 327 E-LERVRGLEKQLEE----LEKRYDEIVERLEE--KEVAY--SELQEELEEILEQLEEIEEEQ---EEFKESLQS----- 389
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528946901 413 kLSAVNKD-QEKTDTLE---HELRREVEdlKLRLQMAADHYKEKFK----ECQRLQKQINK 465
Cdd:pfam06160 390 -LRKDELEaREKLDEFKlelREIKRLVE--KSNLPGLPESYLDYFFdvsdEIEDLADELNE 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
127-455 |
4.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 127 EELLTMEDEgNSDMLvvtTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKAL 206
Cdd:PRK02224 286 ERLEELEEE-RDDLL---AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 207 TKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKT-EKDEKElykv 285
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAElEATLRT---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 286 hLKNTEIENTKLVSE---------------VQTLKNLDGNKENM---ITHFKEEISRLQFSLAEKENLQRTFLLTTSSKE 347
Cdd:PRK02224 438 -ARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVEELeaeLEDLEEEVEEVEERLERAEDLVEAEDRIERLEE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 348 DTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLHTAHLENEKVK---KQLTDALAELK--LSAVNKDQE 422
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKLAELKerIESLERIRT 596
|
330 340 350
....*....|....*....|....*....|....*.
gi 528946901 423 KTDTLEhELRREVEDLKLRLQMAA---DHYKEKFKE 455
Cdd:PRK02224 597 LLAAIA-DAEDEIERLREKREALAelnDERRERLAE 631
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
206-599 |
5.98e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 206 LTKVSQSLKMENeeFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEReqlecQLKTEKDEKELYKV 285
Cdd:TIGR01612 1348 IANIYNILKLNK--IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKS-----KIESTLDDKDIDEC 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 286 HLKNTEIENTKLVSEVQT---LKNLDGNKENMITHFKEeisrlqfslaekenlqrtflLTTSSKEDTFILKEQLRKAEEQ 362
Cdd:TIGR01612 1421 IKKIKELKNHILSEESNIdtyFKNADENNENVLLLFKN--------------------IEMADNKSQHILKIKKDNATND 1480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 363 IQATRQEAvflaKELSDAVNvRDKTMADLHTAHLENEKV-----KKQLTDALAELKLSAVNKDQEKTDTLEHELRREVED 437
Cdd:TIGR01612 1481 HDFNINEL----KEHIDKSK-GCKDEADKNAKAIEKNKElfeqyKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKD 1555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 438 LKLRLQMAADHYKEKFKECQRLQKQInklSDQSANSNSVFTKKIGSQqkvndASINTDPAATASTVDVKPLPSTAETDFD 517
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKEIKKEKFRI---EDDAAKNDKSNKAAIDIQ-----LSLENFENKFLKISDIKKKINDCLKETE 1627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 518 NLTKgQVSEMT--------KEIADKTEKYNKCKQLLQDEKTKCNKYADELAKMELKwkeqvkiAENIKLELAEVVDNYKL 589
Cdd:TIGR01612 1628 SIEK-KISSFSidsqdtelKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSE-------IEKIEIDVDQHKKNYEI 1699
|
410
....*....|
gi 528946901 590 QLAEKEKEIS 599
Cdd:TIGR01612 1700 GIIEKIKEIA 1709
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
211-297 |
6.32e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.05 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 211 QSLKMENEEFKKRYNDVTSKALQLEEDivsvthkAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNT 290
Cdd:pfam12718 3 NSLKLEAENAQERAEELEEKVKELEQE-------NLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNN 75
|
....*..
gi 528946901 291 EIENTKL 297
Cdd:pfam12718 76 ENLTRKI 82
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
151-260 |
6.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 151 ELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMER-------ELNHEKE----RGDQLQAEQKALTKVSQSLKMENEE 219
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKrllqkeeNLDRKLEllekREEELEKKEKELEQKQQELEKKEEE 132
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528946901 220 FKKRYNdvtsKALQLEEDIVSVTHKAIeKETELDSLKDKLK 260
Cdd:PRK12704 133 LEELIE----EQLQELERISGLTAEEA-KEILLEKVEEEAR 168
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
149-217 |
7.34e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 7.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528946901 149 LLELK--IEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMEN 217
Cdd:COG4026 137 LLELKekIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKR 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-627 |
7.49e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMErelnhEKERGDQLQ--AEQK 204
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE-----EKKKADEAKkkAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 205 altKVSQSLKMENEEFKKRYNDVTSKALQLEEdivsvthKAIEKETELDSLKDKLKKAQCEREQLEcqLKTEKDEKelyK 284
Cdd:PTZ00121 1315 ---KKADEAKKKAEEAKKKADAAKKKAEEAKK-------AAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKK---K 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 285 VHLKNTEIENTKLVSEVQTLKNLDGNKenmithfKEEISRLQFSLAEKENLQRtfllttsSKEDTFILKEQLRKAEEQIQ 364
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKK-------ADELKKAAAAKKKADEAKK-------KAEEKKKADEAKKKAEEAKK 1445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 365 AtrQEAVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAElKLSAVNKDQEKTDTLEHELRREVEDLKLRLQM 444
Cdd:PTZ00121 1446 A--DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK-KAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 445 AADHYK--EKFKECQRLQK-QINKLSDQSANSNSVftKKIGSQQKVNDASINTD--PAATASTVDVKPLPSTAETDFDNL 519
Cdd:PTZ00121 1523 KADEAKkaEEAKKADEAKKaEEKKKADELKKAEEL--KKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKL 1600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 520 TKGQVSEMTKEIADKTEKYNKCKQLLQDEKTKcnKYADELAKMElkwKEQVKIAENIKLElAEVVDNYKLQLAEKEKEIS 599
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--KKVEQLKKKE---AEEKKKAEELKKA-EEENKIKAAEEAKKAEEDK 1674
|
490 500
....*....|....*....|....*...
gi 528946901 600 GLTsywENLSREKEHKRSVENQAERKLE 627
Cdd:PTZ00121 1675 KKA---EEAKKAEEDEKKAAEALKKEAE 1699
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
156-322 |
7.59e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.85 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 156 KTMKEKEELLKLIAvlEKETTQLReqvGRMERELNH-----EKERGDQ-----LQAEQKALT---KVSQSLKMENEEFKK 222
Cdd:PRK00106 27 KSAKEAAELTLLNA--EQEAVNLR---GKAERDAEHikktaKRESKALkkellLEAKEEARKyreEIEQEFKSERQELKQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 223 RYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQcEREQLECQLKTEKDEkELYKVhlKNTEIENTKLVSEVQ 302
Cdd:PRK00106 102 IESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKA-ELERV--AALSQAEAREIILAE 177
|
170 180
....*....|....*....|
gi 528946901 303 TLKNLDGNKENMITHFKEEI 322
Cdd:PRK00106 178 TENKLTHEIATRIREAEREV 197
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-632 |
7.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 352 LKEQLRKAEEQ-IQATRqeavflAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHE 430
Cdd:COG1196 198 LERQLEPLERQaEKAER------YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 431 LRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANsNSVFTKKIGSQQKVNDASINTDPAATAstvdvkplps 510
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-LEERLEELEEELAELEEELEELEEELE---------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 511 TAETDFDNLTKgQVSEMTKEIADKTEKY-NKCKQLLQDEKTKCNKYADELAKMelkwKEQVKIAENIKlELAEVVDNYKL 589
Cdd:COG1196 341 ELEEELEEAEE-ELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEAL----RAAAELAAQLE-ELEEAEEALLE 414
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 528946901 590 QLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKLEGQNSQ 632
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-469 |
8.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 352 LKEQLRKAEEQIQATRQEAVFLAKELsDAVNVRDKTMADLhTAHLENEKVKKQLTDALAEL--KLSAVNKDQektDTLEh 429
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAEL-DALQERREALQRL-AEYSWDEIDVASAEREIAELeaELERLDASS---DDLA- 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 528946901 430 ELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-413 |
9.38e-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: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 158 MKEKEELLKLIAVLEKETTQLReqvgRMERELnhekergDQLQAEQKALTKVsqslkmenEEFKKRYNDVTSKALQLEED 237
Cdd:COG4913 217 MLEEPDTFEAADALVEHFDDLE----RAHEAL-------EDAREQIELLEPI--------RELAERYAAARERLAELEYL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 238 IVSVTHKAIEK-----ETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKvhlknteientklvsevQTLKNLDGNKe 312
Cdd:COG4913 278 RAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELE-----------------AQIRGNGGDR- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528946901 313 nmITHFKEEISRLQFSLAEKENLQRTFllttsskedtfilKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLH 392
Cdd:COG4913 340 --LEQLEREIERLERELEERERRRARL-------------EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
250 260
....*....|....*....|.
gi 528946901 393 TAHLENEKVKKQLTDALAELK 413
Cdd:COG4913 405 EALAEAEAALRDLRRELRELE 425
|
|
| |
