|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
186-719 |
0e+00 |
|
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: 655.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 186 ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTVVAKKYFHAQLQLEQLQEENFRLE 265
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQE 345
Cdd:pfam05622 80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 346 TNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKE 425
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 426 TNEELRCSQVQQDHLNQTDASATKSY---ENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRK 502
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSdpgDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 503 MNELETEQRLSKERIRELQQQIEDLQKSLQEQgsKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNV 582
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQ--GSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 583 -QKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPAS-AEIMLLRKQLAEKERRIEILESECKVAKF-RD 659
Cdd:pfam05622 398 aQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASpPEIQALKNQLLEKDKKIEHLERDFEKSKLqRE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 660 YEEKLIVSAWYNKSLAFQKLGMESRLVSGGGacsdtgactPARSFLAQQRHITNTRRNLS 719
Cdd:pfam05622 478 QEEKLIVTAWYNMGMALHRKAIEERLAGLSS---------PGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
15-163 |
1.19e-97 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 297.92 E-value: 1.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22225 2 CDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41688595 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225 82 QQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
15-163 |
7.07e-89 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 275.06 E-value: 7.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:pfam19047 3 CDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41688595 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:pfam19047 83 QQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
15-161 |
1.71e-84 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 263.34 E-value: 1.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
15-162 |
3.09e-71 |
|
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411798 Cd Length: 150 Bit Score: 228.99 E-value: 3.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22227 3 CDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688595 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22227 83 HQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
15-162 |
9.92e-71 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 227.54 E-value: 9.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22226 6 CESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688595 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22226 86 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
16-161 |
8.42e-48 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 165.53 E-value: 8.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 16 DSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSriKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQ 95
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41688595 96 QISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
17-159 |
4.23e-22 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 93.04 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 17 SLMIWLQTFNTASPCQ-DVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVgdNWRIKasNVKKVLQGIMSYYHEFLGQ 95
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 96 QISEALiPDLNQIteCSDP------VELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22223 81 LIVMKL-PDILTI--GREPeseqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-655 |
3.98e-13 |
|
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: 73.18 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 290 DELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnMMYMHNTVSLEEELKKANAART 369
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA--LLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 370 QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRD-TLKETNEELrcsQVQQDHLNQTDASAT 448
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGEL---EAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 449 KSYENLAAEIMPVEyrevfirlqhenkmlrlQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:TIGR02169 315 RELEDAEERLAKLE-----------------AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 529 KSLQE--QGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERy 606
Cdd:TIGR02169 378 KEFAEtrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK- 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 41688595 607 kmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVA 655
Cdd:TIGR02169 457 ---LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-618 |
1.66e-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: 71.24 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 271 YRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEIYRQK-----LQDLNDLRKQVKTLQE 345
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNE---LERQLKSLERQAEKAERYKELKAELRELelallVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 346 TNMMYMHNTVSLEEELKKANAartQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALlkeKERLIEQRDTLKE 425
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 426 TNEELRCSQVQQDHLNQTDASATKSYENLAAEIMpveyrevfiRLQHENKMLRLQQEGSENeRIEELQEQLEQKHRKMNE 505
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELE---------SLEAELEELEAELEELES-RLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 506 LETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKI 585
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 41688595 586 NELEAALQKKDED----------MKAMEERYKMYLEKARNVIK 618
Cdd:TIGR02168 471 EEAEQALDAAERElaqlqarldsLERLQENLEGFSEGVKALLK 513
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
18-159 |
2.96e-12 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 64.95 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 18 LMIWLQTFNTASPCQDVK-----QLTSGVAMAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEF 92
Cdd:cd22228 6 LVTWVKTFGPLGFGSEDKlsmymDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41688595 93 LGQQISEALiPDLNQITEcsDPV------ELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22228 82 LQQLIVMNL-PNVLMIGK--DPLsgksmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-651 |
3.88e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 317 NKLESTveiyRQKLQDLNDLRKQVKTlqetnmmymhNTVSLEEELKKANAARTqletYKRQVQDLHVKLSSesKRADTLA 396
Cdd:COG1196 179 RKLEAT----EENLERLEDILGELER----------QLEPLERQAEKAERYRE----LKEELKELEAELLL--LKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 397 FEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKM 476
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 477 LRLQQEGSENERIEELQEQLEQkhrKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgSKSEGESSSKLKQKLEAHMEK 556
Cdd:COG1196 316 ERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 557 LTEVHEELQKKQELIEDLQpdinQNVQKINELEAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRK 636
Cdd:COG1196 392 LRAAAELAAQLEELEEAEE----ALLERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLE 463
|
330
....*....|....*
gi 41688595 637 QLAEKERRIEILESE 651
Cdd:COG1196 464 LLAELLEEAALLEAA 478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
171-651 |
1.17e-11 |
|
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: 68.61 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 171 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVT-------------TLQDEKNSLVSENEMMNE-KLDQLDGSF 236
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrekelSLEKEQNKRLWDRDTGNSiTIDHLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 237 DDPNTVVAkkyfhaqlqleqlqeenfRLEAAKDDYRVHCE-ELEKQLIEFQHRNDELTSLAEETRalkdeidvlratsdk 315
Cdd:pfam15921 422 DDRNMEVQ------------------RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTA--------------- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 316 anKLESTVEIYRQKLQDLNdlrkqvktlqetnmmymhntvsleeelkkanAARTQLETYKRQVQDLHVKLSSESKRADTL 395
Cdd:pfam15921 469 --QLESTKEMLRKVVEELT-------------------------------AKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 396 AFEMKRLEEKHEALLKEKERLieqrdtlKETNEELRCSQVQQDHLNQTDASATKSYEnlaaeimpveyrevFIRLQHENK 475
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHL-------KNEGDHLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENM 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 476 MLRLQQEGSENERIEELQEQLEQ----KHRKMNELETEQRLSKERIRELQQQIEDLQKSlqeqgsksegesssklKQKL- 550
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKeindRRLELQEFKILKDKKDAKIRELEARVSDLELE----------------KVKLv 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 551 EAHMEKLTEVHEELQKKQELIEDLQP---DINQNVQKINELEAALQKKDEDMKAMEERYKMYL-------EKARNVIKTL 620
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVKTsrnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLksaqselEQTRNTLKSM 718
|
490 500 510
....*....|....*....|....*....|.
gi 41688595 621 DPKLNPASAEIMLLRKQLAEKERRIEILESE 651
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-593 |
1.62e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 277 ELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTVEIYRQKLQDLNDlrkqvktlqetnmmymhntvS 356
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELEELEL--------------------E 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 357 LEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqvq 436
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 437 qdhlnQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQkhrKMNELETEQRLSKER 516
Cdd:COG1196 358 -----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 517 IRELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQ 593
Cdd:COG1196 430 LAELEEEEEEEEEALEEA-----AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-616 |
6.76e-11 |
|
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: 65.86 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 290 DELTSLAEETRALKDEIDVLRatsDKANKLESTVEIYRQKLQDLNdlrKQVKTLQEtnmmymhntvSLEEELKKANAART 369
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDAS---RKIGEIEK----------EIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 370 QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE---------KERLIEQRDTLKETNEELRCSQVQQDHL 440
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlsHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 441 NQTDASATKSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIREL 520
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 521 QQQIEDLQKSLQEQGSK--SEGESSSKLKQKLEAHMEKLTE--------------------VHEELQKKQELIEDLQP-- 576
Cdd:TIGR02169 895 EAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALEPvn 974
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 41688595 577 -----DINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNV 616
Cdd:TIGR02169 975 mlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
163-641 |
6.84e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 163 EILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDmqvttlqdeknSLVSENEMMNEKLDQLDGSFDDPNTV 242
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAD-----------EVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 243 VAKKyfhaqlqleqlqeenfrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLES 321
Cdd:PRK02224 267 IAET------------------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 322 TVEIYRQKLQDLND----LRKQVKTLQETNMMYMHNTVSLEEELKkanAARTQLETYKRQVQDLHVKLSSESKRADTLAF 397
Cdd:PRK02224 329 RLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 398 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELR--------------CSQVQQDHLNQTDASATKsyenlaaeimpvEY 463
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkCPECGQPVEGSPHVETIE------------ED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 464 REVFIRLQHENKMLRLQQEGSEN--ERIEELQEQLEQKHRKMNELET-EQRLS--KERIRELQQQIEDLQKSLQEqgsks 538
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE----- 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 539 egessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEA----------------ALQKKDEDMKAM 602
Cdd:PRK02224 549 -------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedeieRLREKREALAEL 621
|
490 500 510
....*....|....*....|....*....|....*....
gi 41688595 603 EERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEK 641
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
291-651 |
6.87e-11 |
|
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: 65.91 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 291 ELTSLAEETRALKDEIDVLRATSDkaNKLESTVEIYRQKLQDL-NDLRKQVKTLQETNMMYMHNTVSLEEELKK-ANAAR 368
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQ--NKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEIiQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 369 TQLETYKRQVQDLHVKLSSeskradtLAFEMKRLEEKHEALLKEKERlieqrdTLKETNEELRCSQVQQDHLNQTDASAT 448
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQ-------LRSELREAKRMYEDKIEELEK------QLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 449 KSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETeqrLSKERIRELQQQIEDLQ 528
Cdd:pfam15921 377 DQLQKLLADL---HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLKAMKSECQGQMERQM 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 529 KSLQEQGSKSEGESSskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKM 608
Cdd:pfam15921 451 AAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 41688595 609 YLEKARNvIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESE 651
Cdd:pfam15921 529 KLQELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-532 |
8.46e-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: 65.85 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvakkyfhAQLQL 254
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--------------VEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEI-YRQKLQDL 333
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 334 NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAA----RTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEAL 409
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 410 LKEKERLIEQRDTLKETNE--ELRCSQVQQDHLNQTDAsATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQE----G 483
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAqlELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 41688595 484 SENER-IEELQEQleqkhrkmneleteqrlsKERIRELQQQIEDLQKSLQ 532
Cdd:TIGR02168 986 PVNLAaIEEYEEL------------------KERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-651 |
1.44e-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: 65.08 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 403 EEKHEALLK---EKERLIEQRDTLKETNEelrcsqvQQDHLnQTDASATKSYENLAAEIMPVEYREVFIRL-QHENKMLR 478
Cdd:TIGR02168 172 ERRKETERKlerTRENLDRLEDILNELER-------QLKSL-ERQAEKAERYKELKAELRELELALLVLRLeELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 479 LQQEGSENER--------IEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGessskLKQKL 550
Cdd:TIGR02168 244 LQEELKEAEEeleeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN-----LERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 551 EAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMY---LEKARNVIKTLDPKLNPA 627
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASL 398
|
250 260
....*....|....*....|....
gi 41688595 628 SAEIMLLRKQLAEKERRIEILESE 651
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQE 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
331-640 |
1.66e-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: 64.69 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 331 QDLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALL 410
Cdd:TIGR02168 677 REIEELEEKIEELEE----------KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 411 -------KEKERLIEQRDTLKETNEELRCS-QVQQDHLNQTDASATKSYENLAAEI-MPVEYREVFIRLQHENKMLRLQQ 481
Cdd:TIGR02168 747 eriaqlsKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALReALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 482 EGSENE------RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSegesssklkQKLEAHME 555
Cdd:TIGR02168 827 ESLERRiaaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---------ALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 556 KL-TEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLL 634
Cdd:TIGR02168 898 ELsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*.
gi 41688595 635 RKQLAE 640
Cdd:TIGR02168 978 ENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-604 |
2.61e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV-LRATSDKANKLESTVEIYRQKLQDLNDLRKQV- 340
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSKELTELe 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 341 KTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQR 420
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 421 DTLKETNEELRCSQvqqdhlnqtdASATKSYENLAAEImpveyREVFIRLQHEnkmlrLQQEGSENERIEELQEQLEQKH 500
Cdd:TIGR02168 841 EDLEEQIEELSEDI----------ESLAAEIEELEELI-----EELESELEAL-----LNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 501 RKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHE-ELQKKQELIEDLQPDIN 579
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG------------LEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEE 968
|
330 340
....*....|....*....|....*.
gi 41688595 580 QNVQKINELEAALQKKDE-DMKAMEE 604
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPvNLAAIEE 994
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-663 |
4.23e-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: 63.55 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 410 LKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMpveyrevfiRLQHENKMLrLQQEGSENERI 489
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---------EIEKEIEQL-EQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 490 EELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSsklkQKLEAHMEKLTEVH-------- 561
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI----PEIQAELSKLEEEVsriearlr 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 562 ---EELQKKQELIEDLQPDINQNVQKINELE---AALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLR 635
Cdd:TIGR02169 816 eieQKLNRLTLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260
....*....|....*....|....*...
gi 41688595 636 KQLAEKERRIEILESECKVAKFRDYEEK 663
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
18-159 |
4.30e-10 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 58.65 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 18 LMIWLQTF-----NTASPCQDVKQLTSGVAMAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEF 92
Cdd:cd22229 9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41688595 93 LGQQISEALiPDL-----NQITEcSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22229 85 LQQLIMMSL-PNVlvlgrNPLSE-QGTEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-651 |
9.81e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 172 AVGELEQQLKRALEELQEALAEKEElrqrcEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKkyfHAQ 251
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE---HEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 252 LQLEQLqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEIYRQKLQ 331
Cdd:PRK02224 249 RREELE-----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 332 D--------LNDLRKQVKTLQETNMMYMHNTVSLEEELKKA-----------NAARTQLETYKRQVQDLHVKLSSESKRA 392
Cdd:PRK02224 321 DrdeelrdrLEECRVAAQAHNEEAESLREDADDLEERAEELreeaaeleselEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 393 DTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELR--------------CSQVQQDHLNQTDASATKsyenlaaei 458
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkCPECGQPVEGSPHVETIE--------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 459 mpvEYREVFIRLQHENKMLRLQQEGSEN--ERIEELQEQLEQKHRKMNELET-EQRLS--KERIRELQQQIEDLQKSLQE 533
Cdd:PRK02224 472 ---EDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 534 qgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEaalqkKDEDMKAMEERYKMYLEKA 613
Cdd:PRK02224 549 ------------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-----RIRTLLAAIADAEDEIERL 611
|
490 500 510
....*....|....*....|....*....|....*...
gi 41688595 614 RNVIKTLDPKLNpasaeimLLRKQLAEKERRIEILESE 651
Cdd:PRK02224 612 REKREALAELND-------ERRERLAEKRERKRELEAE 642
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-650 |
1.09e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 414 ERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKsYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgseneRIEELQ 493
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 494 EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIED 573
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-----------LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 574 LQPDINQNVQKINELEAALQKKDEDMKAMEERykmylekarnviktLDPKLNPASAEIMLLRKQLAEKERRIEILES 650
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-664 |
1.86e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 174 GELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVvAKKYFHAQLQ 253
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 254 LEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKlqdL 333
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE---I 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 334 NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKR------QVQDLHVKLSSESKraDTLAFEMKRLEEKHE 407
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEakakkeELERLKKRLTGLTP--EKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 408 ALLKEKERLIEQRDTLKETNEELRCS----------------QVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ 471
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 472 HEN--KMLRLQQEGSENERIEELQEQLEQKHRKMN--ELE---TEQRLSKERIRELQQQIEDLQKSLQEqgsksegesSS 544
Cdd:PRK03918 482 LREleKVLKKESELIKLKELAEQLKELEEKLKKYNleELEkkaEEYEKLKEKLIKLKGEIKSLKKELEK---------LE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 545 KLKQKLEAHMEKLTEVHEELQK-KQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEErykmyLEKARNVIKTLDPK 623
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE-----LEREEKELKKLEEE 627
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41688595 624 LNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKL 664
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
2.20e-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: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfddPNTVVAKKYFHAQL 252
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------EGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 253 QLEQLQEENFRLEAAKDDYRVHCEELEKQLIEfqhRNDELTSLAEETRALKDE--IDVLRATSDKANKLESTVEIYRQKL 330
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 331 QDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLET----YKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 406
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 407 EALLKEKERLIEQRDTLKETNEELRcSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSEN 486
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 41688595 487 --ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQ 532
Cdd:TIGR02169 474 lkEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-650 |
2.31e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 133 KKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQ 212
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 213 DEKNSLVSENEMMNEKLDQLDGSFDDpntvvAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDEL 292
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 293 TSLAEETRALKDEIDVLRatsdkanKLESTVEIYRQKLQDLNDLRKQVKTLqetnmmymhNTVSLEEELKKANAARTQLE 372
Cdd:PRK03918 341 EELKKKLKELEKRLEELE-------ERHELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 373 TYKRQVQDLHVKLSSESKRADTLAFEMKR-----------LEEKHEALLKEK--ERLIEQRDTLKETNEELRCSQVQQDH 439
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 440 LNQTDASATK--SYENLAAEIMPVEYR-EVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKER 516
Cdd:PRK03918 485 LEKVLKKESEliKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 517 IRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHME--KLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQK 594
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688595 595 KDEDMKAMEERYKMylEKARNViktldpklnpaSAEIMLLRKQLAEKERRIEILES 650
Cdd:PRK03918 645 LRKELEELEKKYSE--EEYEEL-----------REEYLELSRELAGLRAELEELEK 687
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
480-665 |
4.24e-09 |
|
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: 59.01 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 480 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLK------------ 547
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplallls 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 548 -----------QKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNV 616
Cdd:COG4942 128 pedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 41688595 617 IKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKLI 665
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
263-662 |
6.07e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 263 RLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKT 342
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 343 LQETNMMyMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDT 422
Cdd:PTZ00121 1304 ADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 423 LKETNEELRCS----------QVQQDHLNQTDASATKSYE--NLAAEIMPVEyrEVFIRLQHENKMLRLQQEGSENERIE 490
Cdd:PTZ00121 1383 AKKKAEEKKKAdeakkkaeedKKKADELKKAAAAKKKADEakKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 491 ELQEQLEQKhRKMNELETEQRlSKERIRELQQQIEDLQKSLQE-QGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQE 569
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAE-EAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 570 LIEDLQPDINQNVQKINELEAALQ-KKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEil 648
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-- 1616
|
410
....*....|....
gi 41688595 649 ESECKVAKFRDYEE 662
Cdd:PTZ00121 1617 EAKIKAEELKKAEE 1630
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-649 |
7.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 176 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDpntvVAKKYFHAQLQLE 255
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----AEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 256 QLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELtsLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLND 335
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 336 LRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQD-----LHVKLSSESKRADTLAFEMKRLEEKHEALL 410
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 411 KEKERLIEQRDTLKETNEELRCSQVQQDH---------LNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQ 481
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 482 EGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVH 561
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 562 EELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKArnviktLDPKLNPASAEImlLRKQLAEK 641
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA------LEELPEPPDLEE--LERELERL 772
|
....*...
gi 41688595 642 ERRIEILE 649
Cdd:COG1196 773 EREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-662 |
1.35e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpntvvakkyfHAQLQL 254
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEIYRQKLQD 332
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 333 LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 413 KERLIEQRDTLKETNEELRCS-QVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENK---------MLRLQQE 482
Cdd:COG1196 472 AALLEAALAELLEELAEAAARlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeaaleaalAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 483 GSENERIEELQEQLEQKHRK-------MNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKL--------- 546
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvaar 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 547 KQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNP 626
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510
....*....|....*....|....*....|....*.
gi 41688595 627 ASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEE 662
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-529 |
2.18e-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: 57.76 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 170 NDAVGELEQQLKRAleELQEALAEK-EELRQRCEELDMQVTTLQdeknslvsenemMNEKLDQLDgsfddpntvvakkyf 248
Cdd:TIGR02168 192 EDILNELERQLKSL--ERQAEKAERyKELKAELRELELALLVLR------------LEELREELE--------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 249 haqlqleqlqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID-VLRATSDKANKLESTVEIYR 327
Cdd:TIGR02168 243 --------------ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 328 QKLQDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMK-RLEEKH 406
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEE----------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 407 EALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSE- 485
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELEr 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 41688595 486 -NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQK 529
Cdd:TIGR02168 459 lEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-656 |
2.22e-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: 57.76 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 174 GELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDpnTVVAKKYFHAQLQ 253
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 254 LEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDL 333
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 334 NDLRKQVKTLQETNMMYMH---NTVSLEEELKKA----------NAARTQLETYKRQVQDLhvkLSSESKRADTLA---F 397
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGvlsELISVDEGYEAAieaalggrlqAVVVENLNAAKKAIAFL---KQNELGRVTFLPldsI 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 398 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsQVQQDHLNQTdaSATKSYENLAAEIMPVEYREVFIRLQHE---- 473
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR--KALSYLLGGV--LVVDDLDNALELAKKLRPGYRIVTLDGDlvrp 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 474 ------------NKMLRLQQEGSENE-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgskseG 540
Cdd:TIGR02168 658 ggvitggsaktnSSILERRREIEELEeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-----R 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 541 ESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMY---LEKARNVI 617
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAEL 812
|
490 500 510
....*....|....*....|....*....|....*....
gi 41688595 618 KTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAK 656
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-664 |
2.70e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 262 FRLEAAKDDYRVHCEELEKQLIEFQHRNDELT------SLAEETRALKDEIDVLratSDKANKLESTVEIYRQKLQDLND 335
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAEL---PERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 336 LRKQVKTLQEtnmmymhntvSLEEELKK-ANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE 414
Cdd:COG4717 168 LEAELAELQE----------ELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 415 RLiEQRDTLKETNEELR--CSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEEL 492
Cdd:COG4717 238 AA-ALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 493 QEQLEQKHRKmnELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKL-TEVHEELQKKQELI 571
Cdd:COG4717 317 EEEELEELLA--ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 572 EDLQpdinQNVQKINELEAALQKKDEDMKAMEERYKmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESE 651
Cdd:COG4717 395 EEYQ----ELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410
....*....|...
gi 41688595 652 CKVAKFRDYEEKL 664
Cdd:COG4717 469 GELAELLQELEEL 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-621 |
2.79e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 132 EKKQEHIQNIMTLEESVQHVVMTAIQELMSKEILssppNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTL 211
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 212 QDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDE 291
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 292 LTSLAEETRALKDEIDVLRATS-DKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKAN----- 365
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrgla 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 366 -----------AARTQLETYK-RQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETN------ 427
Cdd:COG1196 524 gavavligveaAYEAALEAALaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdl 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 428 -------EELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHEN--KMLRLQQEGSENERIEELQEQLEQ 498
Cdd:COG1196 604 vasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSagGSLTGGSRRELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 499 KHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEvHEELQKKQELIEDLQPDI 578
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE-EELLEEEALEELPEPPDL 762
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 579 NQNVQKINELEAALQKK-------DEDMKAMEERYKMY------LEKARN----VIKTLD 621
Cdd:COG1196 763 EELERELERLEREIEALgpvnllaIEEYEELEERYDFLseqredLEEAREtleeAIEEID 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-525 |
2.94e-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: 57.37 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 179 QLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfhaqlqLEQLQ 258
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 259 EENFRLEAAKDDYrvhcEELEKQLIEFQHRNDEltsLAEETRALKDEIDVLRAtsdkanklestveiyrqklqDLNDLRK 338
Cdd:TIGR02168 306 ILRERLANLERQL----EELEAQLEELESKLDE---LAEELAELEEKLEELKE--------------------ELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 339 QVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIE 418
Cdd:TIGR02168 359 ELEELEAE----------LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 419 QRDTLketneELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQ 498
Cdd:TIGR02168 429 KLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340
....*....|....*....|....*..
gi 41688595 499 KHRKMNELETEQRLSKERIRELQQQIE 525
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-665 |
8.24e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 181 KRALEEL----QEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfDDPNTVVAKKYFHAQLQLEQ 256
Cdd:PTZ00121 1314 AKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 257 LQEENFRLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRAlKDEIDVLRATSDKANKLESTVEiYRQKLQDLNDL 336
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 337 RKQVKTLQETNmmymhntvSLEEELKKANAARTQLETYKRQVQDLHvKLSSESKRADTL--------AFEMKRLEEKHEA 408
Cdd:PTZ00121 1466 AEEAKKADEAK--------KKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAkkaeeakkADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 409 LLKEKERLIEQRDTLKETnEELRCSQ----VQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGS 484
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKA-EELKKAEekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 485 ENERI--EELQEQLEQKH-------------RKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQK 549
Cdd:PTZ00121 1616 EEAKIkaEELKKAEEEKKkveqlkkkeaeekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 550 LEAH----MEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKmyleKARNVIKTLDPKLN 625
Cdd:PTZ00121 1696 KEAEeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAE 1771
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 41688595 626 PASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKLI 665
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
177-665 |
1.34e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 177 EQQLKRA--LEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQL 254
Cdd:TIGR02169 347 EERKRRDklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLN 334
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 335 DLRKQVKTLQETNMMYMHNTVS------------LE----------------------EELKKANAAR-TQLETYKRQVQ 379
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAqlgsvgeryataIEvaagnrlnnvvveddavakeaiELLKRRKAGRaTFLPLNKMRDE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 380 DLHVKLSSESKRADtLAFEMKRLEEKHEALLKEKER---LIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAA 456
Cdd:TIGR02169 587 RRDLSILSEDGVIG-FAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 457 EIMPVEYREVFIRLQHENKML-----RLQQEGSENE-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKS 530
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLkrelsSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 531 LQEqgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQ---------------PDINQNVQKINE----LEAA 591
Cdd:TIGR02169 746 LSS------------LEQEIENVKSELKELEARIEELEEDLHKLEealndlearlshsriPEIQAELSKLEEevsrIEAR 813
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688595 592 LQKKDEDMKAMEERyKMYLEKARNVIKT----LDPKLNPASAEIMLLRKQLAEKERRIEILEseckvAKFRDYEEKLI 665
Cdd:TIGR02169 814 LREIEQKLNRLTLE-KEYLEKEIQELQEqridLKEQIKSIEKEIENLNGKKEELEEELEELE-----AALRDLESRLG 885
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
487-651 |
2.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 487 ERIEELQEQL---EQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 563
Cdd:COG4717 71 KELKELEEELkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 564 LQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERykmYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKER 643
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
....*...
gi 41688595 644 RIEILESE 651
Cdd:COG4717 228 ELEQLENE 235
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
36-159 |
2.48e-07 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 50.98 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 36 QLTSGVAMAQVLHQIDAawfNESWLSRIKEDVGDN-WRIKasNVKKVLQGIMSYYHEFLGQQISEALiPDL-----NQIT 109
Cdd:cd22230 46 RLSNGDLLNRVMGIIDP---SPRGGPRMRGDDGPAaHRVQ--NLHILWGRLRDFYQEELQQLILSPP-PDLqvmgrDPFT 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41688595 110 ECSdPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22230 120 EEA-VQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-430 |
3.63e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFH 249
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 250 AQLQLEQLQEENFRLEAAK----------DDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATsdkANKL 319
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALL---NERASLEEALALLRSELEELSEE---LREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 320 ESTVEIYRQKLQDLNDLRKQVKT-LQETNMMYMHNT--------VSLEEELKKANAARTQLETYKRQVQDLHVKLsSESK 390
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELrLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKI-KELG 985
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41688595 391 RADTLAF-EMKRLEEKHEALLKEKERLIEQRDTLKETNEEL 430
Cdd:TIGR02168 986 PVNLAAIeEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
178-620 |
4.99e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 178 QQLKRALEELQEALA----EKEELRQRCEELDMQVTTLQDEKNSLVSE-------NEMMNEKLDQLDGSFDDPNTVVAKK 246
Cdd:PRK02224 254 ETLEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEEC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 247 YFHAQLQLEQLQEENFR---LEAAKDDYRVHCEELEKqliEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTV 323
Cdd:PRK02224 334 RVAAQAHNEEAESLREDaddLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 324 EIYRQKLQ-DLNDLRKQVKTLqETNMMYMHNTVSLEEELKKA-------------------NAARTQLETYKRQVQDLHV 383
Cdd:PRK02224 411 EDFLEELReERDELREREAEL-EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 384 KLSSESKRADTL------AFEMKRLEEKHEALlkeKERLIEQRDTLKETNEELRCSQVQQDHLNqtDASATKSYENLAAE 457
Cdd:PRK02224 490 EVEEVEERLERAedlveaEDRIERLEERREDL---EELIAERRETIEEKRERAEELRERAAELE--AEAEEKREAAAEAE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 458 IMPVEYREVFIRLqhENKMLRLQQEGSENERIEELQ-------EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKS 530
Cdd:PRK02224 565 EEAEEAREEVAEL--NSKLAELKERIESLERIRTLLaaiadaeDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 531 LQEqgsksegESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAAlqkkDEDMKAMEERyKMYL 610
Cdd:PRK02224 643 FDE-------ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL----RERREALENR-VEAL 710
|
490
....*....|
gi 41688595 611 EKARNVIKTL 620
Cdd:PRK02224 711 EALYDEAEEL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-609 |
5.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSL---VSENEMMNEKLDQLDG--SFDDPNTV--VAKKY 247
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKKEELERlkKRLTGLTPekLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 248 FHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQ----------------HRNDELTSLAEETRALKDEIDVLRA 311
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 312 TSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAArtQLETYKRQVQDLHVKLSSESKR 391
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQLKE-----------LEEKLKKYNLE--ELEKKAEEYEKLKEKLIKLKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 392 ADTLAFEMKRLEEkheaLLKEKERLIEQRDTLKETNEELrcsqvqqdhLNQTDASATKSYENLAAEIMPVE--YREvFIR 469
Cdd:PRK03918 541 IKSLKKELEKLEE----LKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELEERLKELEpfYNE-YLE 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 470 LQHENKMLRlqqegSENERIEELQEQLEQKHRKMNELETeqrlskeRIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQK 549
Cdd:PRK03918 607 LKDAEKELE-----REEKELKKLEEELDKAFEELAETEK-------RLEELRKELEELEKKYSEEEYEELREEYLELSRE 674
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 550 LEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEaALQKKDEDMKAMEERYKMY 609
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKY 733
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-570 |
9.24e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 244 AKKYFHAQLQLEqlqeenfRLEAAKDDYRVHCEELEKQLiefQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTV 323
Cdd:COG1196 231 LLKLRELEAELE-------ELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQA---EEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 324 EIYRQKLQDLNDLRKQvktlqetnmmymhNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAfemKRLE 403
Cdd:COG1196 298 ARLEQDIARLEERRRE-------------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 404 EKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEG 483
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---------ERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 484 SENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 563
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
....*..
gi 41688595 564 LQKKQEL 570
Cdd:COG1196 513 ALLLAGL 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
382-663 |
1.20e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 382 HVKLSSESKRADTLA-FEMKRLEEKHEALLKEKERlieqRDTLKETnEELRCSQVQQDhlnqtdASATKSYENLAAEIMP 460
Cdd:pfam17380 280 HQKAVSERQQQEKFEkMEQERLRQEKEEKAREVER----RRKLEEA-EKARQAEMDRQ------AAIYAEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 461 VEYREVFIRLQHENKMLRLQQEGSENERIEELQ----EQLEQKHRKMNELETEQR---LSKERIRELQQQIEDLQKSLQE 533
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRELErlqmERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 534 QGSKSEGESSSkLKQKLEAHMEKlteVHEELQKKQELIEDLQPDINQNVQKINELEaalqKKDEDMKAMEERYKMYLEKa 613
Cdd:pfam17380 429 QEEARQREVRR-LEEERAREMER---VRLEEQERQQQVERLRQQEEERKRKKLELE----KEKRDRKRAEEQRRKILEK- 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41688595 614 rnviktldpklnpasaEIMLLRKQLAEKERRIEILESECKVAKFRDYEEK 663
Cdd:pfam17380 500 ----------------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-663 |
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 41688595 178 QQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQL 257
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 258 QEENFRLEAAK---DDYRVHCEELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRqKLQDLN 334
Cdd:PTZ00121 1360 EAAEEKAEAAEkkkEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 335 DLRKQVKTLQETNmmymhntvSLEEELKKANAARTQLETyKRQVQDLHVKlSSESKRADTLAFEMKRLEEKHEALlKEKE 414
Cdd:PTZ00121 1438 KKAEEAKKADEAK--------KKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA-KKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 415 RLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEimpveyrevfirlqhENKMLRLQQEGSENERIEELQE 494
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD---------------ELKKAEELKKAEEKKKAEEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 495 QLEQKHRKMNELETEQRLSKERIREL--------QQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTE---VHEE 563
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVmklyeeekKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkKAEE 1651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 564 LQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKtldpklnpasaeimlLRKQLAEKER 643
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE---------------LKKKEAEEKK 1716
|
490 500
....*....|....*....|
gi 41688595 644 RIEILESECKVAKFRDYEEK 663
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAK 1736
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
290-653 |
2.37e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 290 DELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQK----LQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKA- 364
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTq 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 365 ---NAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERlieqrDTLKETNEELRCsqvQQDHLN 441
Cdd:TIGR04523 253 tqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ-----DWNKELKSELKN---QEKKLE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 442 QTDASATKSYENLAaeimpveyrevfiRLQHENKMLRLQQEGSENERiEELQEQLEQKHRKMNELETEQRLSKERIRELQ 521
Cdd:TIGR04523 325 EIQNQISQNNKIIS-------------QLNEQISQLKKELTNSESEN-SEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 522 QQIEDLQKSLQEQgsksegessSKLKQKLEahmEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEaalqKKDEDMKA 601
Cdd:TIGR04523 391 SQINDLESKIQNQ---------EKLNQQKD---EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT----NQDSVKEL 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 41688595 602 MEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECK 653
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
171-662 |
2.41e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 171 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQL----DGSFDDPNTVVAKK 246
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAH 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 247 YFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIY 326
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 327 RQKLQDLNDLRKQVKTLQETNMMYMHNtvsLEEELkkaNAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLeekh 406
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHD---LEIQL---TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL---- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 407 eallkekerLIEQRDTLKETNEELRCSQVQQDHLNqtdaSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSEN 486
Cdd:pfam05483 498 ---------LLENKELTQEASDMTLELKKHQEDII----NCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 487 E-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQ 565
Cdd:pfam05483 565 KcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE------------LHQENKALKKKGSAENKQLN 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 566 KKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVI-------KTLDPKLNPASAEIM-LLRKQ 637
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAdeavklqKEIDKRCQHKIAEMVaLMEKH 712
|
490 500
....*....|....*....|....*
gi 41688595 638 LAEKERRIEILESECKVAKFRDYEE 662
Cdd:pfam05483 713 KHQYDKIIEERDSELGLYKNKEQEQ 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
292-669 |
3.01e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 292 LTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVS----LEEELKKANAA 367
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkaLEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 368 RTQL-ETYKRQVQDLHVKLSSESKRADTLAFEMKRLEekhEALLKEKERLIEQRDTLKETNEELRCSQVQQDHL------ 440
Cdd:pfam05483 326 ICQLtEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfknn 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 441 --------------NQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQ--------QEGSENERIEELQEQLEQ 498
Cdd:pfam05483 403 keveleelkkilaeDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktSEEHYLKEVEDLKTELEK 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 499 KHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGEsssklkQKLEAHMEKLTEVHEElqKKQELIEDLQPDI 578
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC------KKQEERMLKQIENLEE--KEMNLRDELESVR 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 579 NQNVQKINELEAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKLNPasaeimlLRKQLAEKERRIEILESECKVAKFR 658
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYE----VLKKEKQMKILENKCNN-------LKKQIENKNKNIEELHQENKALKKK 623
|
410
....*....|.
gi 41688595 659 DYEEKLIVSAW 669
Cdd:pfam05483 624 GSAENKQLNAY 634
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
449-653 |
3.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 449 KSYENLAAEIMPVEYREvfirlqhENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRI-------ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 529 KSLQEqgSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdinQNVQKINELEaalqKKDEDMKAMEERYKM 608
Cdd:PRK03918 235 ELKEE--IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----EKVKELKELK----EKAEEYIKLSEFYEE 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41688595 609 YLEKARNVIKTLDpKLNPASAEIMLLRKQLAEKERRIEILESECK 653
Cdd:PRK03918 305 YLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
273-533 |
3.20e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.70 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 273 VHCEELEKQLIEFQHRndELTSLAEEtraLKDEIDVLRATSDKANKLESTVEiyRQKLQDLNDLRKQVKTlqetnmmymh 352
Cdd:PRK05771 31 VHIEDLKEELSNERLR--KLRSLLTK---LSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEE---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 353 NTVSLEEELKKANAARTQLETYKRqvqdlhvKLSSESKRADTL-AFEMKrleekhEALLKEKERLIEQRDTLKETNEELR 431
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIK-------ELEQEIERLEPWgNFDLD------LSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 432 CSQVQQDhlNQTDASATKSYENLAAeIMPVEYREVFIRL--QHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELete 509
Cdd:PRK05771 161 KLESDVE--NVEYISTDKGYVYVVV-VVLKELSDEVEEElkKLGFERLELEEEGTPSELIREIKEELEEIEKERESL--- 234
|
250 260
....*....|....*....|....
gi 41688595 510 qrlsKERIRELQQQIEDLQKSLQE 533
Cdd:PRK05771 235 ----LEELKELAKKYLEELLALYE 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
480-703 |
3.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 480 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEA-HMEKLT 558
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVsYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 559 EVH--EELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRK 636
Cdd:COG3883 110 GSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 637 QLAEKERRIEILESECKVAKFRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGGGACSDTGACTPARS 703
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-523 |
5.97e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLdgsfddpntvvAKKYFH 249
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-----------EEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 250 AQLQLEQLQEENFRLEAAKDDYRVHCEELEKQL--IEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYR 327
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 328 QKLQDLndlrkqVKTLQETNMMYMHNTVSLEEELKKANaarTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHE 407
Cdd:TIGR02169 829 EYLEKE------IQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 408 ALLKEKERLIEQRDTLKETNEELRCS-QVQQDHLNQTDA---------SATKSYENLAAEIMPVEYRevfIRLQHENKML 477
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKlEALEEELSEIEDpkgedeeipEEELSLEDVQAELQRVEEE---IRALEPVNML 976
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41688595 478 RLQQEGSENERIEELQEQLEQkhrkmneLETEQRLSKERIRELQQQ 523
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAK-------LEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-595 |
6.22e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 403 EEKHEALLKEKERLIEQRDTLKETNEELrcsQVQQDHLNQtdasatksyeNLAAEIMPVEYREVFIRL-QHENKMLRLQQ 481
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL---EAELDALQE----------RREALQRLAEYSWDEIDVaSAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 482 E----GSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ---KSLQEQGSKSEGESSSKLKQKLEAHm 554
Cdd:COG4913 676 ElerlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEER- 754
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41688595 555 eklteVHEELQKK--QELIEDLQPDINQNVQKINELEAALQKK 595
Cdd:COG4913 755 -----FAAALGDAveRELRENLEERIDALRARLNRAEEELERA 792
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-614 |
8.91e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 290 DELTSLAEETRALKDEI------DVLRATSDKANKLESTVEIYRQKLQDLNDLRK--QVKTLQETNMMymhnTVSLEEEL 361
Cdd:COG3206 71 SGLSSLSASDSPLETQIeilksrPVLERVVDKLNLDEDPLGEEASREAAIERLRKnlTVEPVKGSNVI----EISYTSPD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 362 KK--ANAARTQLETYKRQVQDLhvKLSSESKRADTLAFEMKRLEEKhealLKEKERLIEQrdtLKETNEELRcSQVQQDH 439
Cdd:COG3206 147 PElaAAVANALAEAYLEQNLEL--RREEARKALEFLEEQLPELRKE----LEEAEAALEE---FRQKNGLVD-LSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 440 LNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQqEGSENERIEELQEQLEQKHRKMNELEteQRLSKE--RI 517
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAELEAELAELS--ARYTPNhpDV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 518 RELQQQIEDLQKSLQEQGSKsegessskLKQKLEAHMEKLTEVHEELQKKQEliedlqpDINQNVQKINELEAALQKKDE 597
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQR--------ILASLEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLER 358
|
330
....*....|....*..
gi 41688595 598 DMKAMEERYKMYLEKAR 614
Cdd:COG3206 359 EVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
178-609 |
9.87e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 178 QQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvvakkyfhaqlqleql 257
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP------------------------ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 258 qeenfrLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTveiyrQKLQDLNDLR 337
Cdd:COG4717 130 ------LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-----ATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 338 KQVKTLQETNMMYMHNTVSLEEELKKANAARTQLET------YKRQVQDLHVKLSSESKRAD------------------ 393
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENeleaaaLEERLKEARLLLLIAAALLAllglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 394 -----TLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDAsaTKSYENLAAEImpVEYREVFI 468
Cdd:COG4717 279 lflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS--PEELLELLDRI--EELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 469 RLQHENKmlRLQQEGSENERIEELQ-------EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGE 541
Cdd:COG4717 355 EAEELEE--ELQLEELEQEIAALLAeagvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688595 542 SSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDinqnvQKINELEAALQKKDEDMKAMEERYKMY 609
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAAL 495
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
476-600 |
1.19e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 476 MLRLQQEgSENERIEELQEQLEQKHRKMNELETEQRL-SKERIRELQQQIEDLQKSLQEqgsksegesssklkqkLEAHM 554
Cdd:COG0542 401 RVRMEID-SKPEELDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEA----------------LKARW 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41688595 555 EKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMK 600
Cdd:COG0542 464 EAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
405-591 |
1.19e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 405 KHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEImpveyREVFIRLQHENKMLRLQQEGS 484
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-----EKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 485 ENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgsksEGESSSKLKQKLEAHMEKLTEVHEEL 564
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA----TEEELQDLAEELEELQQRLAELEEEL 215
|
170 180
....*....|....*....|....*..
gi 41688595 565 QKKQELIEDLQPDINQNVQKINELEAA 591
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALE 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
420-665 |
1.20e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 420 RDTLKETNEELRCSQVQQDHLNQTdasaTKSYENLAAEimpveyrevfirlqhenkmlrlqQEGSENERIEELQEQLEQK 499
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQ----IKTYNKNIEE-----------------------QRKKNGENIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 500 HRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegesSSKLKQKLEAHMEKLTEVHEELQKKQEL------IED 573
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK---------LNTAAAKIKSKIEQFQKVIKMYEKGGVCptctqqISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 574 LQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEkARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECK 653
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*..
gi 41688595 654 -----VAKFRDYEEKLI 665
Cdd:PHA02562 376 dnaeeLAKLQDELDKIV 392
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
263-534 |
1.23e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETraLKDEIDVLRATSDKANKLESTVeiyRQKLQDLNDLRKQVKT 342
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAKRFV---QQHGNALAQLEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 343 LQETNMMYmhntvsleEELKKA-NAARTQLETYKRQVQDLhvklSSESKRADTLAFE--MKRLEEKHEALLKEKERLIEQ 419
Cdd:PRK04863 930 LQSDPEQF--------EQLKQDyQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEdaAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 420 RDTLKETNEELRCSQVQQDHLNQTDASATKSYENlaaeimpveYREVFIRLQHENKMLRLQQEGSENERI----EELQEQ 495
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA---------KRQMLQELKQELQDLGVPADSGAEERArarrDELHAR 1068
|
250 260 270
....*....|....*....|....*....|....*....
gi 41688595 496 LEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
310-600 |
1.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 310 RATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSes 389
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERYAAARERLAELEYLRAALRLWFAQ-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 390 KRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKEtneelrcsqvqqdhlnqtdasatksyenlaaeimpvEYREvfir 469
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALRE------------------------------------ELDE---- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 470 lqhenkmLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgSKSEGESSSKLKQK 549
Cdd:COG4913 328 -------LEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL-RAEAAALLEALEEE 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41688595 550 LEAHMEKLTEVHEELQKKQELIEDLQPDIN----------QNVQKI-NELEAALQKKDEDMK 600
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIAslerrksnipARLLALrDALAEALGLDEAELP 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
484-651 |
1.48e-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: 47.84 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 484 SENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEE 563
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA------------LARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 564 LQKKQELIEDLQPDINQNVQKINELEAALQK-----------KDEDMKAMEERYkMYLEKARNVIKTLDPKLNPASAEIM 632
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELA 163
|
170
....*....|....*....
gi 41688595 633 LLRKQLAEKERRIEILESE 651
Cdd:COG4942 164 ALRAELEAERAELEALLAE 182
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
354-615 |
1.82e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 354 TVSLEEELKKANAARTQLETYKR-------QVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKET 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEkrdelneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 427 NEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYRevfirlqHENKMLRLQQEGSENERIEELQEQLE------QKH 500
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-------QQTEVLSPEEEKELVEKIKELEKELEkakkalEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 501 RKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQ 580
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQE-----LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 41688595 581 NVQKINELEAALQ---------KKDEDMKAMEERYKMYLEKARN 615
Cdd:COG1340 235 LQKELRELRKELKklrkkqralKREKEKEELEEKAEEIFEKLKK 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-569 |
2.23e-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: 47.45 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 327 RQKLQDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 406
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 407 EALlkeKERLIEQRDTLKETNeelrcsQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHEnkmlRLQQEGSEN 486
Cdd:COG4942 93 AEL---RAELEAQKEELAELL------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE----QAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 487 ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESssklkQKLEAHMEKLTEVHEELQK 566
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIARLEA 234
|
...
gi 41688595 567 KQE 569
Cdd:COG4942 235 EAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-533 |
2.62e-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: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 177 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLvsenemmnEKLDQLDGSFDDpntvvakkyfhaqlqleq 256
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEID------------------ 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 257 lqeenfrleaakddyrvhceelekqliefqhrndeLTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDL 336
Cdd:COG4913 663 -----------------------------------VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 337 RKQvktlqetnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE-KER 415
Cdd:COG4913 708 LDE-----------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElREN 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 416 LIEQRDTLKETNEELRcsqvqqDHLNQTDASATKSYENLAAEIMPV-----EYREVFIRLQ------HENKMLRLQQEgS 484
Cdd:COG4913 771 LEERIDALRARLNRAE------EELERAMRAFNREWPAETADLDADleslpEYLALLDRLEedglpeYEERFKELLNE-N 843
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 41688595 485 ENERIEELQEQLEQKhrkmneleteqrlskerIRELQQQIEDLQKSLQE 533
Cdd:COG4913 844 SIEFVADLLSKLRRA-----------------IREIKERIDPLNDSLKR 875
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
487-651 |
5.68e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 487 ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQK 566
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-----EQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 567 KQELIEDLQPDInQNVQKINELEAALQKKD-EDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRI 645
Cdd:COG4942 102 QKEELAELLRAL-YRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
....*.
gi 41688595 646 EILESE 651
Cdd:COG4942 181 AELEEE 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
487-664 |
7.43e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 487 ERIEELQEQLEqkhRKMNELETeQRLSKERIRELQQQIEDLQKSL-------QEQGSKSEGESSSKLKQKLEAHMEKLTE 559
Cdd:TIGR02168 189 DRLEDILNELE---RQLKSLER-QAEKAERYKELKAELRELELALlvlrleeLREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 560 VHEEL-------QKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMY----------LEKARNVIKTLDP 622
Cdd:TIGR02168 265 LEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELeaqleeleskLDELAEELAELEE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 41688595 623 KLNPASAEIMLLRKQLAEKERRIEILESeckvaKFRDYEEKL 664
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELES-----RLEELEEQL 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-628 |
1.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 392 ADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ 471
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 472 HEN------KMLRLQQEGSENERIEELQEQleqkhRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegesSSK 545
Cdd:COG4942 99 LEAqkeelaELLRALYRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAE---------LAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 546 LKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLN 625
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 41688595 626 PAS 628
Cdd:COG4942 245 AAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
280-651 |
1.06e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 280 KQLIEFQHR----NDELTSLAEETRALKDEidvLRATSDKANKLESTV------EIYRQKLQDLN-DLRKQVKTLQETNM 348
Cdd:COG3096 299 RQLAEEQYRlvemARELEELSARESDLEQD---YQAASDHLNLVQTALrqqekiERYQEDLEELTeRLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 349 MYMHNTVSLEEELKKANAARTQLETYKRQVQDLHvklssesKRADTLAFEMKRLEEKhEALLKE--------KERLIEQR 420
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQ-------TRAIQYQQAVQALEKA-RALCGLpdltpenaEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 421 DTLKETNEELRcsqVQQDHLNQTDASAT---KSYENLAAEIMPVEYREVFirlQHENKMLRlqqEGSENERIEELQEQLE 497
Cdd:COG3096 448 AKEQQATEEVL---ELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAW---QTARELLR---RYRSQQALAQRLQQLR 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 498 QKHRkmnelETEQRLskERIRELQQQIEDLQKSLQEQGsksegesssklkqkleAHMEKLTEVHEELQkkqELIEDLQPD 577
Cdd:COG3096 519 AQLA-----ELEQRL--RQQQNAERLLEEFCQRIGQQL----------------DAAEELEELLAELE---AQLEELEEQ 572
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 578 INQNVQKINELEAALQKKDEDMKAMEERYKMYLeKARNVIKTLDPKLNPA---SAEIMLLRKQLAEKERRIEILESE 651
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKELAARAPAWL-AAQDALERLREQSGEAladSQEVTAAMQQLLEREREATVERDE 648
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
357-552 |
1.33e-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: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 357 LEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE----KERLIEQRDTLKEtneelRC 432
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGE-----RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 433 SQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRlqHENKMLRLQQEgsENERIEELQEQLEQKHRKMNELETEQRL 512
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIAD--ADADLLEELKA--DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 41688595 513 SKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEA 552
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
358-657 |
1.37e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 358 EEELKKANAARTQLETYKRQVQ---DLHVKLSSESKRadtlaFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQ 434
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQaemDRQAAIYAEQER-----MAMERERELERIRQEERKRELERIRQEEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 435 VQQDHLNQTDASATKSYENLAA---EIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQR 511
Cdd:pfam17380 380 LERLQMERQQKNERVRQELEAArkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 512 LSKERIRelQQQIEDLQKSLQEQGSKSEGESSSKLKQK-LEAHMEKLTEVHEELQKKQELIEdlqpdinqnvQKINELEA 590
Cdd:pfam17380 460 QQVERLR--QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLE----------KEMEERQK 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 591 ALQKKDEDMKAMEERYKMYLEKARNVIKTldpKLNPASAEIMLLRKQLAEKERRIEILESECKVAKF 657
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
276-656 |
1.65e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 276 EELEKQLIEFQHRNDELTSLAEE--TRALKDEIDvlratsDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHN 353
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEQdwNKELKSELK------NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 354 TVSLEEELKKANAA-----------RTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDT 422
Cdd:TIGR04523 358 NSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 423 LKETNEELrcsqvqqdhlNQTDASATKSYENLaaeimpveyrEVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRK 502
Cdd:TIGR04523 438 NNSEIKDL----------TNQDSVKELIIKNL----------DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 503 MNELETEQRLSKERIRELQQQIEDLQKSLqeqgsksegesssklkQKLEAhmEKLTEVHEELQKKQELIEDlqpdinQNV 582
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKI----------------EKLES--EKKEKESKISDLEDELNKD------DFE 553
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688595 583 QKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKlnpaSAEIMLLRKQLAEKERRIEILESECKVAK 656
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK----EKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
407-646 |
2.31e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 407 EALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQtDASATKSYENLaaeimpveyreVFIRLQHENKMLRLQQEGSE- 485
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELEELSARESDLEQ-DYQAASDHLNL-----------VQTALRQQEKIERYQEDLEEl 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 486 NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSL--------QEQGSKSEGESSSKLKQKLEAHMEKL 557
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvqqtraiQYQQAVQALEKARALCGLPDLTPENA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 558 TEVHEELQKKQELIEDLQPDINqnvQKINELEAALQKKDEDMKAME------ERYKMYlEKARNVIKTLdPKLNPASAEI 631
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELE---QKLSVADAARRQFEKAYELVCkiagevERSQAW-QTARELLRRY-RSQQALAQRL 514
|
250
....*....|....*
gi 41688595 632 MLLRKQLAEKERRIE 646
Cdd:COG3096 515 QQLRAQLAELEQRLR 529
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
302-581 |
2.83e-04 |
|
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: 44.58 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 302 LKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEEL-KKANAARTQLETYKRQVQD 380
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 381 LHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYEnlaaeimp 460
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-------- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 461 vEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEG 540
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41688595 541 ESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQN 581
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
359-534 |
2.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 359 EELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLiEQRDTLKETNEELRCSQVQQD 438
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 439 HLNQTDasatKSYENLAAEImpVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIR 518
Cdd:COG4717 150 ELEERL----EELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*.
gi 41688595 519 ELQQQIEDLQKSLQEQ 534
Cdd:COG4717 224 ELEEELEQLENELEAA 239
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
291-663 |
2.97e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 291 ELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLN-----------DLRKQVKTLQETNMMYMHNTVSLEE 359
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKkqiaddekshsITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 360 ELKKANAARTQLETYKRQVQDLHVKLSSESKRADtlafEMKRLEEKH-----EALLKEKERLIE------QRDTLKETNE 428
Cdd:PRK01156 240 ALNELSSLEDMKNRYESEIKTAESDLSMELEKNN----YYKELEERHmkiinDPVYKNRNYINDyfkyknDIENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 429 ELRcSQVQQDHLNQTDASATKSYENlAAEIMPVEYREVfirlqhenKMLRLQQEGSENERIEELQEqLEQKHRKMNELET 508
Cdd:PRK01156 316 NID-AEINKYHAIIKKLSVLQKDYN-DYIKKKSRYDDL--------NNQILELEGYEMDYNSYLKS-IESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 509 EQ-RLSKERIRELQQQI---EDLQKSLQE--QGSKSEGESSSKLKQKLEAHMEKLTEVHEEL------------------ 564
Cdd:PRK01156 385 NIeRMSAFISEILKIQEidpDAIKKELNEinVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlge 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 565 QKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERyKMYLEKAR-NVIKTLDPKLNPASAEI---MLLRKQLAE 640
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR-KEYLESEEiNKSINEYNKIESARADLediKIKINELKD 543
|
410 420
....*....|....*....|...
gi 41688595 641 KERRIEILESECKVAKFRDYEEK 663
Cdd:PRK01156 544 KHDKYEEIKNRYKSLKLEDLDSK 566
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
464-617 |
3.11e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 464 REVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKslQEQGSKSEGESS 543
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ--KQQELEKKEEEL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688595 544 SKLKQKLEAHMEKLTEVHEElQKKQELIEDLQPDInqnvqkinELEAALQKKDEDMKAMEERYKmyleKARNVI 617
Cdd:PRK12704 134 EELIEEQLQELERISGLTAE-EAKEILLEKVEEEA--------RHEAAVLIKEIEEEAKEEADK----KAKEIL 194
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
170-659 |
3.44e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELD---MQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvvakk 246
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQSSLAEAEQRIKELE------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 247 YFHAQLQLEQLQEENFRLEAAKddyrvhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKANKL 319
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSELAR------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAATL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 320 ESTVEIYRQKLQ-----------DLN---DLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQdlhvkl 385
Cdd:pfam05557 251 ELEKEKLEQELQswvklaqdtglNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYL------ 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 386 ssesKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELrcsqvqQDHLNQTDASATKSYENLAAEIMPVEYRE 465
Cdd:pfam05557 325 ----KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESY------DKELTMSNYSPQLLERIEEAEDMTQKMQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 466 VFIRLQHENKMLrLQQEGSENERIEELQEQLeqKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKsegesssk 545
Cdd:pfam05557 395 HNEEMEAQLSVA-EEELGGYKQQAQTLEREL--QALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQ-------- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 546 lKQKLEAHMEkltevheelqkKQELIEDLQPDINQNVQ-KINELEAALQKKDEDMKAME---ERYKMYLEKARNVIKTLD 621
Cdd:pfam05557 464 -KNELEMELE-----------RRCLQGDYDPKKTKVLHlSMNPAAEAYQQRKNQLEKLQaeiERLKRLLKKLEDDLEQVL 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 41688595 622 ----PKLNPASAEIMLLRKQLAEKERRIEILESECKVA--KFRD 659
Cdd:pfam05557 532 rlpeTTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKiqEFRD 575
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
468-624 |
3.45e-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: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 468 IRLQH-ENKMLRLQQE-GSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ---KSLQEQGSKSE--- 539
Cdd:COG1579 10 LDLQElDSELDRLEHRlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVRnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 540 -----GESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALqkkDEDMKAMEERYKMYLEKAR 614
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAERE 166
|
170
....*....|
gi 41688595 615 NVIKTLDPKL 624
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
400-534 |
4.49e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.82 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 400 KRLEEKHEALLKEKERLIEQRDTLKETnEELRcsQVQQDHLNQTdasATKSYENLAAEIMPVEYREVFIRLQHENKMLRL 479
Cdd:pfam13779 489 RRLRAAQERLSEALERGASDEEIAKLM-QELR--EALDDYMQAL---AEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDR 562
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 41688595 480 QQEGSENERIEELQEQLEQKHRKMNELETEQR--LSKERIRELQQQIEDLQKSLQEQ 534
Cdd:pfam13779 563 IEELARSGRRAEAQQMLSQLQQMLENLQAGQPqqQQQQGQSEMQQAMDELGDLLREQ 619
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
520-665 |
4.88e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 520 LQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdinqnvQKINELEAALQKKDEDM 599
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLEREL 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41688595 600 KAMEERYKMYLEKaRNVIKTLDpklnpasAEIMLLRKQLAEKERRIEILESecKVAKFRDYEEKLI 665
Cdd:COG2433 451 SEARSEERREIRK-DREISRLD-------REIERLERELEEERERIEELKR--KLERLKELWKLEH 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
487-662 |
5.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 487 ERIEELQEQLEQKHRKMNELET--EQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEEL 564
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 565 QKKQELIEDLQPDINQNVQKINELEAALQKKDEDmkameerykmylekarnviktldpKLNPASAEIMLLRKQLAEKERR 644
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGD------------------------RLEQLEREIERLERELEERERR 360
|
170
....*....|....*...
gi 41688595 645 IEILESECKVAKFRDYEE 662
Cdd:COG4913 361 RARLEALLAALGLPLPAS 378
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
161-533 |
8.19e-04 |
|
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: 43.04 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 161 SKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPN 240
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 241 TVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSDKANKLE 320
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-------EKLKVEEEKEEKLKAQEEELRALE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 321 STVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMK 400
Cdd:pfam02463 808 EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 401 RLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ-HENKMLRL 479
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEeERNKRLLL 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41688595 480 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
506-592 |
8.89e-04 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 41.11 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 506 LETEQRLSKERIRELQQQIEDLQKSLQEqgsksegesssklkqkleahMEKLTEVHEELQKKQELIEDLQPDINQNVQKI 585
Cdd:COG3166 43 LQGQIAQQQARNAALQQEIAKLDKQIAE--------------------IKELKKQKAELLARLQVIEQLQQSRPPWVHLL 102
|
....*..
gi 41688595 586 NELEAAL 592
Cdd:COG3166 103 DELARLL 109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
465-650 |
9.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 465 EVFIRLQHENKMLRLQQEGSE-NERIEELQEQLEQKHRK-----------------------MNELETEQRLSKERIREL 520
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFlEEQLPELRKELEEAEAAleefrqknglvdlseeaklllqqLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 521 QQQIEDLQKSLQEQGSKSEGESS-----------SKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKI-NEL 588
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41688595 589 EAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKlnpasaeimllRKQLAEKERRIEILES 650
Cdd:COG3206 319 EAELEALQAREASLQAQ----LAQLEARLAELPEL-----------EAELRRLEREVEVARE 365
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
165-393 |
9.50e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.53 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 165 LSSPpnDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpNTVVA 244
Cdd:pfam09726 391 LSKP--DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLH---------NAVSA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 245 KKyfhaqlqleqlqeenfrleaaKDDYRVhcEELEKQLIEFQ-HRNDELTSLAEETRALKDEIDVL-RATSDKANKLEST 322
Cdd:pfam09726 460 KQ---------------------KDKQTV--QQLEKRLKAEQeARASAEKQLAEEKKRKKEEEATAaRAVALAAASRGEC 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41688595 323 VEIYRQKLQdlnDLRKQVKTLQetnmmymHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRAD 393
Cdd:pfam09726 517 TESLKQRKR---ELESEIKKLT-------HDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQD 577
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
276-557 |
1.18e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 276 EELEKQLIEFQHRNDELTSLAEETRALKDE-IDVLRATSDKANKLESTVEIYRQKLQDLNDLRK----QVKTLQEtnmmy 350
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEAQELREKRDelneKVKELKE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 351 mhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSEskraDTLAFEMKRLEEKHE--ALLKEKER-LIEQRDTLKETN 427
Cdd:COG1340 79 -----ERDELNEKLNELREELDELRKELAELNKAGGSI----DKLRKEIERLEWRQQteVLSPEEEKeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 428 EELRCSQVQQDHLNQTDASATKSYENLAAEIMPV-EYREvfIRLQHENKMLRLQQEGSE-NERIEELQEQLEQKHRKMNE 505
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIkELAE--EAQELHEEMIELYKEADElRKEADELHKEIVEAQEKADE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41688595 506 LETEQRLSKERIRELQQQIEDLQKslqEQGSKSEGESSSKLKQKLEAHMEKL 557
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRK---KQRALKREKEKEELEEKAEEIFEKL 276
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
107-342 |
1.54e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 107 QITECSDPVE---LGRLLQLilgcAINCEKKQEHIQNIMTLEESVQHVVMTaIQELMSKEILSSPpNDAVGELEQQLKRA 183
Cdd:PRK05771 32 HIEDLKEELSnerLRKLRSL----LTKLSEALDKLRSYLPKLNPLREEKKK-VSVKSLEELIKDV-EEELEKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 184 LEELQEALAEKEELRQRCEEL------DMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYfhaqlqleqL 257
Cdd:PRK05771 106 EEEISELENEIKELEQEIERLepwgnfDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTD---------K 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 258 QEENFRLEAAKDDYRVHCEELEK---QLIEFQHR---NDELTSLAEETRALKDEIDVLRAT-SDKANKLE----STVEIY 326
Cdd:PRK05771 177 GYVYVVVVVLKELSDEVEEELKKlgfERLELEEEgtpSELIREIKEELEEIEKERESLLEElKELAKKYLeellALYEYL 256
|
250
....*....|....*.
gi 41688595 327 RQKLQDLNDLRKQVKT 342
Cdd:PRK05771 257 EIELERAEALSKFLKT 272
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
357-649 |
1.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 357 LEEELKKANAARTQLETYKRQVQDLHVKLSS--ESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEElrcsq 434
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 435 vqqdhlnqtdasatksyenlaAEIMPVEYREvfirlqhenkmlrlqqegsENERIEELQEQLEQKHRKMNELETEQRLSK 514
Cdd:PRK02224 239 ---------------------ADEVLEEHEE-------------------RREELETLEAEIEDLRETIAETEREREELA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 515 ERIRELQQQIEDLQKSLQEQGSKSEGEsssklkqklEAHMEKLTEVHEELQKKQELIEDlqpDINQNVQKINELEAALQK 594
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLD---------DADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAES 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41688595 595 KDEDMKAMEERYKmyleKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILE 649
Cdd:PRK02224 347 LREDADDLEERAE----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
484-574 |
1.85e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 40.75 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 484 SENERIEELQEQLEQKhrkmneleteqrlsKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 563
Cdd:pfam03961 153 ELKEKLEELEKELEEL--------------EEELEKLKKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEE 218
|
90
....*....|.
gi 41688595 564 LQKKQELIEDL 574
Cdd:pfam03961 219 LKELKEELESL 229
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
482-652 |
1.91e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 482 EGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKltevH 561
Cdd:COG2433 401 KEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE------------ARSEERREIRK----D 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 562 EELQKKQELIEDLQPDINQNVQKINELEAALQKKdEDMKAMEERYKMYLEKA-----RNVIKTLDPKLNPASAEIMLLRK 636
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHSGELVPVKVvekftKEAIRRLEEEYGLKEGDVVYLRD 543
|
170 180
....*....|....*....|....*.
gi 41688595 637 ----------QLAEKERRIEILESEC 652
Cdd:COG2433 544 asgagrstaeLLAEAGPRAVIVPGEL 569
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
135-663 |
2.12e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 135 QEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDE 214
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 215 KNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEfQHRNDELTS 294
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK-SEDLLKETQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 295 LAEETRALKDEIDV---------LRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKAN 365
Cdd:pfam02463 479 LVKLQEQLELLLSRqkleersqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 366 AARTQLETYKRQVQDLHVK-----LSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHL 440
Cdd:pfam02463 559 EVEERQKLVRALTELPLGArklrlLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 441 NQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgseNERIEELQEQLEQKHRKMNELETEQRLSKERIREL 520
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE---LQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 521 QQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQN--VQKINELEAALQKKDED 598
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaeEREKTEKLKVEEEKEEK 795
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41688595 599 MKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEK 663
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
172-619 |
2.15e-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: 41.49 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 172 AVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLD--GSFDDPNTVVAKKYFH 249
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLTQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 250 AQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAeetRALKDEIDVLRATSDKANKLESTVEIYRQK 329
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 330 LQDLNDLRKQVKTLQEtNMMYMHNTVSLEEELKKANAARTQLET-----YKRQVQDLHVKLsSESKRADTLAFEMKRLEE 404
Cdd:TIGR00618 458 KIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLELQeepcpLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQ 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 405 KHEALLKEKERLIEQRDTLKETNEELRcsqvQQDHLNQTDASATKSYENLAAEIMPVEYREVfIRLQHENKM---LRLQQ 481
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLK----EQMQEIQQSFSILTQCDNRSKEDIPNLQNIT-VRLQDLTEKlseAEDML 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 482 EGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE------QGSKSEGESSSKLKQKLEAHME 555
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirVLPKELLASRQLALQKMQSEKE 690
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688595 556 KLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKT 619
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
302-528 |
2.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 302 LKDEIDVLRATSDKANK-LESTVEIYRQKLQDLndlRKQVKTLQETNmmymhNTVSLEEElkkANAARTQLETYKRQVQD 380
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEA---EAALEEFRQKN-----GLVDLSEE---AKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 381 LHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE--RLIEQRDTLKETNEELRcSQVQQDH--LNQTDASATKSYENLAA 456
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELS-ARYTPNHpdVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41688595 457 EImpveyREVFIRLQHENKMLRlQQEGSENERIEELQEQLE---QKHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:COG3206 310 EA-----QRILASLEAELEALQ-AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
398-634 |
2.36e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 398 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPveyrEVFIRLQHENKML 477
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIE----NLEFKTELIARLK 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 478 RLQQEGS----------ENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDL---QKSLQEQGSKSEG--ES 542
Cdd:COG5022 935 KLLNNIDleegpsieyvKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELknfKKELAELSKQYGAlqES 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 543 SSKLKQK------LEAHMEKLTEVHEELQKKQelieDLQPDINQNVQKINELEA---ALQKKDEDMKAMEERyKMYLEKA 613
Cdd:COG5022 1015 TKQLKELpvevaeLQSASKIISSESTELSILK----PLQKLKGLLLLENNQLQArykALKLRRENSLLDDKQ-LYQLEST 1089
|
250 260
....*....|....*....|.
gi 41688595 614 RNVIKTLDPKLNPASAEIMLL 634
Cdd:COG5022 1090 ENLLKTINVKDLEVTNRNLVK 1110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
507-602 |
3.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 507 ETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdinqnvQKIN 586
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDA------------LQAELEELNEEYNELQAELEALQAEIDKLQ-------AEIA 75
|
90
....*....|....*.
gi 41688595 587 ELEAALQKKDEDMKAM 602
Cdd:COG3883 76 EAEAEIEERREELGER 91
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-606 |
3.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 171 DAVGELEQQLKRA---LEELQEALAEKEELRQRCEELDMQVTTLQDEKNSL--VSENEMMNEKLDQLDGSFDDPNTVVAK 245
Cdd:COG4717 71 KELKELEEELKEAeekEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 246 KYFHAQLQLEQLQEENfRLEAAKDDYRVHCEELEKQLI-----EFQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLE 320
Cdd:COG4717 151 LEERLEELRELEEELE-ELEAELAELQEELEELLEQLSlateeELQDLAEELEELQQRLAELEEELEEAQE---ELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 321 STVEIYRQKLQDLNDLRKQVKTLQETN--------MMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRA 392
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 393 DTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEI------MPVEYREV 466
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 467 FIRLQHenkmlRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLS--KERIRELQQQIEDLQKSLQEQGSKsegesss 544
Cdd:COG4717 387 LRAALE-----QAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREE------- 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41688595 545 klKQKLEAHMEKLTEVhEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERY 606
Cdd:COG4717 455 --LAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
475-605 |
3.55e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 475 KMLRLQQEGSENERIEE---LQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDlQKSLQEQGSKSEGESSSKLKQKLE 551
Cdd:pfam15709 344 EMRRLEVERKRREQEEQrrlQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-ERQRQEEEERKQRLQLQAAQERAR 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41688595 552 AHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEER 605
Cdd:pfam15709 423 QQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEER 476
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
177-456 |
3.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 177 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGsfddpntvvakkyfhaqlqleq 256
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 257 lqeenfRLEAAKDDYRVHCEELEKQLIEFQhRNDELTSLAEEtralkdeidVLRATS-----DKANKLESTVEIYRQKLQ 331
Cdd:COG3883 73 ------EIAEAEAEIEERREELGERARALY-RSGGSVSYLDV---------LLGSESfsdflDRLSALSKIADADADLLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 332 DLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDlhvKLSSESKRADTLAFEMKRLEEKHEALLK 411
Cdd:COG3883 137 ELKADKAELEAKKA----------ELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 41688595 412 EKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAA 456
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
291-607 |
3.77e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 291 ELTSLAEETRALKDEIDVLRATSdkaNKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMymHNTVSLEEELKKANAARTQ 370
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQE---QQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 371 LETYKRQVQDLHVKLSSeskradtlafeMKRLEEKHEALLKEKERLIEQRDTLKETNEELrcSQVQQ--DHLNQTDASAt 448
Cdd:COG3096 912 IQQHGKALAQLEPLVAV-----------LQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL--SEVVQrrPHFSYEDAVG- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 449 ksyenlaaeiMPVEYREVFIRLQHenKMLRLQQEGSE-NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDL 527
Cdd:COG3096 978 ----------LLGENSDLNEKLRA--RLEQAEEARREaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 528 QKSLQEQGSKSegesssklkqkleAHMEKlTEVHEELqkkqeliedlqpdiNQNVQKINELEAALQKKDEDMKAMEERYK 607
Cdd:COG3096 1046 GVQADAEAEER-------------ARIRR-DELHEEL--------------SQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
276-663 |
3.88e-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: 40.80 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 276 EELEKQLIEFQHRNDELTSLAE--------ETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQeTN 347
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPgrqsiidlKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCL-TD 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 348 MMYMHNtvsLEEELKKaNAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETN 427
Cdd:TIGR00606 791 VTIMER---FQMELKD-VERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 428 EELRCSQVQQDHLNQTDASATKSYENLAAEIMPVeYREVfirlqhenKMLRLQQEGSENERIEELQEQLEQKHRKmnelE 507
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL-IREI--------KDAKEQDSPLETFLEKDQQEKEELISSK----E 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 508 TEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKlEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINE 587
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 588 LEAALQ------KKDEDMKAMEERYKMYLE--------KARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECK 653
Cdd:TIGR00606 1013 QERWLQdnltlrKRENELKEVEEELKQHLKemgqmqvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
410
....*....|
gi 41688595 654 VAKFRDYEEK 663
Cdd:TIGR00606 1093 EPQFRDAEEK 1102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
176-589 |
4.10e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 176 LEQQLKRALEELQEALAEKEELRQRCEE---LDMQVTTLQDEKNSLVSENEM-MNEKLDQLDGSFDDPNTVVAKKYFHAQ 251
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCGSCIhPNPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 252 LQLEQLQeenfrLEAAKDDYRVHCEELEKQLIEFQHrndELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQ 331
Cdd:TIGR00618 540 LETSEED-----VYHQLTSERKQRASLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 332 DLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAfemkRLEEKHEALLK 411
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLA----SRQLALQKMQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 412 EKERLIEQRDTLKETNEELRC---------SQVQQDHLNQTDASATKSYENLAAEIMPVEYREVF------IRLQHENKM 476
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRElethieeydREFNEIENASSSLGSDLAAREDALNQSLKELMHQArtvlkaRTEAHFNNN 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 477 LRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgsksEGESSSKLKQKLEAHMEK 556
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET----LVQEEEQFLSRLEEKSAT 843
|
410 420 430
....*....|....*....|....*....|...
gi 41688595 557 LTEVHEELQKKQELIEDLQPDINQNVQKINELE 589
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| Med21 |
pfam11221 |
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ... |
173-210 |
5.25e-03 |
|
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.
Pssm-ID: 463241 Cd Length: 134 Bit Score: 37.96 E-value: 5.25e-03
10 20 30
....*....|....*....|....*....|....*...
gi 41688595 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTT 210
Cdd:pfam11221 97 IKELEEELREAEEERQEAVKEKEELLKKLDELIRSVAR 134
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
176-429 |
5.72e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 176 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTVVAKKYFHAQ 251
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRLSE-TDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 252 LQLEQLQEENFRLeaaKDDyrvhCEELEKQLIEFQHRNDELTSLAEEtRALKD------EIDVLRATSDKANKLESTVEI 325
Cdd:PLN02939 226 KELDVLKEENMLL---KDD----IQFLKAELIEVAETEERVFKLEKE-RSLLDaslrelESKFIVAQEDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 326 YRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYkrqvqdlhvKLSSEskRADTLAFEMKRLEEK 405
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS---------KFSSY--KVELLQQKLKLLEER 366
|
250 260 270
....*....|....*....|....*....|..
gi 41688595 406 HEALLKE--------KERLIEQRDTLKETNEE 429
Cdd:PLN02939 367 LQASDHEihsyiqlyQESIKEFQDTLSKLKEE 398
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
277-534 |
5.97e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 277 ELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRqklqdLNDLRKQVKTLQETNMMYMHNTVS 356
Cdd:COG3096 847 ELERELAQHR---AQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADR-----LEELREELDAAQEAQAFIQQHGKA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 357 LEEELKKANAART---QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLE----EKHEALLKE--------KERLIEQRD 421
Cdd:COG3096 919 LAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlneklRARLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 422 TLKETNEELRCSQVQQDHLNQTDASATKSYEnlAAEIMPVEYREVFIRLQhenkmLRLQQEGSENERIE--ELQEQLEQK 499
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRD--AKQQTLQELEQELEELG-----VQADAEAEERARIRrdELHEELSQN 1071
|
250 260 270
....*....|....*....|....*....|....*
gi 41688595 500 HRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:COG3096 1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-431 |
6.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 263 RLEAAKDDYRVHCEELEKQLIEFQHR-----NDELTSLAEETRALKDEIDVLRATSDKANKLESTVE--IYRQKLQDLND 335
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 336 LRKQVKTLQETNMMYMHNTVSLEEELK----KANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKR----LEEKHE 407
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdLRRELR 422
|
170 180
....*....|....*....|....
gi 41688595 408 ALLKEKERLIEQRDTLKETNEELR 431
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALR 446
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
174-614 |
6.61e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 174 GELEQQLKRALEELQEALAEKEELR-QRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDP------NTVVAKK 246
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQleqakrNKANLEK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 247 YFHAQLQLEQLQEENFR-LEAAKDDYRVHCEELEKQLIEFQHRNDEL----TSLAEETRALKDEID----VLRATSDKAN 317
Cdd:pfam01576 378 AKQALESENAELQAELRtLQQAKQDSEHKRKKLEGQLQELQARLSESerqrAELAEKLSKLQSELEsvssLLNEAEGKNI 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 318 KLESTVEIYRQKLQDLNDLRK-----------QVKTLQETNMMYMHNtvsLEEELKKANAARTQLETYKRQVQDLHVKLS 386
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQeetrqklnlstRLRQLEDERNSLQEQ---LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 387 SESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETN----EELRCSQVQQDHLNQTDASATKSYENLaaEIMPVE 462
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKnrlqQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAE 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 463 YREVFIRLQHENKmlRLQQEGSENE-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKsege 541
Cdd:pfam01576 613 EKAISARYAEERD--RAEAEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERS---- 686
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688595 542 sssklKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKIN-ELEAALQKKDEdmkAMEERYKMYLEKAR 614
Cdd:pfam01576 687 -----KRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKaQFERDLQARDE---QGEEKRRQLVKQVR 752
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
363-605 |
7.22e-03 |
|
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: 39.49 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 363 KANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEqrdtlkETNEELRCSQVQQDHLNQ 442
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA------ELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 443 TDASATKSYENLAAEimpveyrevfirlqhenKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIREL-- 520
Cdd:pfam07888 102 KYKELSASSEELSEE-----------------KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAga 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 521 QQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALqkkdEDMK 600
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL----EELR 240
|
....*
gi 41688595 601 AMEER 605
Cdd:pfam07888 241 SLQER 245
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
469-643 |
7.31e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 38.35 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 469 RLQHENKMLRLQQEGSEN--ERIEELQEQLEQKHRKMNEletEQRLSKERIRELQQQIEDLQKSLQEQgsksegessskl 546
Cdd:pfam15619 29 ELRKENRLLKRLQKRQEKalGKYEGTESELPQLIARHNE---EVRVLRERLRRLQEKERDLERKLKEK------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 547 kqklEAHMEKLtevHEELQKKQELIEDLQ-PDINQNVQKINELEAALQKKDEDMKAMEER-------YKMYLEKARNVIK 618
Cdd:pfam15619 94 ----EAELLRL---RDQLKRLEKLSEDKNlAEREELQKKLEQLEAKLEDKDEKIQDLERKlelenksFRRQLAAEKKKHK 166
|
170 180
....*....|....*....|....*
gi 41688595 619 TLDPKLNPASAEIMLLRKQLAEKER 643
Cdd:pfam15619 167 EAQEEVKILQEEIERLQQKLKEKER 191
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
171-528 |
7.97e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 171 DAVGELEQqlkrALEELQEALAEKEELRQRCEEldmQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvAKKYFHA 250
Cdd:COG3096 354 EDLEELTE----RLEEQEEVVEEAAEQLAEAEA---RLEAAEEEVDSLKSQLADYQQALDVQQTR--------AIQYQQA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 251 QLqleqlqeenfRLEAAK---DDYRVHCEELEKQLIEFQHRNDELTslaEETRALKDEIDVLRATS---DKANKLESTV- 323
Cdd:COG3096 419 VQ----------ALEKARalcGLPDLTPENAEDYLAAFRAKEQQAT---EEVLELEQKLSVADAARrqfEKAYELVCKIa 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 324 ---------EIYRQKLQDLNDLRKQVKTLQetnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADT 394
Cdd:COG3096 486 geversqawQTARELLRRYRSQQALAQRLQ-----------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 395 LAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcSQVQQdhlnqtdaSATKSYENLAAeimpveyREVFIRLQhen 474
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR-ARIKE--------LAARAPAWLAA-------QDALERLR--- 615
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41688595 475 kmlrlQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:COG3096 616 -----EQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
398-520 |
8.31e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 398 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqvqqdhlnqtdasaTKSYENLAAEIMPVEYREVFIRLQHENKML 477
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLE----------------RELSEARSEERREIRKDREISRLDREIERL 477
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41688595 478 RLQQEgSENERIEELQEQLEqKHRKMNELETEQR---------LSKERIREL 520
Cdd:COG2433 478 ERELE-EERERIEELKRKLE-RLKELWKLEHSGElvpvkvvekFTKEAIRRL 527
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
336-663 |
9.76e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 336 LRKQVKTLQETNMMYMHNTVSLEEELkkanaaRTQLETYkrqvQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKER 415
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDEL------RAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHER 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 416 LIEQRDTLKETNEELRCS-QVQQDHLNQTDASATKSYENLAAEIMPveyrevfiRLQHENKMLRLQQEGSENERIEELQE 494
Cdd:pfam10174 128 QAKELFLLRKTLEEMELRiETQKQTLGARDESIKKLLEMLQSKGLP--------KKSGEEDWERTRRIAEAEMQLGHLEV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 495 QLEQKHRKMNELETEQRLSKE------RIRELQQQIE--DLQKSLQEQGSKSEGESSSKLKQKLEAHMEkltEVHEELqk 566
Cdd:pfam10174 200 LLDQKEKENIHLREELHRRNQlqpdpaKTKALQTVIEmkDTKISSLERNIRDLEDEVQMLKTNGLLHTE---DREEEI-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688595 567 KQELIEDLQPDINQNvqKINELEAALQKKDEDMKAMEERykmylekarnvIKTLDPKLNPASAEIMLLRKQLAEKERRIE 646
Cdd:pfam10174 275 KQMEVYKSHSKFMKN--KIDQLKQELSKKESELLALQTK-----------LETLTNQNSDCKQHIEVLKESLTAKEQRAA 341
|
330
....*....|....*..
gi 41688595 647 ILESECKVAKFRdYEEK 663
Cdd:pfam10174 342 ILQTEVDALRLR-LEEK 357
|
|
| |
