|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
17-120 |
1.58e-47 |
|
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: 163.57 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 17 VIFQNVAKSYLPNAHLECHYTLTPYIHPHPKDWVGIFKVGWSTARDYYTFLWSpmPEHYVEGSTVNCVLAFQGYYLPNDD 96
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 2161896568 97 GEFYQFCYVTHKGEIRGASTPFQF 120
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
125-460 |
1.64e-38 |
|
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: 150.05 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 125 PVEELLTME-----DEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAV------------------LEKETAQLREQ 181
Cdd:pfam07888 2 PLDELVTLEeeshgEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAanrqrekekerykrdreqWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 182 VGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRK 261
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 262 AQHereqlecQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKEnlQRTFLL 341
Cdd:pfam07888 162 AGA-------QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH--RKEAEN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 342 TTsskedtffLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELK-------- 413
Cdd:pfam07888 233 EA--------LLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegrarwaq 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 414 -----LNAMKKDQDKTDTLEHELRREVEDL--------KLRLQMAADhykekfKECQRLQ 460
Cdd:pfam07888 305 eretlQQSAEADKDRIEKLSAELQRLEERLqeermereKLEVELGRE------KDCNRVQ 358
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
150-448 |
4.50e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATS 229
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDG 309
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 310 NKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDtffLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMA 389
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2161896568 390 DLhtaRLENEKVKKQLADAVAELKLnamkkDQDKTDTLEHELRREVEDLKLRLQMAADH 448
Cdd:COG1196 453 EL---EEEEEALLELLAELLEEAAL-----LEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-412 |
7.47e-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: 69.32 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGL 206
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 207 TEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHERE-------QLECQLKTEKDE 279
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 280 KELYKVHLKNTEIENTKLMSEVQTLknldgNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDtffLKEQLRKA 359
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEEL-----LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE---LREELEEA 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2161896568 360 EEQVQATRQEVVFLAKELsDAVNVRDRTMADLHTARLENEKVKKQLADAVAEL 412
Cdd:TIGR02168 474 EQALDAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
752-778 |
1.03e-11 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 59.58 E-value: 1.03e-11
10 20
....*....|....*....|....*..
gi 2161896568 752 KKCPLCELMFPPNYDQSKFEEHVESHW 778
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
779-805 |
1.29e-11 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 59.49 E-value: 1.29e-11
10 20
....*....|....*....|....*..
gi 2161896568 779 KVCPMCSEQFPPDYDQQVFERHVQTHF 805
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-466 |
2.15e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 145 TKAGLLELKiektmKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRF 224
Cdd:TIGR02168 668 TNSSILERR-----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 225 SDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEkelykvhLKNTEIENTKLMSEVQTL 304
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-------LKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 305 KNLDGNKESvithfkeeigRLQLCLAEKENLQRTFLLTTSSKEDtffLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVR 384
Cdd:TIGR02168 816 NEEAANLRE----------RLESLERRIAATERRLEDLEEQIEE---LSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 385 DRTMADLHTARLENEKVKKQLADavAELKLNAMKKDQDKTDTLEHELRREVEDLKLR---------------LQMAADHY 449
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRE--LESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeysltLEEAEALE 960
|
330
....*....|....*..
gi 2161896568 450 KEKFKECQRLQKQINKL 466
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRL 977
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
754-777 |
4.04e-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: 4.04e-11
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-416 |
5.37e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGL 206
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 207 TEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVH 286
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 287 LKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTfllttsskedtffLKEQLRKAEEQVQAT 366
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE-------------LEEEEEALLELLAEL 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2161896568 367 RQEVVFLAKELSDAVNVRDRtMADLHTARLENEKVKKQLADAVAELKLNA 416
Cdd:COG1196 469 LEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-469 |
5.78e-10 |
|
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: 63.16 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 153 KIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHeKERCDQLQAEqKGLTEVTQSLKmENEEFKKRFSDATSKAL 232
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKE-KREYEGYELLK-EKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 233 QLEEDIVSVTHKAIEKETELDSLKDKLR------KAQHEREQLECQLKTEKDEKELYK----VHLKNTEIEntKLMSEVQ 302
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEelnkkiKDLGEEEQLRVKEKIGELEAEIASlersIAEKERELE--DAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 303 TLKNLDGNKESVITHFKEEIGRLQlclAEKENLQRTFlltTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVN 382
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEER---KRRDKLTEEY---AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 383 VRDRTMADLhtARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQ 462
Cdd:TIGR02169 400 EINELKREL--DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
....*..
gi 2161896568 463 INKLSDQ 469
Cdd:TIGR02169 478 YDRVEKE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-412 |
8.65e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 121 RASSPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQ 200
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 201 AEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEK 280
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 281 ELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFF--LKEQLRK 358
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEeeARRRLKR 976
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2161896568 359 AEEQVQATrQEVVFLAKELSDAVNVR----DRTMADLHTARlenekvkKQLADAVAEL 412
Cdd:TIGR02168 977 LENKIKEL-GPVNLAAIEEYEELKERydflTAQKEDLTEAK-------ETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
151-443 |
2.13e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 151 ELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEqkgLTEVTQSLKMENEEFKKRFSDatsK 230
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR---LEEIEQLLEELNKKIKDLGEE---E 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 231 ALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKN---- 306
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeled 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 307 LDGNKESVITHFKEEIGRLQLCLAEKENLQRTFlltTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDR 386
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREI---NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2161896568 387 TMADLHTARLENEKVKKQLADavAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQ 443
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSK--YEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
155-622 |
2.86e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 155 EKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKrfsdatskalql 234
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 235 eediVSVTHKAI--EKETELDSLKDKLRKAQHEREQLECQLKTekdekelykvhlknTEIENTKLMSEVQTLKNLDGNKE 312
Cdd:pfam05483 343 ----AKAAHSFVvtEFEATTCSLEELLRTEQQRLEKNEDQLKI--------------ITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 313 SvithfkeEIGRLQLCLAEKENLqrtfllttsskedtFFLKEQLRKAEEQVQATRQEVVFL----AKELSD-AVNVRDRT 387
Cdd:pfam05483 405 V-------ELEELKKILAEDEKL--------------LDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDlEIQLTAIK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 388 MADLHTARlENEKVKKQLADavAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLS 467
Cdd:pfam05483 464 TSEEHYLK-EVEDLKTELEK--EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 468 DQSANNNNVFT------KKMGNQQKVNDASVNTDPATSASTVDVKPSPSAAETDFDIVTKGQVCEMTKEIADKTEKYNKC 541
Cdd:pfam05483 541 EKEMNLRDELEsvreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 542 KQLLQDEKAKCNKYADELAKMELKwkeqvkiAENVKFELAEVQDNYKLQLaeKDKEISGltshlENLSREKELKRSLENQ 621
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELE-------LASAKQKFEEIIDNYQKEI--EDKKISE-----EKLLEEVEKAKAIADE 686
|
.
gi 2161896568 622 A 622
Cdd:pfam05483 687 A 687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-488 |
3.02e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMK------EKEELLKLIAVLEKEtaQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKR 223
Cdd:TIGR02168 205 LERQAEKAERykelkaELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 224 FSDATSKALQLEEDIVsvthkaiEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQT 303
Cdd:TIGR02168 283 IEELQKELYALANEIS-------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 304 LKNLDGNKESVITHFKEEIGRLQlclaekENLQRtfllttsskedtffLKEQLRKAEEQVQATRQEVVFLAKELSDAVNV 383
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELE------EQLET--------------LRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 384 RDRTMADlhtarlenekvKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQI 463
Cdd:TIGR02168 416 RERLQQE-----------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340
....*....|....*....|....*
gi 2161896568 464 NKLSDQSANNNNVFTKKMGNQQKVN 488
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-451 |
6.82e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 171 LEKETAQLREQVGKMERELNhekercdQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKET 250
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELS-------SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 251 ELDSLKDKLRKAQHEREQLECQLktEKDEKELYKVHLKNTEIENTKLMSEVQtlkNLDGNKESVithfKEEIGRLQLCLA 330
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKL----EEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 331 EKE-NLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAV 409
Cdd:TIGR02169 816 EIEqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2161896568 410 AELKlnAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKE 451
Cdd:TIGR02169 896 AQLR--ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-627 |
7.70e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 146 KAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTqSLKMENEEFKKRFS 225
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS-RLEEEINGIEERIK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 226 DATSKALQLEEdivsVTHKAIEKETELDSLK------DKLRKAQHEREQLECQLK---TEKDEKELYKVHLKNTEIEN-- 294
Cdd:PRK03918 332 ELEEKEERLEE----LKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTgltPEKLEKELEELEKAKEEIEEei 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 295 TKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFFLKEqLRKAEEQVQATRQEVVFLA 374
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKE-LKEIEEKERKLRKELRELE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 375 KELSdavnvRDRTMADLHTARLENEKVKKQLADAVAElKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKfk 454
Cdd:PRK03918 487 KVLK-----KESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-- 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 455 ecQRLQKQINKLSDQSANNNNVFTKKmgnqqkvndasvntdpatSASTVDvkpspsaaetdfdivtkgQVCEMTKEIADK 534
Cdd:PRK03918 559 --AELEKKLDELEEELAELLKELEEL------------------GFESVE------------------ELEERLKELEPF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 535 TEKYNKCK---QLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDNY--------KLQLAEKDKEISGLTS 603
Cdd:PRK03918 601 YNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyeelREEYLELSRELAGLRA 680
|
490 500
....*....|....*....|....*
gi 2161896568 604 HLENL-SREKELKRSLENQAERKME 627
Cdd:PRK03918 681 ELEELeKRREEIKKTLEKLKEELEE 705
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
779-805 |
9.98e-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: 51.11 E-value: 9.98e-09
10 20
....*....|....*....|....*..
gi 2161896568 779 KVCPMCSEQFPPDYDQQVFERHVQTHF 805
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-413 |
1.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 146 KAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELN------HEKE-RCDQLQAEQKGLTEVTQSLKMENE 218
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelrlevSELEeEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 219 EFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLM 298
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 299 SEVQTLKnldgNKESVIThfkeeiGRLQLCLAEKENLQRTFLLTTSSKEDtfflkEQLRKAEEQVQATRQEVVFLAKELS 378
Cdd:TIGR02168 386 SKVAQLE----LQIASLN------NEIERLEARLERLEDRRERLQQEIEE-----LLKKLEEAELKELQAELEELEEELE 450
|
250 260 270
....*....|....*....|....*....|....*
gi 2161896568 379 DAVNVRDRTMADLHTARLENEKVKKQLADAVAELK 413
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
781-804 |
1.63e-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: 50.65 E-value: 1.63e-08
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
149-625 |
2.41e-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: 58.06 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 149 LLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQkgltevtQSLKMENEEFKKRFSDAT 228
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL-------RDEQEEIESSKQEIEKEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 229 SKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLD 308
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 309 GNKESVITHFKEEIGRLQLcLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEE-----QVQATRQEVVFLAKELSDAVNV 383
Cdd:pfam02463 345 KELEIKREAEEEEEEELEK-LQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelksEEEKEAQLLLELARQLEDLLKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 384 RDRTMadlhtARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQI 463
Cdd:pfam02463 424 EKKEE-----LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 464 NKLSDQSANNNNVFTKKMGNQQKVNDASV---NTDPATSASTVDVKPS---PSAAETDFDIVTKGQVCEMTKEIADKTEK 537
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRIISAhgrLGDLGVAVENYKVAIStavIVEVSATADEVEERQKLVRALTELPLGAR 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 538 YNKckqlLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLENLSREKELKRS 617
Cdd:pfam02463 579 KLR----LLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
....*...
gi 2161896568 618 LENQAERK 625
Cdd:pfam02463 655 EEGLAEKS 662
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
150-610 |
2.81e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELnhEKERCDQLQAEQKGLTEVTQSLKM---------ENEEF 220
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL--EAAKCLKEDMLEDSNTQIEQLRKMmlshegvlqEIRSI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 221 KKRFSDATSKALQlEEDIVSVTH-----KAIEK-----ETELDSLKDKLRKAQherEQLECqLKTEKDEKELYKVHLKNT 290
Cdd:pfam15921 193 LVDFEEASGKKIY-EHDSMSTMHfrslgSAISKilrelDTEISYLKGRIFPVE---DQLEA-LKSESQNKIELLLQQHQD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 291 EIEntKLMSEVQT-LKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFF-LKEQLRKA----EEQVQ 364
Cdd:pfam15921 268 RIE--QLISEHEVeITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSqLRSELREAkrmyEDKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 365 ATRQEVVFLAKELSDAVNVRDRTMADlhTARLENEkVKKQLADAVAELKLNAMKKDQDK---------TDTLEHeLRREV 435
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQE--SGNLDDQ-LQKLLADLHKREKELSLEKEQNKrlwdrdtgnSITIDH-LRREL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 436 EDLKLRLQMAADHYKEKFKECQ-RLQKQINKLsdQSANNNnvftkkmgnQQKVNDASVNTDpatsastvdvkpspSAAET 514
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQgQMERQMAAI--QGKNES---------LEKVSSLTAQLE--------------STKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 515 DFDIVTKGQVCEMTKEIADKTekYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFE---LAEVQ---DNYK 588
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERT--VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQtecEALK 554
|
490 500
....*....|....*....|..
gi 2161896568 589 LQLAEKDKEISGLTSHLENLSR 610
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQ 576
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
781-804 |
4.53e-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: 4.53e-08
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-626 |
6.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATS 229
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KALQLEEDIVSvtHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDG 309
Cdd:TIGR02168 422 EIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 310 NKES----VITHFKEEI----------------------------GRLQLCLAEKENLQR--------------TFLLTT 343
Cdd:TIGR02168 500 NLEGfsegVKALLKNQSglsgilgvlselisvdegyeaaieaalgGRLQAVVVENLNAAKkaiaflkqnelgrvTFLPLD 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 344 SSKEDTF-FLKEQLRKAEEQVQATRQEVVFLAKELSDAVN---------------------------------------- 382
Cdd:TIGR02168 580 SIKGTEIqGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpgg 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 383 -----VRDRTMADLHTAR--LENEKVKKQLADAVAELK--LNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKF 453
Cdd:TIGR02168 660 vitggSAKTNSSILERRReiEELEEKIEELEEKIAELEkaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 454 KECQRLQKQINKLSDQSANNNNvftKKMGNQQKVNDASVNTDpATSASTVDVKPSPSAAETDFDIVT------KGQVCEM 527
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALRealdelRAELTLL 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 528 TKEIADKTEKYNKckqlLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLEN 607
Cdd:TIGR02168 816 NEEAANLRERLES----LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
570
....*....|....*....
gi 2161896568 608 LSREKELKRSLENQAERKM 626
Cdd:TIGR02168 892 LRSELEELSEELRELESKR 910
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-466 |
8.11e-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: 56.23 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 153 KIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKAL 232
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 233 QLEEDIVSVTHKAIEKetELDSLKDKLRKAQHEREQLECQLKTEKDEKElykvhlkntEIENTKLMSEvQTLKNLDGNKE 312
Cdd:TIGR02169 797 QAELSKLEEEVSRIEA--RLREIEQKLNRLTLEKEYLEKEIQELQEQRI---------DLKEQIKSIE-KEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 313 SvithFKEEIGRLQLCLAEKEnlqrtfllttSSKEDtffLKEQLRKAEEQVQATRQEVvflaKELSDAVNVRDRTMADLH 392
Cdd:TIGR02169 865 E----LEEELEELEAALRDLE----------SRLGD---LKKERDELEAQLRELERKI----EELEAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161896568 393 TARLENEKVKKQLADAVAELK-----LNAMKKDQDKTDTLEHELRReVEDLKLRlqmAADHYKEKFKECQRLQKQINKL 466
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEeipeeELSLEDVQAELQRVEEEIRA-LEPVNML---AIQEYEEVLKRLDELKEKRAKL 998
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
754-777 |
1.06e-07 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 48.34 E-value: 1.06e-07
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-585 |
1.37e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATS 229
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KalQLEEDIVSVTHKAIEKETELD-------SLKDKLRKAQHEREQLEC--------------QLKTEKDEKELYKVHLK 288
Cdd:TIGR04523 310 K--ELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESensekqreleekqnEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 289 NTEIENTKLMSEVQTLKNLDGNKESVITHFKEEigrLQLCLAEKENLqrtfllttssKEDTFFLKEQLRKAEEQVQATRQ 368
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQE---KELLEKEIERL----------KETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 369 EVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELK-LNAMKKDQDKTDTlehELRREVEDLKLRLQMAAD 447
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKkLNEEKKELEEKVK---DLTKKISSLKEKIEKLES 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 448 HYKEKFKECQRLQKQINKLsDQSANNNNVFTKKMGNQQKVNDASVNTDpatsastvDVKPSPSAAETDFDIVTKgQVCEM 527
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKD-DFELKKENLEKEIDEKNKEIEELKQTQK--------SLKKKQEEKQELIDQKEK-EKKDL 601
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2161896568 528 TKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQD 585
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
116-447 |
4.73e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 116 TPFQFRASSPVEELLTMEDEGNSdMLVVTTKAGLLELKiektMKEKEELLKLiavleketaqLREQVGKMERELNHEKER 195
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQ----MAEKDKVIEI----------LRQQIENMTQLVGQHGRT 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 196 CDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEediVSVTHKAIEKETELDSLKDKLRKA---QHEREQLECQ 272
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE---ARVSDLELEKVKLVNAGSERLRAVkdiKQERDQLLNE 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 273 LKTEKDE----KELYKVHLKN-----TEIENTKLMSEVQtLKNLDGNKESVITHFKEEIG------RLQLCLAEKENLQR 337
Cdd:pfam15921 662 VKTSRNElnslSEDYEVLKRNfrnksEEMETTTNKLKMQ-LKSAQSELEQTRNTLKSMEGsdghamKVAMGMQKQITAKR 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 338 TFLLTTSSKEDtfFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKLNAM 417
Cdd:pfam15921 741 GQIDALQSKIQ--FLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818
|
330 340 350
....*....|....*....|....*....|
gi 2161896568 418 KKDQDKtDTLEhelRREVEDLKLRLQMAAD 447
Cdd:pfam15921 819 QFAECQ-DIIQ---RQEQESVRLKLQHTLD 844
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
160-469 |
5.37e-07 |
|
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: 53.64 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 160 EKEELLkliAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEfkkrfSDATSKALQLEEdiV 239
Cdd:pfam01576 58 EAEEMR---ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-----EEAARQKLQLEK--V 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 240 SVTHKAIEKETELDSLKDKLRKAQHEREQLECQLK------TEKDE--KELYKVHLKN----TEIENtKLMSEVQTLKNL 307
Cdd:pfam01576 128 TTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISeftsnlAEEEEkaKSLSKLKNKHeamiSDLEE-RLKKEEKGRQEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 308 DGNK---ESVITHFKEEIGRLQLCLAEkenlqrtfllttsskedtffLKEQLRKAEEQVQATRQEV-------VFLAKEL 377
Cdd:pfam01576 207 EKAKrklEGESTDLQEQIAELQAQIAE--------------------LRAQLAKKEEELQAALARLeeetaqkNNALKKI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 378 SDAVNVRDRTMADLHTARLENEKVKKQLADAVAElkLNAMKKD-QDKTDT--LEHELR----REVEDLKLRLQMAADHYK 450
Cdd:pfam01576 267 RELEAQISELQEDLESERAARNKAEKQRRDLGEE--LEALKTElEDTLDTtaAQQELRskreQEVTELKKALEEETRSHE 344
|
330 340
....*....|....*....|
gi 2161896568 451 EKFKEC-QRLQKQINKLSDQ 469
Cdd:pfam01576 345 AQLQEMrQKHTQALEELTEQ 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-413 |
6.24e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 197 DQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTE 276
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 277 KDE-KELYKVHLKNTEIENTKLM----SEVQTLKNLDGNKeSVITHFKEEIGRLQlclAEKENLQRtfllttsskedtff 351
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLK-YLAPARREQAEELR---ADLAELAA-------------- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2161896568 352 LKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELK 413
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-471 |
7.05e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 251 ELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLA 330
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 331 EKENLqrtfllttsskedtffLKEQLRKAEEQVQATRQEVVFLAKELSDAV----------NVRDRTMADLHTARLENEK 400
Cdd:COG4942 101 AQKEE----------------LAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylaPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2161896568 401 VKKQLADAVAELK--LNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSA 471
Cdd:COG4942 165 LRAELEAERAELEalLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-469 |
9.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLE--KETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEF---KKRF 224
Cdd:COG4717 107 LEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 225 SDATSKALQ-LEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYK------------------- 284
Cdd:COG4717 187 SLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglgg 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 285 ------------------------VHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRlqlclaeKENLQRTFL 340
Cdd:COG4717 267 sllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGL-------PPDLSPEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 341 LTTSSK-EDTFFLKEQLRKAEEQVQatRQEVVFLAKELSDAVNVRDRTM-ADLHTARLENEKVKKQLADAVAELKLNAMK 418
Cdd:COG4717 340 LELLDRiEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2161896568 419 KDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:COG4717 418 LEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-614 |
1.42e-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: 51.94 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 149 LLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNhekercdQLQAEQKGLTEVTQSLKMENEEFKKRFSDAT 228
Cdd:TIGR04523 201 LLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN-------EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 229 SKALQLEEDIvsvthkaIEKETELDSLKDKLRKAQHEREQ-LECQLKTEKDEKELYKVHLKNTEIENTKLMSEV------ 301
Cdd:TIGR04523 274 KELEQNNKKI-------KELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLneqisq 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 302 --QTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDtffLKEQLRKAEEQVQATRQEVVFLAKELsd 379
Cdd:TIGR04523 347 lkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEK-- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 380 avNVRDRTMADLHTARLENEKVKKQLA--DAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQ 457
Cdd:TIGR04523 422 --ELLEKEIERLKETIIKNNSEIKDLTnqDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 458 RLQKQINKLSDQSANNNNVFTKKMGNQQKVNDasvntdpatsastvdvkpspsaaetdfdivtkgQVCEMTKEIADKTEK 537
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLES---------------------------------EKKEKESKISDLEDE 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2161896568 538 YNKCKQLLQDEKAKcnKYADELAKMELKWKEQVKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLENLSREKEL 614
Cdd:TIGR04523 547 LNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-537 |
1.49e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 151 ELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQL-QAEQKGLTEVT----QSLKMENEEFKKRfS 225
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMklyeEEKKMKAEEAKKA-E 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 226 DATSKALQL--EEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQT 303
Cdd:PTZ00121 1617 EAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 304 LKNLDGNKESVITHFKEEIGRL-QLCLAEKENLQRTFLLTTSSKEDTfFLKEQLRKAEEQVQATRQEVVFLAKELSDAVN 382
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAeELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 383 VRDRTMADlhTARLENEKVKKQLADAVAELKLN-AMKKDQDKTDTLEHELRREVEDLKLR-LQMAADHYKEKFKECQRLQ 460
Cdd:PTZ00121 1776 EKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNfANIIEGGKEGNLVINDSKEMEDSAIKeVADSKNMQLEEADAFEKHK 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 461 KQINKLSDQSANNNNVFTKKMGNQQKVNDASVNTDPATSASTVDVK---PSPSAAETDFDIV-TKGQVCEMTKEIADKTE 536
Cdd:PTZ00121 1854 FNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEreiPNNNMAGKNNDIIdDKLDKDEYIKRDAEETR 1933
|
.
gi 2161896568 537 K 537
Cdd:PTZ00121 1934 E 1934
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
158-469 |
1.60e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 158 MKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQkgltevtqslKMENEEFKKRFSDATSKALQLEED 237
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ----------LKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 238 IVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITH 317
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 318 FKEEIGRLQlclaEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLE 397
Cdd:pfam02463 319 SEKEKKKAE----KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161896568 398 NEKVKK-------QLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:pfam02463 395 EELELKseeekeaQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
156-452 |
1.87e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 156 KTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMEN--EEFKKRFSDATSKALQ 233
Cdd:COG5022 807 GSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETiyLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 234 LEEDIVSVTHKAiEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKelYKVHLKNTEIENTKLMSEVQtlknldgnkes 313
Cdd:COG5022 887 LKIDVKSISSLK-LVNLELESEIIELKKSLSSDLIENLEFKTELIAR--LKKLLNNIDLEEGPSIEYVK----------- 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 314 vithfKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTfflKEQLRKAEEQVQATRQEVVFLAKEL------SDAVNVRDRT 387
Cdd:COG5022 953 -----LPELNKLHEVESKLKETSEEYEDLLKKSTIL---VREGNKANSELKNFKKELAELSKQYgalqesTKQLKELPVE 1024
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 388 MADLHTA--RLENEKVKKQLADAVAELKLNAMKKDQD-KTDTLEHELRRE--VEDLKLRLQMAADHYKEK 452
Cdd:COG5022 1025 VAELQSAskIISSESTELSILKPLQKLKGLLLLENNQlQARYKALKLRREnsLLDDKQLYQLESTENLLK 1094
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
151-593 |
3.58e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 151 ELKIEKTMKEK--EELLKLIAVLEKETAQLREQVGKMERELNHEKercDQLQAEQKGLTEVTQSLKMENEEFKKRFSDAT 228
Cdd:pfam15921 332 ELREAKRMYEDkiEELEKQLVLANSELTEARTERDQFSQESGNLD---DQLQKLLADLHKREKELSLEKEQNKRLWDRDT 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 229 SKALQLEEDIVSVTHKAIEK---ETELDSLKDKLrKAQHEREQLECQLKTEkdekELYKVHLKNTEIENTKLM------- 298
Cdd:pfam15921 409 GNSITIDHLRRELDDRNMEVqrlEALLKAMKSEC-QGQMERQMAAIQGKNE----SLEKVSSLTAQLESTKEMlrkvvee 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 299 ---------SEVQTLKNLDGN---KESVITHFKEEI----GRLQLCLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQ 362
Cdd:pfam15921 484 ltakkmtleSSERTVSDLTASlqeKERAIEATNAEItklrSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 363 VQATRQEVvflaKELSDAVNVRDRTMADLhtaRLENEKVKKQLADAVAELKlnAMKKDQDKTDTLEHELRREVEDLKL-- 440
Cdd:pfam15921 564 IEILRQQI----ENMTQLVGQHGRTAGAM---QVEKAQLEKEINDRRLELQ--EFKILKDKKDAKIRELEARVSDLELek 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 441 ---------RLQMAADHYKEK---FKECQRLQKQINKLSD------QSANNNNVFTKKMGNQQKVNDASVNTDPATSAST 502
Cdd:pfam15921 635 vklvnagseRLRAVKDIKQERdqlLNEVKTSRNELNSLSEdyevlkRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 503 V------DVKPSPSAAETDFDIVTK-GQVCEMTKEIA---DKTEKYNKCKQLLQDEKAKC-----------NKYADELAK 561
Cdd:pfam15921 715 LksmegsDGHAMKVAMGMQKQITAKrGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLsqelstvatekNKMAGELEV 794
|
490 500 510
....*....|....*....|....*....|....*....
gi 2161896568 562 M---ELKWKEQVKIAE----NVKFELAEVQDNYKLQLAE 593
Cdd:pfam15921 795 LrsqERRLKEKVANMEvaldKASLQFAECQDIIQRQEQE 833
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
123-462 |
3.66e-06 |
|
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: 50.52 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 123 SSPVEELLTMEDEGNSdmlvvttkagLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAE 202
Cdd:pfam07111 69 SRQLQELRRLEEEVRL----------LRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 203 QKGLTEVtQSLKMEN-----EEFKKRFSDATSKALQLEEDIVSVTHK---------AIEKETELdsLKDKLRKAQherEQ 268
Cdd:pfam07111 139 QRELEEI-QRLHQEQlssltQAHEEALSSLTSKAEGLEKSLNSLETKrageakqlaEAQKEAEL--LRKQLSKTQ---EE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 269 LECQ------LKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLqrtflLT 342
Cdd:pfam07111 213 LEAQvtlvesLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEE-----LT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 343 TSSKEDTFFLKEQLRKAEEQVQATRQEVVFLakelsdavnvrdrtMADLHTARLENEKVKKQLADAVAELKLNAMKKD-- 420
Cdd:pfam07111 288 RKIQPSDSLEPEFPKKCRSLLNRWREKVFAL--------------MVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSqe 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2161896568 421 --------QDKTDTLEHElRREVEDLKLRLQMAadhykekfKECQRLQKQ 462
Cdd:pfam07111 354 qailqralQDKAAEVEVE-RMSAKGLQMELSRA--------QEARRRQQQ 394
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-469 |
4.23e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 352 LKEQLRKAEEQVQATRQE--VVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEH 429
Cdd:COG3206 187 LRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ 266
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2161896568 430 ELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
152-463 |
1.19e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 152 LKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKA 231
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 232 LQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQ-------------------LECQLKTEKDEKELYKVHLKNTEI 292
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 293 EN--------TKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKEnlQRTFLLTTSSKEDtfflKEQLRKAEEQVQ 364
Cdd:PRK02224 495 EErleraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR--ERAAELEAEAEEK----REAAAEAEEEAE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 365 ATRQEVVFLAKELSDAVNVRDR--TMADLHTARLENEKVKKQLADAVAEL-KLNAMKKDQ-----DKTDTLEHELRRE-V 435
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALaELNDERRERlaekrERKRELEAEFDEArI 648
|
330 340 350
....*....|....*....|....*....|....*
gi 2161896568 436 EDLKLRLQMA-------ADHYKEKFKECQRLQKQI 463
Cdd:PRK02224 649 EEAREDKERAeeyleqvEEKLDELREERDDLQAEI 683
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
184-479 |
1.26e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 184 KMERELNHEKERCDQLQAEQKGL-------TEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLK 256
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLdknlnkdEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 257 DKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAeKENLQ 336
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID-KIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 337 RTFLLTTSSKEDTFF-----LKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAE 411
Cdd:TIGR04523 196 LLKLELLLSNLKKKIqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2161896568 412 LKlNAMKKDQDKTDTLEhELRREVEDLKlrLQMAADHYKEKFKECQRLQKQINKLSDQSANNNNVFTK 479
Cdd:TIGR04523 276 LE-QNNKKIKELEKQLN-QLKSEISDLN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ 339
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-631 |
1.96e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKErcdQLQAEQKGLTeVTQSLKMENEEFKKRFSDATS 229
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN---KLLKLELLLS-NLKKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNldg 309
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 310 NKESVIT-HFKEEIgrlqlclaekenlqrtflltTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNvrdrtm 388
Cdd:TIGR04523 303 QKEQDWNkELKSEL--------------------KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES------ 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 389 adlhtarlENEKVKKQLADAVAELKlNAMKKDQDKTDTLEhELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSD 468
Cdd:TIGR04523 357 --------ENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 469 QSANNNNVFTKKmgnqqkvndasvntdpatsastvdvkpspsaaetdfdivtKGQVCEMTKEIADKTEKYNKCKQLLQDE 548
Cdd:TIGR04523 427 EIERLKETIIKN----------------------------------------NSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 549 KAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDNYKL---QLAEKDKEISGLTSHLENLSREKELKRSLENQAERK 625
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleeKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
....*.
gi 2161896568 626 MEGQNF 631
Cdd:TIGR04523 547 LNKDDF 552
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
150-282 |
2.51e-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: 46.93 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMEREL----NHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFS 225
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELrqlkQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2161896568 226 DATSKALQLEEDIVSVTHKAIEKETELDSLKDKLrkaqhereqLECQLKTEKDEKEL 282
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKL---------EQCRGFTFKEIEKL 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-442 |
3.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 168 IAVLEKETAQLreqvgkmERELNHEKERCDQLQAEQKGLTEvtqslkmeneefkkrFSDATSKALQLEEDIVSV--THKA 245
Cdd:COG4913 612 LAALEAELAEL-------EEELAEAEERLEALEAELDALQE---------------RREALQRLAEYSWDEIDVasAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 246 I-EKETELDSLK---DKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEE 321
Cdd:COG4913 670 IaELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 322 IGRLQLCLAEKENLQRTFLLTTSSKEDTffLKEQLRKAEEQVQATRQEvvFLAKELSDAVNVrDRTMADLHT-----ARL 396
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDA--LRARLNRAEEELERAMRA--FNREWPAETADL-DADLESLPEylallDRL 824
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2161896568 397 ENEKVKKQLADAvAELKLNAMkkDQDKTDtLEHELRREVEDLKLRL 442
Cdd:COG4913 825 EEDGLPEYEERF-KELLNENS--IEFVAD-LLSKLRRAIREIKERI 866
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-623 |
3.27e-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: 47.86 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 146 KAGLLELKIEKTMKEkEELLKLIAVLEKETAQ-------LRE---QVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKM 215
Cdd:pfam01576 228 QAQIAELRAQLAKKE-EELQAALARLEEETAQknnalkkIREleaQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 216 ENEEFKKrfSDATSKALQLE-EDIVSVTHKAIEKETE----------------LDSLKDKLRKAQHEREQLE-CQLKTEK 277
Cdd:pfam01576 307 ELEDTLD--TTAAQQELRSKrEQEVTELKKALEEETRsheaqlqemrqkhtqaLEELTEQLEQAKRNKANLEkAKQALES 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 278 DEKELyKVHLK-------NTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQlclAEKENLqrTFLLTTSSKEDTF 350
Cdd:pfam01576 385 ENAEL-QAELRtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ---SELESV--SSLLNEAEGKNIK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 351 FLKE------QLRKAEEQVQA-TRQEVVFLAK--ELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKlnamKKDQ 421
Cdd:pfam01576 459 LSKDvsslesQLQDTQELLQEeTRQKLNLSTRlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK----KKLE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 422 DKTDTLE------HELRREVEDLKLRlqmaadhYKEKFKECQRLQKQINKLsdqsannnnvftkkmgnQQKVNDASVNTD 495
Cdd:pfam01576 535 EDAGTLEaleegkKRLQRELEALTQQ-------LEEKAAAYDKLEKTKNRL-----------------QQELDDLLVDLD 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 496 patsastvdvkpspsaaetdfdivTKGQVCemtkeiADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAEN 575
Cdd:pfam01576 591 ------------------------HQRQLV------SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2161896568 576 VKFELAEVQD-------NYKLQLAEKDKEISGLTSHLENLSREKELKRSLENQAE 623
Cdd:pfam01576 641 LARALEEALEakeelerTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
151-303 |
3.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 151 ELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAE----QKGLTEVTQSLKMENEEFKKR--- 223
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 224 -------------------FSDATSKALQLeEDIVSVTHKAIEketELDSLKDKLRKAQHEREQLECQLKTEKDEKELYK 284
Cdd:COG3883 95 lyrsggsvsyldvllgsesFSDFLDRLSAL-SKIADADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170
....*....|....*....
gi 2161896568 285 VHLKNTEIENTKLMSEVQT 303
Cdd:COG3883 171 AELEAQQAEQEALLAQLSA 189
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
150-281 |
3.73e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKG----LTEVT-----QSLKMENEEF 220
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqLGNVRnnkeyEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2161896568 221 KKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKE 281
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-446 |
4.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 149 LLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDAT 228
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 229 SKALQLEEDIVSVthkaiekETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLD 308
Cdd:COG4372 108 EEAEELQEELEEL-------QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 309 GNKEsVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTM 388
Cdd:COG4372 181 AEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2161896568 389 ADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAA 446
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-281 |
4.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 145 TKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMEREL-NHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKR 223
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2161896568 224 FSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKE 281
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
134-296 |
4.49e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 134 DEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERC--DQLQAEQKGLTEVTQ 211
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 212 SLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYK--VHLKN 289
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKqeVKQIK 651
|
....*..
gi 2161896568 290 TEIENTK 296
Cdd:TIGR04523 652 ETIKEIR 658
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-630 |
5.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 153 KIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENeefkKRFSDATSKAL 232
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED----AKKAEAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 233 QLEedivsvthKAIEKETELDSLK-DKLRKAQHEREQLEC-QLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGN 310
Cdd:PTZ00121 1186 EVR--------KAEELRKAEDARKaEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 311 KESVITHFKEEIGRLQlcLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQAT--RQEVVFLAKELSDAVNVRDRTM 388
Cdd:PTZ00121 1258 EEARMAHFARRQAAIK--AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 389 ADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSD 468
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 469 QSANNNNVfTKKMGNQQKVNDASVNTDPATSAStvDVKPSPSAAETDFDIVTKGQVCEMTKEIADKTEKYNKCKQLLQD- 547
Cdd:PTZ00121 1416 AKKKADEA-KKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKa 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 548 EKAKcnKYADELAKMELKWK--EQVKIAENVKF--ELAEVQDNYKLQLAEKDKEIsgltSHLENLSREKELKRSLE---- 619
Cdd:PTZ00121 1493 EEAK--KKADEAKKAAEAKKkaDEAKKAEEAKKadEAKKAEEAKKADEAKKAEEK----KKADELKKAEELKKAEEkkka 1566
|
490
....*....|.
gi 2161896568 620 NQAERKMEGQN 630
Cdd:PTZ00121 1567 EEAKKAEEDKN 1577
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
155-613 |
5.45e-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: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 155 EKTMKEKEELLKLIAV----LEKETAQLREQVGKMERELNHEKERcdqlqaeqkgltevtqsLKMENEEFKKRFSDATSk 230
Cdd:pfam12128 397 DKLAKIREARDRQLAVaeddLQALESELREQLEAGKLEFNEEEYR-----------------LKSRLGELKLRLNQATA- 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 231 alqlEEDIvsVTHKAIeKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGN 310
Cdd:pfam12128 459 ----TPEL--LLQLEN-FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFP 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 311 KESVITHF--------KEEIGRlqlcLAEKENLQRTFL-----LTTSSKEDTFF--------------------LKEQLR 357
Cdd:pfam12128 532 QAGTLLHFlrkeapdwEQSIGK----VISPELLHRTDLdpevwDGSVGGELNLYgvkldlkridvpewaaseeeLRERLD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 358 KAEEQVQATRQEVVFLAKELSDA---VNVRDRTM---------ADLHTARLENEkvKKQLADAVAELKLNAMKKDQDKTD 425
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQAngeLEKASREEtfartalknARLDLRRLFDE--KQSEKDKKNKALAERKDSANERLN 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 426 TLEHELRRevedLKLRLQMAADHYKEKFKE--CQRLQKQINKLSDQSANNNNVFTKKMG--NQQKVNDASVNTDPATSAS 501
Cdd:pfam12128 686 SLEAQLKQ----LDKKHQAWLEEQKEQKREarTEKQAYWQVVEGALDAQLALLKAAIAArrSGAKAELKALETWYKRDLA 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 502 TVDVKPspsaaETDFDIvtKGQVCEMTKEIAD--------------KTEKYNKCKQLLQDEKAKCNKYADELaKMELKwk 567
Cdd:pfam12128 762 SLGVDP-----DVIAKL--KREIRTLERKIERiavrrqevlryfdwYQETWLQRRPRLATQLSNIERAISEL-QQQLA-- 831
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2161896568 568 eqvKIAENVKFELAEVQDNYKL---QLAEKDKEISGLTSHLENLSREKE 613
Cdd:pfam12128 832 ---RLIADTKLRRAKLEMERKAsekQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-307 |
5.53e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLtevTQSLKMENEEFKKR------ 223
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 224 ---------------FSDATSKA----------LQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKD 278
Cdd:COG4942 116 lgrqpplalllspedFLDAVRRLqylkylaparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190
....*....|....*....|....*....|...
gi 2161896568 279 EKELY----KVHLKNTEIENTKLMSEVQTLKNL 307
Cdd:COG4942 196 ERQKLlarlEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-624 |
7.30e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELlkliavlEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATS 229
Cdd:PRK02224 263 LRETIAETEREREEL-------AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKElykvhlkntEIEntklmSEVQTLKNLDG 309
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE---------ELE-----EEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 310 NKEsviTHFKEEIGRLQLCLAEKENL-QRTFLLTTSSKEdtffLKEQLRKAEEQVQATR-----QEV--VFLAKELSDAV 381
Cdd:PRK02224 402 DAP---VDLGNAEDFLEELREERDELrEREAELEATLRT----ARERVEEAEALLEAGKcpecgQPVegSPHVETIEEDR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 382 NVRDRTMADLHTARLENEKVKKQLADAVAelklnaMKKDQDKTDTLehelRREVEDLKLRLQMAADHYKEKFKECQRLQK 461
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAED------LVEAEDRIERL----EERREDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 462 QINKLSDQSANNNNVFTKKMGNQQKVND--ASVNTDPATSASTVDvkpSPSAAETDFDIVT--KGQVCEMTKEIADKTEK 537
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREevAELNSKLAELKERIE---SLERIRTLLAAIAdaEDEIERLREKREALAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 538 YNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKiaENVKFELAEVQDNYKLQLAEKD---KEISGLTSHLENLSREKEL 614
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEARIEEAREDK--ERAEEYLEQVEEKLDELREERDdlqAEIGAVENELEELEELRER 699
|
490
....*....|
gi 2161896568 615 KRSLENQAER 624
Cdd:PRK02224 700 REALENRVEA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-300 |
9.01e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNhekercdQLQAEQKGLTEVTQSLKMENEEFKKRFSDATS 229
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN-------ELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2161896568 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLktEKDEKELYKVHLKNTEIENTKLMSE 300
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY--DRVEKELSKLQRELAEAEAQARASE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-632 |
1.05e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 351 FLKEQLRKAEEQVQATRqeVVFLAKELsDAVNVRDRTMADLHtARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHE 430
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREEL-EELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 431 LRREVEDLKLRLQmaadHYKEKFkecQRLQKQINKLSDQSANNnnvftkkmgnQQKVNDASvntdpatsastvdvkpsps 510
Cdd:TIGR02168 293 LANEISRLEQQKQ----ILRERL---ANLERQLEELEAQLEEL----------ESKLDELA------------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 511 aaetdfdivtkgqvcemtKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVqdnyKLQ 590
Cdd:TIGR02168 337 ------------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQ 394
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2161896568 591 LAEKDKEISGLTSHLENLSREKELKRSLENQAERKMEGQNFQ 632
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
127-455 |
1.59e-04 |
|
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: 45.07 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 127 EELLTMEDEGNS-----DMLVVTT-KAGLLELKIE---KTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHekercd 197
Cdd:pfam05622 104 EELTSLAEEAQAlkdemDILRESSdKVKKLEATVEtykKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKK------ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 198 qlqaeqkgltevTQSLKMENEEFKKRFSDATSKaLQLEedivsvTHKAIEKETELDSLKDKLRKAQHEREQL--ECQLKT 275
Cdd:pfam05622 178 ------------ANALRGQLETYKRQVQELHGK-LSEE------SKKADKLEFEYKKLEEKLEALQKEKERLiiERDTLR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 276 EKDEkELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQL---CLAEKENLQRTFLLTTS------SK 346
Cdd:pfam05622 239 ETNE-ELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHenkMLRLGQEGSYRERLTELqqlledAN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 347 EDTFFLKEQLRKAEEQVQATRQEVVFLAKELS-------DAVNVR---DRTMADLHTARLENEKVKKQLADAVAELKLNA 416
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKALQeqgskaeDSSLLKqklEEHLEKLHEAQSELQKKKEQIEELEPKQDSNL 397
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2161896568 417 MKKdqdkTDTLEHELRREVEDLKlrlqMAADHYK---EKFKE 455
Cdd:pfam05622 398 AQK----IDELQEALRKKDEDMK----AMEERYKkyvEKAKS 431
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
157-322 |
1.63e-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: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 157 TMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEE 236
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 237 DIVSVT----HKAIEKE-----TELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQT-LKN 306
Cdd:COG1579 81 QLGNVRnnkeYEALQKEieslkRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAeLEE 160
|
170
....*....|....*.
gi 2161896568 307 LDGNKESVITHFKEEI 322
Cdd:COG1579 161 LEAEREELAAKIPPEL 176
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
779-806 |
1.73e-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: 39.35 E-value: 1.73e-04
10 20
....*....|....*....|....*...
gi 2161896568 779 KVCPMCSEQFPpDYDQQVFERHVQTHFD 806
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
150-302 |
1.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERC-DQLQAEQKGLTEVT--------QSLK--MENE 218
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSGGSVSyldvllgsESFSdfLDRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 219 EFKKRFSDATSKALqleEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLM 298
Cdd:COG3883 122 SALSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
....
gi 2161896568 299 SEVQ 302
Cdd:COG3883 199 AELE 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
152-281 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 152 LKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATS-- 229
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2161896568 230 --KALQ-----LEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKE 281
Cdd:COG1579 90 eyEALQkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-279 |
1.87e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQkgltevtqslkmenEEFKKRFSDATS 229
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK--------------EDKALEIKKQEW 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDE 279
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-620 |
1.99e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 352 LKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARL---ENEKVKKQLADAVAELK--LNAMKKDQDKTDT 426
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKeeLKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 427 LEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANNNnvftkkmgnqQKVNDASVNTDPATSASTVDVK 506
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELIEELESELEALLN 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 507 PSPSAAEtdfdivtkgQVCEMTKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKE-QVKIAENvkfeLAEVQD 585
Cdd:TIGR02168 881 ERASLEE---------ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlEVRIDNL----QERLSE 947
|
250 260 270
....*....|....*....|....*....|....*.
gi 2161896568 586 NYKLQLAEKDKEISGLTSHLENLSRE-KELKRSLEN 620
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKE 983
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
779-806 |
2.07e-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: 39.05 E-value: 2.07e-04
10 20
....*....|....*....|....*...
gi 2161896568 779 KVCPMCSEQFPPDYDQQVFERHVQTHFD 806
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-623 |
2.83e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 145 TKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQaeqkgltevtqSLKMENEEFKKRF 224
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAD-----------EVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 225 SDatskalqLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQL-----KTEKDEKELYKVHLKNTEIENTK--L 297
Cdd:PRK02224 254 ET-------LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERddllaEAGLDDADAEAVEARREELEDRDeeL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 298 MSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFlltTSSKEDTfflKEQLRKAEEQVQATRQEVVFLAKEL 377
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL---ESELEEA---REAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 378 SDAVNVRDRTMADLHTARLENEKVKKQLADAVAELK------------LNAMK--------KDQDKTDTLEH------EL 431
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRtarerveeaealLEAGKcpecgqpvEGSPHVETIEEdrerveEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 432 RREVEDLKLRlQMAADHYKEKFKECQRLQKQINKLSDQSANNNNVFTKKmgnqqkvnDASVNTDPATSASTVDVKPS-PS 510
Cdd:PRK02224 481 EAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAER--------RETIEEKRERAEELRERAAElEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 511 AAETDFDIVTKGQvcEMTKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKfELAEVQDNYKLQ 590
Cdd:PRK02224 552 EAEEKREAAAEAE--EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE-ALAELNDERRER 628
|
490 500 510
....*....|....*....|....*....|...
gi 2161896568 591 LAEKDKEISGLTSHLENlSREKELKRSLENQAE 623
Cdd:PRK02224 629 LAEKRERKRELEAEFDE-ARIEEAREDKERAEE 660
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
247-411 |
3.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 247 EKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLdgnkesvITHFKEEIGR-- 324
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 325 ----LQLCLAEKENLQRtflLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEK 400
Cdd:COG1579 87 nnkeYEALQKEIESLKR---RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|.
gi 2161896568 401 VKKQLADAVAE 411
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-467 |
3.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 146 KAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQA------EQKG--------LTE--- 208
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkKAKGkcpvcgreLTEehr 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 209 --VTQSLKMENEEFKKRFSDATSKALQLEEDIVSVtHKAIEKETELDSLK---DKLRKAQHEREQLECQlKTEKDEKELY 283
Cdd:PRK03918 451 keLLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKelaEQLKELEEKLKKYNLE-ELEKKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 284 KVHLKNTEIEN--TKLMSEVQTLKNLDGNKESVithfKEEIGRLQLCLAE--KENLQRTFlltTSSKEDTFFLKE----- 354
Cdd:PRK03918 529 KLKEKLIKLKGeiKSLKKELEKLEELKKKLAEL----EKKLDELEEELAEllKELEELGF---ESVEELEERLKElepfy 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 355 ----QLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLhtarlenEKVKKQLadavAELKLNAMKKDQDKTDTLEHE 430
Cdd:PRK03918 602 neylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL-------EELRKEL----EELEKKYSEEEYEELREEYLE 670
|
330 340 350
....*....|....*....|....*....|....*..
gi 2161896568 431 LRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLS 467
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-630 |
3.28e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 410 AELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQmAADHYKEKFKECQRLQKQINKLSDQSANNN--NVFTKKMGNQQKV 487
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREEleELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 488 NDASVNTDpATSASTVDVKPSPSAAETDFDIVTKGqVCEMTKEIADKT---EKYNKCKQLLQDEKAKCNKYADELAKMEL 564
Cdd:TIGR02168 256 EELTAELQ-ELEEKLEELRLEVSELEEEIEELQKE-LYALANEISRLEqqkQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2161896568 565 KWKEQVKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLENLSREKELKRSLENQAERKMEGQN 630
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
779-805 |
3.42e-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: 3.42e-04
10 20
....*....|....*....|....*..
gi 2161896568 779 KVCPMCSEQFPPDYDQQVFERHVQTHF 805
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
145-650 |
3.73e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 145 TKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVG--KMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKK 222
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYheRKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 223 R----FSDATSKALQLEEDIVSVTHKAIEKEteldslKDKLRKAQHEREQLECQLKTEKDEKELyKVHLKNTEIENTKLM 298
Cdd:TIGR00618 259 QqllkQLRARIEELRAQEAVLEETQERINRA------RKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 299 SEVQTLKNLDGNKESVITHFKEEIgrlqlcLAEKENLQRTFLLTTSSKEDTffLKEQLRKAEEQVQATRQEVVFLAKELS 378
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEI------HIRDAHEVATSIREISCQQHT--LTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 379 davnVRDRTMADLHTARLENEKVKKQLADAVAELKLnamkkDQDKTDTLEHELRREVEDLKLR---LQMAADHYKEKFKE 455
Cdd:TIGR00618 404 ----ILQREQATIDTRTSAFRDLQGQLAHAKKQQEL-----QQRYAELCAAAITCTAQCEKLEkihLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 456 CQRLQKQINKLSDQSANNNNVFTKKMGNQQKVNDASVNTDPATSASTVDVKPSPSAAETDFDIVTKGQVCEMTKEIADKT 535
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 536 EKYnkckqlLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDNYKLQLAEKDKEIsgltshLENLSREKELK 615
Cdd:TIGR00618 555 RKQ------RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA------CEQHALLRKLQ 622
|
490 500 510
....*....|....*....|....*....|....*
gi 2161896568 616 RSLENQAERKMEGQNFQSPQCLNTCSEQngYVLTL 650
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHA--LQLTL 655
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
180-471 |
4.40e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 180 EQVGKMERELNHEKERCDQL-QAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLkdk 258
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 259 lrkaQHEREQLECqlktekdekelykvhLKNTEIEntklmsevqtLKNLDGNKesVITHFKEEIGRLQLCLAEKENLQRT 338
Cdd:PRK05771 120 ----EQEIERLEP---------------WGNFDLD----------LSLLLGFK--YVSVFVGTVPEDKLEELKLESDVEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 339 FLLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRtmadLHTARLENEKVKKQLADAVAELKlNAMK 418
Cdd:PRK05771 169 VEYISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEGTPSEL----IREIKEELEEIEKERESLLEELK-ELAK 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2161896568 419 KDQDKTDTLEHELRREVEDLKLRLQMAADHY---------KEKFKecqRLQKQINKLSDQSA 471
Cdd:PRK05771 244 KYLEELLALYEYLEIELERAEALSKFLKTDKtfaiegwvpEDRVK---KLKELIDKATGGSA 302
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-466 |
4.44e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 197 DQLQAEQKGLTEVTQSLKMENEEFKKrFSDATSkalQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTE 276
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEK-FIKRTE---NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 277 KDEKELykvhLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFFLKEQL 356
Cdd:PRK03918 234 EELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 357 RKAEEQVQATRQEVVFLAKELSDAVNVRDRTMadlhtarlENEKVKKQLADAVAELK-----LNAMKKDQDKTDTLEHEL 431
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEerhelYEEAKAKKEELERLKKRL 381
|
250 260 270
....*....|....*....|....*....|....*.
gi 2161896568 432 R-REVEDLKLRLQMAADHYKEKFKECQRLQKQINKL 466
Cdd:PRK03918 382 TgLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
155-493 |
4.74e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 155 EKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEvtqslkmENEEFKKRFSDATSKALQL 234
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE-------ELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 235 EEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKelykvhlKNTEIENTKLMSEVQTLKNLDGNKESV 314
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER-------QDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 315 ITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTA 394
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 395 RLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYK-EKFKECQRLQKQINKLSDQSANN 473
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAlEEAALELKLLALLLNLAALSLIG 311
|
330 340
....*....|....*....|
gi 2161896568 474 NNVFTKKMGNQQKVNDASVN 493
Cdd:COG4372 312 ALEDALLAALLELAKKLELA 331
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-692 |
6.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 408 AVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANNNNVFTKKMGNQQKv 487
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 488 NDASVNTDPATSASTvdvkpSPSAAETDFDIVTKgqvceMTKEIADKTEKYNKCKQLLQDEKAKCnkyadelakmelkwK 567
Cdd:COG3883 98 SGGSVSYLDVLLGSE-----SFSDFLDRLSALSK-----IADADADLLEELKADKAELEAKKAEL--------------E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 568 EQVKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLENLSREKELKRSLENQAERKMEGQNFQSPQCLNTCSEQNGYV 647
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2161896568 648 LTLSNAQPVLQYGNPYASQETRDGADGAFYPDEIQRPPVRVPAWG 692
Cdd:COG3883 234 AAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-625 |
6.47e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 352 LKEQLRKAEEQVQATRQevvflAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHEL 431
Cdd:COG1196 198 LERQLEPLERQAEKAER-----YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 432 RREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLsdqsannnnvftkkmgnQQKVNDASVNTDpatsastvdvkpspsa 511
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARL-----------------EERRRELEERLE---------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 512 aetdfdivtkgqvcEMTKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDnykLQL 591
Cdd:COG1196 320 --------------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE---ELE 382
|
250 260 270
....*....|....*....|....*....|....
gi 2161896568 592 AEKDKEISGLTSHLENLSREKELKRSLENQAERK 625
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
188-626 |
7.29e-04 |
|
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: 43.14 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 188 ELNHEKE----RCDQLQAEQKGLTEVTQSLKMENEEFKKRFSdatskalQLE--EDIVSVTH-KAIEKETELDSLKDKLR 260
Cdd:pfam05622 4 EAQEEKDelaqRCHELDQQVSLLQEEKNSLQQENKKLQERLD-------QLEsgDDSGTPGGkKYLLLQKQLEQLQEENF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 261 KAQHEREQLecQLKTEKDEKELYKVHLKNTEIenTKLMSEVQTLKN-LD---------GNKESVITHFK---EEIGRL-- 325
Cdd:pfam05622 77 RLETARDDY--RIKCEELEKEVLELQHRNEEL--TSLAEEAQALKDeMDilressdkvKKLEATVETYKkklEDLGDLrr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 326 QLCLAEKEN---LQRTFLLTTSSKEdTFFLKEQLRKAEEQVQATRQEV----------VFLAKELSDAVNV----RDRTM 388
Cdd:pfam05622 153 QVKLLEERNaeyMQRTLQLEEELKK-ANALRGQLETYKRQVQELHGKLseeskkadklEFEYKKLEEKLEAlqkeKERLI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 389 ADLHTARLENEKVK-KQLADAVAELKLNAMKKDQDKTDTLEHEL----------RREVEDLKLRLQMAADhYKEKFKECQ 457
Cdd:pfam05622 232 IERDTLRETNEELRcAQLQQAELSQADALLSPSSDPGDNLAAEImpaeirekliRLQHENKMLRLGQEGS-YRERLTELQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 458 RLqkqinkLSDQSANNNNVFTKKMGNQQKVNDASVNT-DPATSASTVDVKP-SPSAAETDFDIVTKgQVCEMTKEIADKT 535
Cdd:pfam05622 311 QL------LEDANRRKNELETQNRLANQRILELQQQVeELQKALQEQGSKAeDSSLLKQKLEEHLE-KLHEAQSELQKKK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 536 EKYNKCKQLLQDEK--------AKCNKYADELAKMELKWKEQVKIAENVKFELAEVQDNY--------KLQLAEKDKEIs 599
Cdd:pfam05622 384 EQIEELEPKQDSNLaqkidelqEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPAsppeiqalKNQLLEKDKKI- 462
|
490 500
....*....|....*....|....*..
gi 2161896568 600 gltshlENLSREKELKRSLENQAERKM 626
Cdd:pfam05622 463 ------EHLERDFEKSKLQREQEEKLI 483
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
127-627 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 127 EELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQL------- 199
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahakkqq 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 200 QAEQKGL-------TEVTQSLKMENEEFKKRFSdATSKALQLEEDIVSVTHKAIEKETELDSLKDKLrkaqherEQLECQ 272
Cdd:TIGR00618 434 ELQQRYAelcaaaiTCTAQCEKLEKIHLQESAQ-SLKEREQQLQTKEQIHLQETRKKAVVLARLLEL-------QEEPCP 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 273 LKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFFL 352
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 353 KEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTM---ADLHTARLENEKVKKQLAD---------------------- 407
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLqpeQDLQDVRLHLQQCSQELALkltalhalqltltqervrehal 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 408 AVAELKLNAMKKDQDKTDTLEHELRR------EVEDLKLRLQMAADHYKEKFKE----CQRLQKQINKLSDQSANNNNVF 477
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQltywkeMLAQCQTLLRELETHIEEYDREfneiENASSSLGSDLAAREDALNQSL 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 478 TKKMGNQQKVNDASVNTDP-ATSASTVDVKPSPSAAETDFDIVTKG-QVCEMTKEIADKTEKY-NKCKQLLQDEKAKCNK 554
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFnNNEEVTAALQTGAELSHLAAEIQFFNrLREEDTHLLKTLEAEIgQEIPSDEDILNLQCET 825
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2161896568 555 YADELAKMELKWKEQVKIAENVKFELAEVQDNYKlQLAEKDKEISGLTSHLENLSREKELKRSLENQAERKME 627
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK-QLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-469 |
1.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 153 KIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQK--GLTEVTQSLKMENEEFKKRFSDATSK 230
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 231 AL---QLEEDIVSVTHKAIEKETELDSLKDKLRKAQHER-EQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKN 306
Cdd:COG4717 155 LEelrELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 307 --------------------------LDGNKESVITHFKEEIGRLQLCLA----EKENLQRTFLLTTSSKEDTFFLKEQL 356
Cdd:COG4717 235 eleaaaleerlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 357 RKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDtlEHELRREVe 436
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED--EEELRAAL- 391
|
330 340 350
....*....|....*....|....*....|...
gi 2161896568 437 dlklrlqmaadhykEKFKECQRLQKQINKLSDQ 469
Cdd:COG4717 392 --------------EQAEEYQELKEELEELEEQ 410
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
131-261 |
1.10e-03 |
|
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: 40.38 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 131 TMEDEGNSDMLVVTTKAGLLeLKIEKTMKEKEELLKLIAVLE-------KETAQLREQVGKMERELNHEKERCDQLQAEQ 203
Cdd:pfam11559 25 TAEGVEENIARIINVIYELL-QQRDRDLEFRESLNETIRTLEaeierlqSKIERLKTQLEDLERELALLQAKERQLEKKL 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2161896568 204 KGLtevTQSLKMENEEFKKRFSDATSKALQLeedivsvTHKAIEKETELDSLKDKLRK 261
Cdd:pfam11559 104 KTL---EQKLKNEKEELQRLKNALQQIKTQF-------AHEVKKRDREIEKLKERLAQ 151
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
135-369 |
1.18e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 135 EGNSDMLVVTTKAGLLELKieKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQA-------EQKGLT 207
Cdd:pfam15905 44 SKDASTPATARKVKSLELK--KKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAklnaavrEKTSLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 208 EVTQSLKME-------NEEFKKRFS-DATSKALQ------------LEEDIVSVTHKAIEKETELDSLKDKLRKAQHERE 267
Cdd:pfam15905 122 ASVASLEKQlleltrvNELLKAKFSeDGTQKKMSslsmelmklrnkLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 268 QLECQLKTEKDEKELYKVHLKNTEIENTKLM------------------------SEVQTLKN-LDGNKESVITHFKEEI 322
Cdd:pfam15905 202 QLEEKLVSTEKEKIEEKSETEKLLEYITELScvseqvekykldiaqleellkeknDEIESLKQsLEEKEQELSKQIKDLN 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2161896568 323 GRLQLCLAEKENL---QRTFLLTTSSKEDTffLKEQLRKAEEQVQATRQE 369
Cdd:pfam15905 282 EKCKLLESEKEELlreYEEKEQTLNAELEE--LKEKLTLEEQEHQKLQQK 329
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
126-469 |
1.29e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 126 VEELLTMEDEGNSDMLvvttkAGLLELKI--EKTMKEKEELLKLIAVLEKE-----------TAQLREQVGKMERELNH- 191
Cdd:PRK04778 110 IESLLDLIEEDIEQIL-----EELQELLEseEKNREEVEQLKDLYRELRKSllanrfsfgpaLDELEKQLENLEEEFSQf 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 192 --EKERCDQLQAEqkgltEVTQSLKMENEEFKK------------------RFSDATSKALQLEEDIVSVTHKAIEKEte 251
Cdd:PRK04778 185 veLTESGDYVEAR-----EILDQLEEELAALEQimeeipellkelqtelpdQLQELKAGYRELVEEGYHLDHLDIEKE-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 252 LDSLKDKLRKAQHEREQLEC--------QLKTEKDEkeLYKVhlknteIENtklmsEVQTLKNLDGNKESVITHFKEEIG 323
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLdeaeekneEIQERIDQ--LYDI------LER-----EVKARKYVEKNSDTLPDFLEHAKE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 324 RLQLCLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKK 403
Cdd:PRK04778 325 QNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSE 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2161896568 404 QLA-----DAVAELKLNAMKKDQdktdtleHELRREVEdlKLRLQMAADHYKEKFKEcqrLQKQINKLSDQ 469
Cdd:PRK04778 405 MLQglrkdELEAREKLERYRNKL-------HEIKRYLE--KSNLPGLPEDYLEMFFE---VSDEIEALAEE 463
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
752-777 |
1.36e-03 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 36.76 E-value: 1.36e-03
10 20
....*....|....*....|....*.
gi 2161896568 752 KKCPLCELMFPPNYDQSKFEEHVESH 777
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
151-260 |
1.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 151 ELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQ----LQAEQKGLTEVTQSLKMENEEFKKR--- 223
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRklelLEKREEELEKKEKELEQKQQELEKKeee 132
|
90 100 110
....*....|....*....|....*....|....*..
gi 2161896568 224 FSDATSKALQLEEDIVSVTHKAIeKETELDSLKDKLR 260
Cdd:PRK12704 133 LEELIEEQLQELERISGLTAEEA-KEILLEKVEEEAR 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-414 |
1.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 197 DQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTE 276
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 277 KDEKELYKV--HLKNTEIENTKLMSEVQTLKNLDGNKESVithfKEEIGRLQlclAEKENLQRTFLLTTsskedtfflKE 354
Cdd:COG4717 129 PLYQELEALeaELAELPERLEELEERLEELRELEEELEEL----EAELAELQ---EELEELLEQLSLAT---------EE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 355 QLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLhtARLENEKVKKQLADAVAELKL 414
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL--EQLENELEAAALEERLKEARL 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
394-635 |
1.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 394 ARLENEKVKKQLADAvaELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANN 473
Cdd:COG4942 25 AEAELEQLQQEIAEL--EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 474 NNVFTKKMGNQQKVNDASvNTDPATSAStvdvkpSPSAAETDFDIVTkgqvcEMTKEIADKTEKYNKCKQLLQDEKAKCN 553
Cdd:COG4942 103 KEELAELLRALYRLGRQP-PLALLLSPE------DFLDAVRRLQYLK-----YLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 554 KYADELAKMELKWKEQVKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLENLSREKELKRSLENQAERKMEGQNFQS 633
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 2161896568 634 PQ 635
Cdd:COG4942 251 LK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-437 |
1.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 222 KRFSDATSKALQLEEDIVSVTHKAIEK-----ETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKvhlknteientk 296
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELE------------ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 297 lmsevQTLKNLDGNKesvITHFKEEIGRLQLCLAEKENLQRTFllttsskedtfflKEQLRKAEEQVQATRQEVVFLAKE 376
Cdd:COG4913 330 -----AQIRGNGGDR---LEQLEREIERLERELEERERRRARL-------------EALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2161896568 377 LSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELK--LNAMKKDQDKTDTLEHELRREVED 437
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeIASLERRKSNIPARLLALRDALAE 451
|
|
| S6OS1 |
pfam15676 |
Six6 opposite strand transcript 1 family; This family of proteins is found in eukaryotes. ... |
162-237 |
1.82e-03 |
|
Six6 opposite strand transcript 1 family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 114 and 587 amino acids in length. The function is not known.
Pssm-ID: 464795 Cd Length: 557 Bit Score: 41.75 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2161896568 162 EELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLqAEQKGLTEVTQSLKMENE---EFKKRFSDATSKALQLEED 237
Cdd:pfam15676 163 EDILKLANTFTQKSSELKKEADEMEMKINYLNKQFERL-SEDKNLSEMLEEKNKSLEkrkEFKERIFEEDEHPLVLEEY 240
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
114-296 |
1.85e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 114 ASTPFQFRASSPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELlkliavlEKETAQLREQVGKMERELNHEK 193
Cdd:pfam15905 146 SEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHS-------KGKVAQLEEKLVSTEKEKIEEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 194 ERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLEcql 273
Cdd:pfam15905 219 SETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELL--- 295
|
170 180
....*....|....*....|...
gi 2161896568 274 kTEKDEKElykvHLKNTEIENTK 296
Cdd:pfam15905 296 -REYEEKE----QTLNAELEELK 313
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-624 |
2.09e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 156 KTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKE-------RCDQLQAEQKGLTE-VTQSLKMENE--EFKKRFS 225
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREivksyenELDPLKNRLKEIEHnLSKIMKLDNEikALKSRKK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 226 DATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKaQHEREQLECQLKTEKDEKELYKVHLKNTEIENtklmsevqtlk 305
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKERRLLNQEKTELLV----------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 306 nldgnkesvithfkeEIGRLQLclaeKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQ---EVVFLAKELSDAVN 382
Cdd:TIGR00606 348 ---------------EQGRLQL----QADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQiknFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 383 VRDRTMADLHtarlENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHElRREVEDLKLRLQMAADHYKEKFKECQRLQKQ 462
Cdd:TIGR00606 409 TAAQLCADLQ----SKERLKQEQADEIRDEKKGLGRTIELKKEILEKK-QEELKFVIKELQQLEGSSDRILELDQELRKA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 463 INKLSdQSANNNNVFTKKMGNQQKVNDasvNTDPATSASTVDVKpspsAAETDFDIVTKGQVCEMTKEIADKTEKYNKCK 542
Cdd:TIGR00606 484 ERELS-KAEKNSLTETLKKEVKSLQNE---KADLDRKLRKLDQE----MEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 543 QLLQDEKAKCNKY---ADELAKMELKWKEQVKIAEN----VKFELAEVQDN---YKLQLAEKDKEISGLTSHLENLSREK 612
Cdd:TIGR00606 556 SRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDrlakLNKELASLEQNknhINNELESKEEQLSSYEDKLFDVCGSQ 635
|
490
....*....|..
gi 2161896568 613 ELKRSLENQAER 624
Cdd:TIGR00606 636 DEESDLERLKEE 647
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
150-627 |
2.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 150 LELKIEKTMKEKEELLKLIAVLEKETAQLrEQVGKMERELNheKERCDQLQAEQKGLTEvtqSLKMENEEFKKRFSDATS 229
Cdd:TIGR00606 442 IELKKEILEKKQEELKFVIKELQQLEGSS-DRILELDQELR--KAERELSKAEKNSLTE---TLKKEVKSLQNEKADLDR 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 230 KALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHERE--------------------QLECQLKTEKDEKELYKVHLKN 289
Cdd:TIGR00606 516 KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeltsllgyfpnkkQLEDWLHSKSKEINQTRDRLAK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 290 TEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRtfllttsskedtffLKEQLRKAEEQVQAtrqe 369
Cdd:TIGR00606 596 LNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLER--------------LKEEIEKSSKQRAM---- 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 370 vvflakeLSDAVNVRDRTMADLHTarlENE----------KVKKQLADAVAEL--KLNAMKKDQDKTDTLEHELRREVED 437
Cdd:TIGR00606 658 -------LAGATAVYSQFITQLTD---ENQsccpvcqrvfQTEAELQEFISDLqsKLRLAPDKLKSTESELKKKEKRRDE 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 438 LKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANNNNVFTKKMGNQQKVN-----------DASVNTDPATSASTVDVK 506
Cdd:TIGR00606 728 MLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpeeesakvcltDVTIMERFQMELKDVERK 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 507 PSPSAAETDfDIVTKGQVCEMTKEIADKTEKYNKCKQ-------LLQDE-------KAKCNKYADELAKMELKWKEQVKI 572
Cdd:TIGR00606 808 IAQQAAKLQ-GSDLDRTVQQVNQEKQEKQHELDTVVSkielnrkLIQDQqeqiqhlKSKTNELKSEKLQIGTNLQRRQQF 886
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2161896568 573 AENVKFELAEVQDNYKlQLAEKDKEISGLTSHLENLSREKELKRSLENQAERKME 627
Cdd:TIGR00606 887 EEQLVELSTEVQSLIR-EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
752-778 |
2.51e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 35.94 E-value: 2.51e-03
10 20
....*....|....*....|....*..
gi 2161896568 752 KKCPLCELMFPPNYDQSKFEEHVESHW 778
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
211-297 |
2.83e-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: 38.82 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 211 QSLKMENEEfkkrfsdATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNT 290
Cdd:pfam12718 3 NSLKLEAEN-------AQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNN 75
|
....*..
gi 2161896568 291 EIENTKL 297
Cdd:pfam12718 76 ENLTRKI 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-297 |
3.39e-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: 41.21 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 146 KAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFS 225
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 226 D---------ATSKALQLEEDIVSVTHKAIEKetELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTK 296
Cdd:TIGR02169 858 NlngkkeeleEELEELEAALRDLESRLGDLKK--ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
.
gi 2161896568 297 L 297
Cdd:TIGR02169 936 I 936
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
130-405 |
4.76e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 130 LTMEDEGNSDMLVVTTKAG-----------LLELKIEKTMKEK-EELLKLIAVLEKETAQLREQVGKMERELnhekercd 197
Cdd:COG3206 127 LTVEPVKGSNVIEISYTSPdpelaaavanaLAEAYLEQNLELRrEEARKALEFLEEQLPELRKELEEAEAAL-------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 198 qlqaeqkgltevtqslkmenEEFKKR--FSDATSKALQLEEDIVSVthkaiekETELDSLKDKLRKAQHEREQLECQLKT 275
Cdd:COG3206 199 --------------------EEFRQKngLVDLSEEAKLLLQQLSEL-------ESQLAEARAELAEAEARLAALRAQLGS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 276 EKDEkelykvhlKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRtfLLTTSSKEDTFFLKEQ 355
Cdd:COG3206 252 GPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--QLQQEAQRILASLEAE 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2161896568 356 LRKAEEQVQATRQEVvflaKELSDAVNVRDRTMADLhtARLENE-KVKKQL 405
Cdd:COG3206 322 LEALQAREASLQAQL----AQLEARLAELPELEAEL--RRLEREvEVAREL 366
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
149-217 |
5.12e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 5.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2161896568 149 LLELK--IEKTMKEKEELLKLIAVLEKETAQLREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMEN 217
Cdd:COG4026 137 LLELKekIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKR 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-454 |
5.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 247 EKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVHLK--NTEIENTKLMSEVQTLKN-----LDGNKEsvITHFK 319
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEysWDEIDVASAEREIAELEAelerlDASSDD--LAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 320 EEIGRLQlclAEKENLQRTfllttsskedtfflKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLEnE 399
Cdd:COG4913 692 EQLEELE---AELEELEEE--------------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-E 753
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2161896568 400 KVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLklrlqMAAdhYKEKFK 454
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELERA-----MRA--FNREWP 801
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
244-639 |
5.80e-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: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 244 KAIEK-----ETELDSLKDKLRKAQHEREQLECQLKTEK--DEKELYKVHLKNTEIENTKLMSEVQT---LKNLDGNKES 313
Cdd:TIGR01612 1372 KEIEEnnkniKDELDKSEKLIKKIKDDINLEECKSKIEStlDDKDIDECIKKIKELKNHILSEESNIdtyFKNADENNEN 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 314 VITHFKEeigrlqlclaekenlqrtflLTTSSKEDTFFLKEQLRKAEEQVQATRQEVvflaKELSDAVNvRDRTMADLHT 393
Cdd:TIGR01612 1452 VLLLFKN--------------------IEMADNKSQHILKIKKDNATNDHDFNINEL----KEHIDKSK-GCKDEADKNA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 394 ARLE-NEKVKKQLADAVAELkLN-----AMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQInklS 467
Cdd:TIGR01612 1507 KAIEkNKELFEQYKKDVTEL-LNkysalAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRI---E 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 468 DQSANNNnvftkkmgnqqKVNDASvntdpatsastVDVKPSPSAAETDF----DIVTKGQVCemTKEIADKTEKYNKCKQ 543
Cdd:TIGR01612 1583 DDAAKND-----------KSNKAA-----------IDIQLSLENFENKFlkisDIKKKINDC--LKETESIEKKISSFSI 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 544 LLQDEKAKCN-KYADELAKMELKWKEQVKIAENVKFELAEV--------------QDNYKLQLAEKDKEISgltshLENL 608
Cdd:TIGR01612 1639 DSQDTELKENgDNLNSLQEFLESLKDQKKNIEDKKKELDELdseiekieidvdqhKKNYEIGIIEKIKEIA-----IANK 1713
|
410 420 430
....*....|....*....|....*....|.
gi 2161896568 609 SREKELKRSLENQAERKMEGQNFQSPQCLNT 639
Cdd:TIGR01612 1714 EEIESIKELIEPTIENLISSFNTNDLEGIDP 1744
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
131-669 |
5.96e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 131 TMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGKME-RELNHEKERCDQLQAEQKGLTEV 209
Cdd:COG5022 835 TEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDvKSISSLKLVNLELESEIIELKKS 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 210 TQSLKMENEEFKKRFSdATSKALQLEEDIVSVTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKDEKElyKVHLKN 289
Cdd:COG5022 915 LSSDLIENLEFKTELI-ARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVR--EGNKAN 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 290 TEIENTKlmsevQTLKNLDGNKESVITHfKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTFFLKEQLRKAEEQVQATRQE 369
Cdd:COG5022 992 SELKNFK-----KELAELSKQYGALQES-TKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQAR 1065
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 370 V--VFLAKELSD-----------------AVNVRDRTMADLHTARLENEKVK----------KQLADAVAELKLNAMKKD 420
Cdd:COG5022 1066 YkaLKLRRENSLlddkqlyqlestenllkTINVKDLEVTNRNLVKPANVLQFivaqmiklnlLQEISKFLSQLVNTLEPV 1145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 421 QDKTDTLEHELR---------------REVEDLKLRLqMAADHYKEKFKECQRLQK----QINKLSDQSANNNNVFTKKM 481
Cdd:COG5022 1146 FQKLSVLQLELDglfweanlealpsppPFAALSEKRL-YQSALYDEKSKLSSSEVNdlknELIALFSKIFSGWPRGDKLK 1224
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 482 GNQQKVNDASVNTDPATSASTVDVKPSPSAAETDFDIVTK----GQVCEMTKEIADKTEKynKCKQLLQDEK-------- 549
Cdd:COG5022 1225 KLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLlnsiDNLLSSYKLEEEVLPA--TINSLLQYINvglfnalr 1302
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 550 AKCNKYADELAK-------MELKWKEQ----------------VKIAENVKFELAEVQDNYKLQLAEKDKEISGLTSHLE 606
Cdd:COG5022 1303 TKASSLRWKSATevnynseELDDWCREfeisdvdeeleeliqaVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYD 1382
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2161896568 607 NLSREKElkrsLENQAERKMEGQNFQSPQCLNTCSEQNGYVL---TLSNAQPVLQYGNPYASQETR 669
Cdd:COG5022 1383 PADKENN----LPKEILKKIEALLIKQELQLSLEGKDETEVHlseIFSEEKSLISLDRNSIYKEEV 1444
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
216-627 |
9.23e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 216 ENEEFKKRFSDATS-----KALQLEEDIVSVTHKAI-EKETELDSLKDKLRKAQHEREQLECQLKTEKDEKELYKVhlKN 289
Cdd:TIGR00606 167 EGKALKQKFDEIFSatryiKALETLRQVRQTQGQKVqEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKS--YE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 290 TEIENTKlmsevQTLKNLDGNKESvITHFKEEIGRLQLCLAEKENLQRTflLTTSSKEDTFFLKEQLRKAEEQVQATRQE 369
Cdd:TIGR00606 245 NELDPLK-----NRLKEIEHNLSK-IMKLDNEIKALKSRKKQMEKDNSE--LELKMEKVFQGTDEQLNDLYHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 370 vvflakelsdavnvRDRTMADLHTARLENEKVKKQLADAVAELkLNAMKKDQDKTDTL-EHELRREVEDLKLRLQMAADh 448
Cdd:TIGR00606 317 --------------KERELVDCQRELEKLNKERRLLNQEKTEL-LVEQGRLQLQADRHqEHIRARDSLIQSLATRLELD- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 449 ykeKFKECQRLQKQINklsdqsannNNVFTKKMGNQQKVNDASVNTDPATSASTVDVKpspSAAETDFDIVTKGQVCEMT 528
Cdd:TIGR00606 381 ---GFERGPFSERQIK---------NFHTLVIERQEDEAKTAAQLCADLQSKERLKQE---QADEIRDEKKGLGRTIELK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 529 KEIADK--TEKYNKCKQLLQDEKAKCN--KYADELAKMElkwKEQVKIAENVKFELAEVQDNY-KLQLAEKDKEISGLTS 603
Cdd:TIGR00606 446 KEILEKkqEELKFVIKELQQLEGSSDRilELDQELRKAE---RELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQ 522
|
410 420
....*....|....*....|....
gi 2161896568 604 HLENLSREKELKRSLENQAERKME 627
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKMD 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-469 |
9.89e-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: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 352 LKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRD--RTMADLHTARLENEKVKKQLADAVAELKlnAMKKDQDKtdtLEh 429
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELE--RLDASSDD---LA- 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2161896568 430 ELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQ 469
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
171-630 |
9.95e-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: 39.39 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 171 LEKETAQ---LREQVGKMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKALQLEE-------DIVS 240
Cdd:pfam01576 477 LQEETRQklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgkkrlqrELEA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 241 VTHKAIEKETELDSLKDKLRKAQHEREQLECQLKTEKD-----EKELYK----------VHLKNTEIEN----------T 295
Cdd:pfam01576 557 LTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsnlEKKQKKfdqmlaeekaISARYAEERDraeaearekeT 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 296 KLMSEVQTLKNLDGNKESVithfkEEIGRLQLclAEKENLqrtflltTSSKEDT----FFLKEQLRKAEEQVQATRQEVV 371
Cdd:pfam01576 637 RALSLARALEEALEAKEEL-----ERTNKQLR--AEMEDL-------VSSKDDVgknvHELERSKRALEQQVEEMKTQLE 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 372 FLAKELSDAVNVRDR---TMA--------DLHTARLENEKVKKQLADAVAELK--LNAMKKDQDKTDTLEHELRREVEDL 438
Cdd:pfam01576 703 ELEDELQATEDAKLRlevNMQalkaqferDLQARDEQGEEKRRQLVKQVRELEaeLEDERKQRAQAVAAKKKLELDLKEL 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 439 KLRLQMAADHYKEKFKECQRLQKQ----INKLSDQSANNNNVFTKKMGNQQKVNdasvntdpATSASTVDVKPSPSAAET 514
Cdd:pfam01576 783 EAQIDAANKGREEAVKQLKKLQAQmkdlQRELEEARASRDEILAQSKESEKKLK--------NLEAELLQLQEDLAASER 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161896568 515 dfdivTKGQVCEMTKEIADKTEKYNKCKQLLQDEKakcNKYADELAKMELkwkeqvkiaenvkfELAEVQDNYKLqLAEK 594
Cdd:pfam01576 855 -----ARRQAQQERDELADEIASGASGKSALQDEK---RRLEARIAQLEE--------------ELEEEQSNTEL-LNDR 911
|
490 500 510
....*....|....*....|....*....|....*..
gi 2161896568 595 DKEISGLTSHLEN-LSREKELKRSLENqAERKMEGQN 630
Cdd:pfam01576 912 LRKSTLQVEQLTTeLAAERSTSQKSES-ARQQLERQN 947
|
|
| |
