|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
144-677 |
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: 647.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 144 ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTVVAKKYFHAQLQLEQLQEENFRLE 223
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 224 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQE 303
Cdd:pfam05622 80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 304 TNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKE 383
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 384 TNEELRCSQVQQDHLNQTDASATKSY---ENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRK 460
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSdpgDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 461 MNELETEQRLSKERIRELQQQIEDLQKSLQEQgsKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNV 540
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQ--GSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 541 -QKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPAS-AEIMLLRKQLAEKERRIEILESECKVAKF-RD 617
Cdd:pfam05622 398 aQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASpPEIQALKNQLLEKDKKIEHLERDFEKSKLqRE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 618 YEEKLIVSAWYNKSLAFQKLGMESRLVSGGGacsdtgactPARSFLAQQRHITNTRRNLS 677
Cdd:pfam05622 478 QEEKLIVTAWYNMGMALHRKAIEERLAGLSS---------PGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
1-121 |
2.23e-77 |
|
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: 243.99 E-value: 2.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQ 80
Cdd:cd22225 30 MAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLDQQISEFLLPDLNRIAEHSDPVELGRLLQ 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370453384 81 LILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 121
Cdd:cd22225 110 LILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
1-121 |
1.63e-71 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 228.83 E-value: 1.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQ 80
Cdd:pfam19047 31 MAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLGQQISDFLLPDVNLIGEHSDPAELGRLLQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370453384 81 LILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 121
Cdd:pfam19047 111 LILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
1-119 |
5.71e-69 |
|
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: 221.74 E-value: 5.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQ 80
Cdd:cd22222 29 IAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQQISGFTMPDVNAIAEKEDPKELGRLLQ 108
|
90 100 110
....*....|....*....|....*....|....*....
gi 1370453384 81 LILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 119
Cdd:cd22222 109 LVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
1-120 |
3.22e-57 |
|
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: 190.86 E-value: 3.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQ 80
Cdd:cd22227 31 IAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLGHQVSEDHLPDVNLIGEFSDDTELGKLLQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370453384 81 LILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 120
Cdd:cd22227 111 LVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
1-120 |
1.05e-56 |
|
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: 189.41 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQ 80
Cdd:cd22226 34 MAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHSDAAELGRMLQ 113
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370453384 81 LILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 120
Cdd:cd22226 114 LILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
1-119 |
6.07e-38 |
|
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: 137.79 E-value: 6.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSriKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQ 80
Cdd:cd22211 29 LAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQLSDLPLPDLSAIARDGDEEEIVKLLE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 1370453384 81 LILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 119
Cdd:cd22211 107 LVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
1-117 |
4.59e-17 |
|
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: 78.40 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNESWLSRIKEDVgdNWRIKasNVKKVLQGIMSYYHEFLGQQISEALiPDLNQIteCSDP------VE 74
Cdd:cd22223 32 LNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEVLQQLIVMKL-PDILTI--GREPeseqslEE 104
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370453384 75 LGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 117
Cdd:cd22223 105 LEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-613 |
1.20e-12 |
|
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: 71.64 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 248 DELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnMMYMHNTVSLEEELKKANAART 327
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA--LLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 328 QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRD-TLKETNEELrcsQVQQDHLNQTDASAT 406
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGEL---EAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 407 KSYENLAAEIMPVEyrevfirlqhenkmlrlQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ 486
Cdd:TIGR02169 315 RELEDAEERLAKLE-----------------AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 487 KSLQE--QGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERy 564
Cdd:TIGR02169 378 KEFAEtrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK- 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370453384 565 kmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVA 613
Cdd:TIGR02169 457 ---LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-576 |
4.69e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 229 YRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEIYRQK-----LQDLNDLRKQVKTLQE 303
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNE---LERQLKSLERQAEKAERYKELKAELRELelallVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 304 TNMMYMHNTVSLEEELKKANAartQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLieqRDTLKE 383
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 384 TNEELRCSQVQQDHLNQTDASATKSYENLAAEIMpveyrevfiRLQHENKMLRLQQEGSENeRIEELQEQLEQKHRKMNE 463
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELE---------SLEAELEELEAELEELES-RLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 464 LETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKI 543
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1370453384 544 NELEAALQKKDED----------MKAMEERYKMYLEKARNVIK 576
Cdd:TIGR02168 471 EEAEQALDAAERElaqlqarldsLERLQENLEGFSEGVKALLK 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
275-609 |
1.09e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 275 NKLESTveiyRQKLQDLNDLRKQVKTlqetnmmymhNTVSLEEELKKANAARTqletYKRQVQDLHVKLSSesKRADTLA 354
Cdd:COG1196 179 RKLEAT----EENLERLEDILGELER----------QLEPLERQAEKAERYRE----LKEELKELEAELLL--LKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 355 FEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKM 434
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 435 LRLQQEGSENERIEELQEQLEQkhrKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgSKSEGESSSKLKQKLEAHMEK 514
Cdd:COG1196 316 ERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 515 LTEVHEELQKKQELIEDLQpdinQNVQKINELEAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRK 594
Cdd:COG1196 392 LRAAAELAAQLEELEEAEE----ALLERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLE 463
|
330
....*....|....*
gi 1370453384 595 QLAEKERRIEILESE 609
Cdd:COG1196 464 LLAELLEEAALLEAA 478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
129-609 |
3.80e-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: 66.68 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 129 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVT-------------TLQDEKNSLVSENEMMNE-KLDQLDGSF 194
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrekelSLEKEQNKRLWDRDTGNSiTIDHLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 195 DDPNTVVAkkyfhaqlqleqlqeenfRLEAAKDDYRVHCE-ELEKQLIEFQHRNDELTSLAEETRalkdeidvlratsdk 273
Cdd:pfam15921 422 DDRNMEVQ------------------RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTA--------------- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 274 anKLESTVEIYRQKLQDLNdlrkqvktlqetnmmymhntvsleeelkkanAARTQLETYKRQVQDLHVKLSSESKRADTL 353
Cdd:pfam15921 469 --QLESTKEMLRKVVEELT-------------------------------AKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 354 AFEMKRLEEKHEALLKEKERLieqrdtlKETNEELRCSQVQQDHLNQTDASATKSYEnlaaeimpveyrevFIRLQHENK 433
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHL-------KNEGDHLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENM 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 434 MLRLQQEGSENERIEELQEQLEQ----KHRKMNELETEQRLSKERIRELQQQIEDLQKSlqeqgsksegesssklKQKL- 508
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKeindRRLELQEFKILKDKKDAKIRELEARVSDLELE----------------KVKLv 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 509 EAHMEKLTEVHEELQKKQELIEDLQP---DINQNVQKINELEAALQKKDEDMKAMEERYKMYL-------EKARNVIKTL 578
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVKTsrnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLksaqselEQTRNTLKSM 718
|
490 500 510
....*....|....*....|....*....|.
gi 1370453384 579 DPKLNPASAEIMLLRKQLAEKERRIEILESE 609
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-551 |
4.51e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 235 ELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTVEIYRQKLQDLNDlrkqvktlqetnmmymhntvS 314
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELEELEL--------------------E 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 315 LEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqvq 394
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 395 qdhlnQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQkhrKMNELETEQRLSKER 474
Cdd:COG1196 358 -----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 475 IRELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQ 551
Cdd:COG1196 430 LAELEEEEEEEEEALEEA-----AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
249-609 |
1.53e-10 |
|
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: 64.75 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 249 ELTSLAEETRALKDEIDVLRATSDkaNKLESTVEIYRQKLQDL-NDLRKQVKTLQETNMMYMHNTVSLEEELKK-ANAAR 326
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQ--NKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEIiQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 327 TQLETYKRQVQDLHVKLSSeskradtLAFEMKRLEEKHEALLKEKERlieqrdTLKETNEELRCSQVQQDHLNQTDASAT 406
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQ-------LRSELREAKRMYEDKIEELEK------QLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 407 KSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETeqrLSKERIRELQQQIEDLQ 486
Cdd:pfam15921 377 DQLQKLLADL---HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLKAMKSECQGQMERQM 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 487 KSLQEQGSKSEGESSskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKM 566
Cdd:pfam15921 451 AAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1370453384 567 YLEKARNvIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESE 609
Cdd:pfam15921 529 KLQELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-574 |
2.49e-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: 63.93 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 248 DELTSLAEETRALKDEIDVLRatsDKANKLESTVEIYRQKLQDLNdlrKQVKTLQEtnmmymhntvSLEEELKKANAART 327
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDAS---RKIGEIEK----------EIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 328 QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE---------KERLIEQRDTLKETNEELRCSQVQQDHL 398
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlsHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 399 NQTDASATKSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIREL 478
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 479 QQQIEDLQKSLQEQGSK--SEGESSSKLKQKLEAHMEKLTE--------------------VHEELQKKQELIEDLQP-- 534
Cdd:TIGR02169 895 EAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALEPvn 974
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1370453384 535 -----DINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNV 574
Cdd:TIGR02169 975 mlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-490 |
2.54e-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: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 133 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvakkyfhAQLQL 212
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--------------VEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 213 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEI-YRQKLQDL 291
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 292 NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAA----RTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEAL 367
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 368 LKEKERLIEQRDTLKETNE--ELRCSQVQQDHLNQTDAsATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQE----G 441
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAqlELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1370453384 442 SENER-IEELQEQleqkhrkmneleteqrlsKERIRELQQQIEDLQKSLQ 490
Cdd:TIGR02168 986 PVNLAaIEEYEEL------------------KERYDFLTAQKEDLTEAKE 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
121-599 |
2.63e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 121 EILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDmqvttlqdeknSLVSENEMMNEKLDQLDGSFDDPNTV 200
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAD-----------EVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 201 VAKKyfhaqlqleqlqeenfrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLES 279
Cdd:PRK02224 267 IAET------------------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 280 TVEIYRQKLQDLND----LRKQVKTLQETNMMYMHNTVSLEEELKkanAARTQLETYKRQVQDLHVKLSSESKRADTLAF 355
Cdd:PRK02224 329 RLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 356 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELR--------------CSQVQQDHLNQTDASATKsyenlaaeimpvEY 421
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkCPECGQPVEGSPHVETIE------------ED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 422 REVFIRLQHENKMLRLQQEGSEN--ERIEELQEQLEQKHRKMNELET-EQRLS--KERIRELQQQIEDLQKSLQEqgsks 496
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE----- 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 497 egessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEA----------------ALQKKDEDMKAM 560
Cdd:PRK02224 549 -------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedeieRLREKREALAEL 621
|
490 500 510
....*....|....*....|....*....|....*....
gi 1370453384 561 EERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEK 599
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-609 |
3.40e-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: 63.54 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 361 EEKHEALLK---EKERLIEQRDTLKETNEelrcsqvQQDHLnQTDASATKSYENLAAEIMPVEYREVFIRL-QHENKMLR 436
Cdd:TIGR02168 172 ERRKETERKlerTRENLDRLEDILNELER-------QLKSL-ERQAEKAERYKELKAELRELELALLVLRLeELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 437 LQQEGSENER--------IEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGessskLKQKL 508
Cdd:TIGR02168 244 LQEELKEAEEeleeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN-----LERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 509 EAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMY---LEKARNVIKTLDPKLNPA 585
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASL 398
|
250 260
....*....|....*....|....
gi 1370453384 586 SAEIMLLRKQLAEKERRIEILESE 609
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQE 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-598 |
4.62e-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: 63.15 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 289 QDLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALL 368
Cdd:TIGR02168 677 REIEELEEKIEELEE----------KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 369 -------KEKERLIEQRDTLKETNEELRCS-QVQQDHLNQTDASATKSYENLAAEI-MPVEYREVFIRLQHENKMLRLQQ 439
Cdd:TIGR02168 747 eriaqlsKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALReALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 440 EGSENE------RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSegesssklkQKLEAHME 513
Cdd:TIGR02168 827 ESLERRiaaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---------ALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 514 KL-TEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLL 592
Cdd:TIGR02168 898 ELsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*.
gi 1370453384 593 RKQLAE 598
Cdd:TIGR02168 978 ENKIKE 983
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
3-117 |
8.23e-10 |
|
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: 58.01 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 3 QVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALiPDLNQITEcsDPV------ELG 76
Cdd:cd22228 38 KIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEVLQQLIVMNL-PNVLMIGK--DPLsgksmeEIK 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370453384 77 RLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 117
Cdd:cd22228 111 KMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-562 |
8.33e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 221 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV-LRATSDKANKLESTVEIYRQKLQDLNDLRKQV- 298
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSKELTELe 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 299 KTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQR 378
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 379 DTLKETNEELRCSQvqqdhlnqtdASATKSYENLAAEImpveyREVFIRLQHEnkmlrLQQEGSENERIEELQEQLEQKH 458
Cdd:TIGR02168 841 EDLEEQIEELSEDI----------ESLAAEIEELEELI-----EELESELEAL-----LNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 459 RKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHE-ELQKKQELIEDLQPDIN 537
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG------------LEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEE 968
|
330 340
....*....|....*....|....*.
gi 1370453384 538 QNVQKINELEAALQKKDE-DMKAMEE 562
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPvNLAAIEE 994
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-621 |
1.06e-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: 62.01 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 368 LKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMpveyrevfiRLQHENKMLrLQQEGSENERI 447
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---------EIEKEIEQL-EQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 448 EELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSsklkQKLEAHMEKLTEVHEE------ 521
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI----PEIQAELSKLEEEVSRiearlr 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 522 -----LQKKQELIEDLQPDINQNVQKINELE---AALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLR 593
Cdd:TIGR02169 816 eieqkLNRLTLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260
....*....|....*....|....*...
gi 1370453384 594 KQLAEKERRIEILESECKVAKFRDYEEK 621
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
372-608 |
2.01e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 372 ERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKsYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgseneRIEELQ 451
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 452 EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIED 531
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-----------LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 532 LQPDINQNVQKINELEAALQKKDEDMKAMEERykmylekarnviktLDPKLNPASAEIMLLRKQLAEKERRIEILES 608
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-609 |
4.04e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 130 AVGELEQQLKRALEELQEALAEKEElrqrcEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKkyfHAQ 209
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE---HEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 210 LQLEQLqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEIYRQKLQ 289
Cdd:PRK02224 249 RREELE-----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 290 D--------LNDLRKQVKTLQETNMMYMHNTVSLEEELKKA-----------NAARTQLETYKRQVQDLHVKLSSESKRA 350
Cdd:PRK02224 321 DrdeelrdrLEECRVAAQAHNEEAESLREDADDLEERAEELreeaaeleselEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 351 DTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELR--------------CSQVQQDHLNQTDASATKsyenlaaei 416
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkCPECGQPVEGSPHVETIE--------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 417 mpvEYREVFIRLQHENKMLRLQQEGSEN--ERIEELQEQLEQKHRKMNELET-EQRLS--KERIRELQQQIEDLQKSLQE 491
Cdd:PRK02224 472 ---EDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 492 qgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEaalqkKDEDMKAMEERYKMYLEKA 571
Cdd:PRK02224 549 ------------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-----RIRTLLAAIADAEDEIERL 611
|
490 500 510
....*....|....*....|....*....|....*...
gi 1370453384 572 RNVIKTLDPKLNpasaeimLLRKQLAEKERRIEILESE 609
Cdd:PRK02224 612 REKREALAELND-------ERRERLAEKRERKRELEAE 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-490 |
5.17e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 131 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfddPNTVVAKKYFHAQL 210
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------EGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 211 QLEQLQEENFRLEAAKDDYRVHCEELEKQLIEfqhRNDELTSLAEETRALKDE--IDVLRATSDKANKLESTVEIYRQKL 288
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 289 QDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLET----YKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 364
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 365 EALLKEKERLIEQRDTLKETNEELRcSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSEN 444
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370453384 445 --ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQ 490
Cdd:TIGR02169 474 lkEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
438-623 |
8.05e-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: 58.24 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 438 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLK------------ 505
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplallls 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 506 -----------QKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNV 574
Cdd:COG4942 128 pedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1370453384 575 IKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKLI 623
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
314-607 |
1.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 314 SLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEElrcsqv 393
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK------ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 394 qqdhlNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSkE 473
Cdd:PRK03918 292 -----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-E 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 474 RIRELQQQIEDLQKSLQEqgsksegESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQK- 552
Cdd:PRK03918 366 EAKAKKEELERLKKRLTG-------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKc 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453384 553 -------KDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILE 607
Cdd:PRK03918 439 pvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-622 |
1.15e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 132 GELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVvAKKYFHAQLQ 211
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 212 LEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKlqdL 291
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE---I 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 292 NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKR------QVQDLHVKLSSESKraDTLAFEMKRLEEKHE 365
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEakakkeELERLKKRLTGLTP--EKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 366 ALLKEKERLIEQRDTLKETNEELRCS----------------QVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ 429
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 430 HEN--KMLRLQQEGSENERIEELQEQLEQKHRKMN--ELE---TEQRLSKERIRELQQQIEDLQKSLQEqgsksegesSS 502
Cdd:PRK03918 482 LREleKVLKKESELIKLKELAEQLKELEEKLKKYNleELEkkaEEYEKLKEKLIKLKGEIKSLKKELEK---------LE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 503 KLKQKLEAHMEKLTEVHEELQK-KQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEErykmyLEKARNVIKTLDPK 581
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE-----LEREEKELKKLEEE 627
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1370453384 582 LNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKL 622
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-620 |
1.47e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 221 RLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKT 300
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 301 LQETNMMyMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDT 380
Cdd:PTZ00121 1304 ADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 381 LKETNEELRCS----------QVQQDHLNQTDASATKSYE--NLAAEIMPVEyrEVFIRLQHENKMLRLQQEGSENERIE 448
Cdd:PTZ00121 1383 AKKKAEEKKKAdeakkkaeedKKKADELKKAAAAKKKADEakKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 449 ELQEQLEQKhRKMNELETEQRlSKERIRELQQQIEDLQKSLQE-QGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQE 527
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAE-EAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 528 LIEDLQPDINQNVQKINELEAALQ-KKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEil 606
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-- 1616
|
410
....*....|....
gi 1370453384 607 ESECKVAKFRDYEE 620
Cdd:PTZ00121 1617 EAKIKAEELKKAEE 1630
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
91-608 |
1.50e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 91 KKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQ 170
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 171 DEKNSLVSENEMMNEKLDQLDGSFDDpntvvAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDEL 250
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 251 TSLAEETRALKDEIDVLRatsdkanKLESTVEIYRQKLQDLNDLRKQVKTLqetnmmymhNTVSLEEELKKANAARTQLE 330
Cdd:PRK03918 341 EELKKKLKELEKRLEELE-------ERHELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 331 TYKRQVQDLHVKLSSESKRADTLAFEMKR-----------LEEKHEALLKEK--ERLIEQRDTLKETNEELRCSQVQQDH 397
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 398 LNQTDASATK--SYENLAAEIMPVEYR-EVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKER 474
Cdd:PRK03918 485 LEKVLKKESEliKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 475 IRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHME--KLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQK 552
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453384 553 KDEDMKAMEERYKMylEKARNViktldpklnpaSAEIMLLRKQLAEKERRIEILES 608
Cdd:PRK03918 645 LRKELEELEKKYSE--EEYEEL-----------REEYLELSRELAGLRAELEELEK 687
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-607 |
1.58e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 134 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDpntvVAKKYFHAQLQLE 213
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----AEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 214 QLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELtsLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLND 293
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 294 LRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQD-----LHVKLSSESKRADTLAFEMKRLEEKHEALL 368
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 369 KEKERLIEQRDTLKETNEELRCSQVQQDH---------LNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQ 439
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 440 EGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVH 519
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 520 EELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKArnviktLDPKLNPASAEImlLRKQLAEK 599
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA------LEELPEPPDLEE--LERELERL 772
|
....*...
gi 1370453384 600 ERRIEILE 607
Cdd:COG1196 773 EREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-620 |
2.96e-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: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 133 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpntvvakkyfHAQLQL 212
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 213 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEIYRQKLQD 290
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 291 LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 370
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 371 KERLIEQRDTLKETNEELRCS-QVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENK---------MLRLQQE 440
Cdd:COG1196 472 AALLEAALAELLEELAEAAARlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeaaleaalAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 441 GSENERIEELQEQLEQKHRK-------MNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKL--------- 504
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvaar 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 505 KQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNP 584
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510
....*....|....*....|....*....|....*.
gi 1370453384 585 ASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEE 620
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-487 |
6.00e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 128 NDAVGELEQQLKRAleELQEALAEK-EELRQRCEELDMQVTTLQdeknslvsenemMNEKLDQLDgsfddpntvvakkyf 206
Cdd:TIGR02168 192 EDILNELERQLKSL--ERQAEKAERyKELKAELRELELALLVLR------------LEELREELE--------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 207 haqlqleqlqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID-VLRATSDKANKLESTVEIYR 285
Cdd:TIGR02168 243 --------------ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 286 QKLQDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMK-RLEEKH 364
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEE----------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 365 EALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSE- 443
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELEr 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1370453384 444 -NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQK 487
Cdd:TIGR02168 459 lEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-614 |
6.59e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 132 GELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDpnTVVAKKYFHAQLQ 211
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 212 LEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDL 291
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 292 NDLRKQVKTLQETNMMYMH---NTVSLEEELKKA----------NAARTQLETYKRQVQDLhvkLSSESKRADTLA---F 355
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGvlsELISVDEGYEAAieaalggrlqAVVVENLNAAKKAIAFL---KQNELGRVTFLPldsI 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 356 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsQVQQDHLNQTdaSATKSYENLAAEIMPVEYREVFIRLQHE---- 431
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR--KALSYLLGGV--LVVDDLDNALELAKKLRPGYRIVTLDGDlvrp 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 432 ------------NKMLRLQQEGSENE-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgskseG 498
Cdd:TIGR02168 658 ggvitggsaktnSSILERRREIEELEeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-----R 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 499 ESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMY---LEKARNVI 575
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAEL 812
|
490 500 510
....*....|....*....|....*....|....*....
gi 1370453384 576 KTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAK 614
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-483 |
7.69e-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: 55.83 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 137 QLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfhaqlqLEQLQ 216
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 217 EENFRLEAAKDDYrvhcEELEKQLIEFQHRNDEltsLAEETRALKDEIDVLRAtsdkanklestveiyrqklqDLNDLRK 296
Cdd:TIGR02168 306 ILRERLANLERQL----EELEAQLEELESKLDE---LAEELAELEEKLEELKE--------------------ELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 297 QVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIE 376
Cdd:TIGR02168 359 ELEELEAE----------LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 377 QRDTLketneELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQ 456
Cdd:TIGR02168 429 KLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340
....*....|....*....|....*..
gi 1370453384 457 KHRKMNELETEQRLSKERIRELQQQIE 483
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-579 |
9.30e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 90 EKKQEHIQNIMTLEESVQHVVMTAIQELMSKEILssppNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTL 169
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 170 QDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDE 249
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 250 LTSLAEETRALKDEIDVLRATS-DKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKAN----- 323
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrgla 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 324 -----------AARTQLETYK-RQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETN------ 385
Cdd:COG1196 524 gavavligveaAYEAALEAALaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdl 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 386 -------EELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHEN--KMLRLQQEGSENERIEELQEQLEQ 456
Cdd:COG1196 604 vasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSagGSLTGGSRRELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 457 KHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEvHEELQKKQELIEDLQPDI 536
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE-EELLEEEALEELPEPPDL 762
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 537 NQNVQKINELEAALQKK-------DEDMKAMEERYKMY------LEKARN----VIKTLD 579
Cdd:COG1196 763 EELERELERLEREIEALgpvnllaIEEYEELEERYDFLseqredLEEAREtleeAIEEID 822
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
220-622 |
1.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 220 FRLEAAKDDYRVHCEELEKQLIEFQHRNDELT------SLAEETRALKDEIDVLratSDKANKLESTVEIYRQKLQDLND 293
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAEL---PERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 294 LRKQVKTLQEtnmmymhntvSLEEELKK-ANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE 372
Cdd:COG4717 168 LEAELAELQE----------ELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 373 RLiEQRDTLKETNEELR--CSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEEL 450
Cdd:COG4717 238 AA-ALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 451 QEQLEQKHRKmnELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKL-TEVHEELQKKQELI 529
Cdd:COG4717 317 EEEELEELLA--ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 530 EDLQpdinQNVQKINELEAALQKKDEDMKAMEERYKmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESE 609
Cdd:COG4717 395 EEYQ----ELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410
....*....|...
gi 1370453384 610 CKVAKFRDYEEKL 622
Cdd:COG4717 469 GELAELLQELEEL 481
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-623 |
2.94e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 139 KRALEEL----QEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfDDPNTVVAKKYFHAQLQLEQ 214
Cdd:PTZ00121 1314 AKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 215 LQEENFRLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRAlKDEIDVLRATSDKANKLESTVEiYRQKLQDLNDL 294
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 295 RKQVKTLQETNmmymhntvSLEEELKKANAARTQLETYKRQVQDLHvKLSSESKRADTL--------AFEMKRLEEKHEA 366
Cdd:PTZ00121 1466 AEEAKKADEAK--------KKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAkkaeeakkADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 367 LLKEKERLIEQRDTLKETnEELRCSQ----VQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGS 442
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKA-EELKKAEekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 443 ENERI--EELQEQLEQKH-------------RKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQK 507
Cdd:PTZ00121 1616 EEAKIkaEELKKAEEEKKkveqlkkkeaeekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 508 LEAH----MEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKmyleKARNVIKTLDPKLN 583
Cdd:PTZ00121 1696 KEAEeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAE 1771
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1370453384 584 PASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKLI 623
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
1-117 |
4.34e-07 |
|
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: 50.17 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 1 MAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALiPDL-----NQITEcSDPVEL 75
Cdd:cd22229 39 LNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQETLQQLIMMSL-PNVlvlgrNPLSE-QGTEEM 112
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370453384 76 GRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 117
Cdd:cd22229 113 KKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
445-609 |
4.90e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 445 ERIEELQEQL---EQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 521
Cdd:COG4717 71 KELKELEEELkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 522 LQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERykmYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKER 601
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
....*...
gi 1370453384 602 RIEILESE 609
Cdd:COG4717 228 ELEQLENE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
135-623 |
5.27e-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: 53.15 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 135 EQQLKRA--LEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQL 212
Cdd:TIGR02169 347 EERKRRDklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 213 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLN 292
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 293 DLRKQVKTLQETNMMYMHNTVS------------LE----------------------EELKKANAAR-TQLETYKRQVQ 337
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAqlgsvgeryataIEvaagnrlnnvvveddavakeaiELLKRRKAGRaTFLPLNKMRDE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 338 DLHVKLSSESKRADtLAFEMKRLEEKHEALLKEKER---LIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAA 414
Cdd:TIGR02169 587 RRDLSILSEDGVIG-FAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 415 EIMPVEYREVFIRLQHENKML-----RLQQEGSENE-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKS 488
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLkrelsSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 489 LQ--EQGSKSEGESSSKLKQKLEAHMEKLTEV------------HEELQKKQELIEDLQPDINQNVQKINELEAALQKKD 554
Cdd:TIGR02169 746 LSslEQEIENVKSELKELEARIEELEEDLHKLeealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370453384 555 EDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILEseckvAKFRDYEEKLI 623
Cdd:TIGR02169 826 LEKEYLEKE----IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE-----AALRDLESRLG 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-388 |
8.23e-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: 52.75 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 128 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFH 207
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 208 AQLQLEQLQEENFRLEAAK----------DDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATsdkANKL 277
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALL---NERASLEEALALLRSELEELSEE---LREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 278 ESTVEIYRQKLQDLNDLRKQVKT-LQETNMMYMHNT--------VSLEEELKKANAARTQLETYKRQVQDLHVKLsSESK 348
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELrLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKI-KELG 985
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370453384 349 RADTLAF-EMKRLEEKHEALLKEKERLIEQRDTLKETNEEL 388
Cdd:TIGR02168 986 PVNLAAIeEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
35-117 |
1.23e-06 |
|
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: 49.06 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 35 NVKKVLQGIMSYYHEFLGQQISEALiPDL-----NQITECSdPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHV 109
Cdd:cd22230 83 NLHILWGRLRDFYQEELQQLILSPP-PDLqvmgrDPFTEEA-VQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAE 160
|
....*...
gi 1370453384 110 VMTAIQEL 117
Cdd:cd22230 161 LAEAIQEV 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-578 |
1.61e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 136 QQLKRALEELQEALA----EKEELRQRCEELDMQVTTLQDEKNSLVSE-------NEMMNEKLDQLDGSFDDPNTVVAKK 204
Cdd:PRK02224 254 ETLEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEEC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 205 YFHAQLQLEQLQEENFR---LEAAKDDYRVHCEELEKqliEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTV 281
Cdd:PRK02224 334 RVAAQAHNEEAESLREDaddLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 282 EIYRQKLQ-DLNDLRKQVKTLqETNMMYMHNTVSLEEELKKA-------------------NAARTQLETYKRQVQDLHV 341
Cdd:PRK02224 411 EDFLEELReERDELREREAEL-EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 342 KLSSESKRADTL------AFEMKRLEEKHEALlkeKERLIEQRDTLKETNEELRCSQVQQDHLNqtDASATKSYENLAAE 415
Cdd:PRK02224 490 EVEEVEERLERAedlveaEDRIERLEERREDL---EELIAERRETIEEKRERAEELRERAAELE--AEAEEKREAAAEAE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 416 IMPVEYREVFIRLqhENKMLRLQQEGSENERIEELQ-------EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKS 488
Cdd:PRK02224 565 EEAEEAREEVAEL--NSKLAELKERIESLERIRTLLaaiadaeDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 489 LQEqgsksegESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAAlqkkDEDMKAMEERyKMYL 568
Cdd:PRK02224 643 FDE-------ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL----RERREALENR-VEAL 710
|
490
....*....|
gi 1370453384 569 EKARNVIKTL 578
Cdd:PRK02224 711 EALYDEAEEL 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
202-528 |
2.00e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 202 AKKYFHAQLQLEqlqeenfRLEAAKDDYRVHCEELEKQLiefQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTV 281
Cdd:COG1196 231 LLKLRELEAELE-------ELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQA---EEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 282 EIYRQKLQDLNDLRKQvktlqetnmmymhNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAfemKRLE 361
Cdd:COG1196 298 ARLEQDIARLEERRRE-------------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 362 EKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEG 441
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---------ERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 442 SENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 521
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
....*..
gi 1370453384 522 LQKKQEL 528
Cdd:COG1196 513 ALLLAGL 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
340-621 |
2.92e-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: 50.51 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 340 HVKLSSESKRADTLA-FEMKRLEEKHEALLKEKERlieqRDTLKETNEELRCSQVQQdhlnqtdASATKSYENLAAEIMP 418
Cdd:pfam17380 280 HQKAVSERQQQEKFEkMEQERLRQEKEEKAREVER----RRKLEEAEKARQAEMDRQ-------AAIYAEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 419 VEYREVFIRLQHENKMLRLQQEGSENERIEELQ----EQLEQKHRKMNELETEQR---LSKERIRELQQQIEDLQKSLQE 491
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRELErlqmERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 492 QGSKSEGESSSkLKQKLEAHMEKlteVHEELQKKQELIEDLQPDINQNVQKINELEaalqKKDEDMKAMEERYKMYLEKa 571
Cdd:pfam17380 429 QEEARQREVRR-LEEERAREMER---VRLEEQERQQQVERLRQQEEERKRKKLELE----KEKRDRKRAEEQRRKILEK- 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1370453384 572 rnviktldpklnpasaEIMLLRKQLAEKERRIEILESECKVAKFRDYEEK 621
Cdd:pfam17380 500 ----------------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-567 |
3.61e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 133 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSL---VSENEMMNEKLDQLDG--SFDDPNTV--VAKKY 205
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKKEELERlkKRLTGLTPekLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 206 FHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQ----------------HRNDELTSLAEETRALKDEIDVLRA 269
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 270 TSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAArtQLETYKRQVQDLHVKLSSESKR 349
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQLKE-----------LEEKLKKYNLE--ELEKKAEEYEKLKEKLIKLKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 350 ADTLAFEMKRLEEkheaLLKEKERLIEQRDTLKETNEELrcsqvqqdhLNQTDASATKSYENLAAEIMPVE--YREvFIR 427
Cdd:PRK03918 541 IKSLKKELEKLEE----LKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELEERLKELEpfYNE-YLE 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 428 LQHENKMLRlqqegSENERIEELQEQLEQKHRKMNELETeqrlskeRIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQK 507
Cdd:PRK03918 607 LKDAEKELE-----REEKELKKLEEELDKAFEELAETEK-------RLEELRKELEELEKKYSEEEYEELREEYLELSRE 674
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 508 LEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEaALQKKDEDMKAMEERYKMY 567
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKY 733
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-621 |
4.54e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 136 QQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQL 215
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 216 QEENFRLEAAK---DDYRVHCEELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRqKLQDLN 292
Cdd:PTZ00121 1360 EAAEEKAEAAEkkkEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 293 DLRKQVKTLQETNmmymhntvSLEEELKKANAARTQLETyKRQVQDLHVKlSSESKRADTLAFEMKRLEEKHEALlKEKE 372
Cdd:PTZ00121 1438 KKAEEAKKADEAK--------KKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA-KKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 373 RLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEimpveyrevfirlqhENKMLRLQQEGSENERIEELQE 452
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD---------------ELKKAEELKKAEEKKKAEEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 453 QLEQKHRKMNELETEQRLSKERIREL--------QQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTE---VHEE 521
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVmklyeeekKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkKAEE 1651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 522 LQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKtldpklnpasaeimlLRKQLAEKER 601
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE---------------LKKKEAEEKK 1716
|
490 500
....*....|....*....|
gi 1370453384 602 RIEILESECKVAKFRDYEEK 621
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAK 1736
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
231-491 |
4.89e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 231 VHCEELEKQLIEFQHRndELTSLAEEtraLKDEIDVLRATSDKANKLESTVEiyRQKLQDLNDLRKQVKTlqetnmmymh 310
Cdd:PRK05771 31 VHIEDLKEELSNERLR--KLRSLLTK---LSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEE---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 311 NTVSLEEELKKANAARTQLETYKRqvqdlhvKLSSESKRADTL-AFEMKrleekhEALLKEKERLIEQRDTLKETNEELR 389
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIK-------ELEQEIERLEPWgNFDLD------LSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 390 CSQVQQDhlNQTDASATKSYENLAAeIMPVEYREVFIRL--QHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELete 467
Cdd:PRK05771 161 KLESDVE--NVEYISTDKGYVYVVV-VVLKELSDEVEEElkKLGFERLELEEEGTPSELIREIKEELEEIEKERESL--- 234
|
250 260
....*....|....*....|....
gi 1370453384 468 qrlsKERIRELQQQIEDLQKSLQE 491
Cdd:PRK05771 235 ----LEELKELAKKYLEELLALYE 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
438-661 |
4.99e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 438 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEA-HMEKLT 516
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVsYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 517 EVH--EELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRK 594
Cdd:COG3883 110 GSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 595 QLAEKERRIEILESECKVAKFRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGGGACSDTGACTPARS 661
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-611 |
9.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 407 KSYENLAAEIMPVEYREvfirlqhENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ 486
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRI-------ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 487 KSLQEqgSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdinQNVQKINELEaalqKKDEDMKAMEERYKM 566
Cdd:PRK03918 235 ELKEE--IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----EKVKELKELK----EKAEEYIKLSEFYEE 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370453384 567 YLEKARNVIKTLDpKLNPASAEIMLLRKQLAEKERRIEILESECK 611
Cdd:PRK03918 305 YLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
129-620 |
9.93e-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: 48.95 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 129 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQL----DGSFDDPNTVVAKK 204
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAH 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 205 YFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIY 284
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 285 RQKLQDLNDLRKQVKTLQETNMMYMHNtvsLEEELkkaNAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLeekh 364
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHD---LEIQL---TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL---- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 365 eallkekerLIEQRDTLKETNEELRCSQVQQDHLNqtdaSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSEN 444
Cdd:pfam05483 498 ---------LLENKELTQEASDMTLELKKHQEDII----NCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 445 E-RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQ 523
Cdd:pfam05483 565 KcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE------------LHQENKALKKKGSAENKQLN 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 524 KKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVI-------KTLDPKLNPASAEIM-LLRKQ 595
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAdeavklqKEIDKRCQHKIAEMVaLMEKH 712
|
490 500
....*....|....*....|....*
gi 1370453384 596 LAEKERRIEILESECKVAKFRDYEE 620
Cdd:pfam05483 713 KHQYDKIIEERDSELGLYKNKEQEQ 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
250-627 |
1.02e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 250 LTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVS----LEEELKKANAA 325
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkaLEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 326 RTQL-ETYKRQVQDLHVKLSSES-----------KRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQV 393
Cdd:pfam05483 326 ICQLtEEKEAQMEELNKAKAAHSfvvtefeattcSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 394 QQDHL------NQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQ--------QEGSENERIEELQEQLEQKHR 459
Cdd:pfam05483 406 ELEELkkilaeDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktSEEHYLKEVEDLKTELEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 460 KMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGEsssklkQKLEAHMEKLTEVHEElqKKQELIEDLQPDINQN 539
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC------KKQEERMLKQIENLEE--KEMNLRDELESVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 540 VQKINELEAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKLNPasaeimlLRKQLAEKERRIEILESECKVAKFRDYE 619
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYE----VLKKEKQMKILENKCNN-------LKKQIENKNKNIEELHQENKALKKKGSA 626
|
....*...
gi 1370453384 620 EKLIVSAW 627
Cdd:pfam05483 627 ENKQLNAY 634
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-611 |
1.10e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 248 DELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQK----LQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKA- 322
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTq 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 323 ---NAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERlieqrDTLKETNEELRCsqvQQDHLN 399
Cdd:TIGR04523 253 tqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ-----DWNKELKSELKN---QEKKLE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 400 QTDASATKSYENLAaeimpveyrevfiRLQHENKMLRLQQEGSENERiEELQEQLEQKHRKMNELETEQRLSKERIRELQ 479
Cdd:TIGR04523 325 EIQNQISQNNKIIS-------------QLNEQISQLKKELTNSESEN-SEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 480 QQIEDLQKSLQEQgsksegessSKLKQKLEahmEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEaalqKKDEDMKA 559
Cdd:TIGR04523 391 SQINDLESKIQNQ---------EKLNQQKD---EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT----NQDSVKEL 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1370453384 560 MEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECK 611
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-553 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 361 EEKHEALLKEKERLIEQRDTLKETNEELrcsQVQQDHLNQtdasatksyeNLAAEIMPVEYREVFIRL-QHENKMLRLQQ 439
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL---EAELDALQE----------RREALQRLAEYSWDEIDVaSAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 440 E----GSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ---KSLQEQGSKSEGESSSKLKQKLEAHm 512
Cdd:COG4913 676 ElerlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEER- 754
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370453384 513 eklteVHEELQKK--QELIEDLQPDINQNVQKINELEAALQKK 553
Cdd:COG4913 755 -----FAAALGDAveRELRENLEERIDALRARLNRAEEELERA 792
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
434-558 |
1.40e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.54 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 434 MLRLQQEgSENERIEELQEQLEQKHRKMNELETEQRL-SKERIRELQQQIEDLQKSLQEqgsksegesssklkqkLEAHM 512
Cdd:COG0542 401 RVRMEID-SKPEELDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEA----------------LKARW 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1370453384 513 EKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMK 558
Cdd:COG0542 464 EAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
378-623 |
1.68e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 378 RDTLKETNEELRCSQVQQDHLNQTdasaTKSYENLAAEimpveyrevfirlqhenkmlrlqQEGSENERIEELQEQLEQK 457
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQ----IKTYNKNIEE-----------------------QRKKNGENIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 458 HRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegesSSKLKQKLEAHMEKLTEVHEELQKKQEL------IED 531
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK---------LNTAAAKIKSKIEQFQKVIKMYEKGGVCptctqqISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 532 LQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEkARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECK 611
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*..
gi 1370453384 612 -----VAKFRDYEEKLI 623
Cdd:PHA02562 376 dnaeeLAKLQDELDKIV 392
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-481 |
1.72e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 128 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLdgsfddpntvvAKKYFH 207
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-----------EEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 208 AQLQLEQLQEENFRLEAAKDDYRVHCEELEKQL--IEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYR 285
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 286 QKLQDLndlrkqVKTLQETNMMYMHNTVSLEEELKKANaarTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHE 365
Cdd:TIGR02169 829 EYLEKE------IQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 366 ALLKEKERLIEQRDTLKETNEELRCS-QVQQDHLNQTDA---------SATKSYENLAAEIMPVEYRevfIRLQHENKML 435
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKlEALEEELSEIEDpkgedeeipEEELSLEDVQAELQRVEEE---IRALEPVNML 976
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370453384 436 RLQQEGSENERIEELQEQLEQkhrkmneLETEQRLSKERIRELQQQ 481
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAK-------LEEERKAILERIEEYEKK 1015
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
221-492 |
2.09e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 221 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETraLKDEIDVLRATSDKANKLESTVeiyRQKLQDLNDLRKQVKT 300
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAKRFV---QQHGNALAQLEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 301 LQETNMMYmhntvsleEELKKA-NAARTQLETYKRQVQDLhvklSSESKRADTLAFE--MKRLEEKHEALLKEKERLIEQ 377
Cdd:PRK04863 930 LQSDPEQF--------EQLKQDyQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEdaAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 378 RDTLKETNEELRCSQVQQDHLNQTDASATKSYENlaaeimpveYREVFIRLQHENKMLRLQQEGSENERI----EELQEQ 453
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA---------KRQMLQELKQELQDLGVPADSGAEERArarrDELHAR 1068
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370453384 454 LEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 492
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-572 |
2.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 248 DELTSLAEETRALKDEI------DVLRATSDKANKLESTVEIYRQKLQDLNDLRK--QVKTLQETNMMymhnTVSLEEEL 319
Cdd:COG3206 71 SGLSSLSASDSPLETQIeilksrPVLERVVDKLNLDEDPLGEEASREAAIERLRKnlTVEPVKGSNVI----EISYTSPD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 320 KK--ANAARTQLETYKRQVQDLhvKLSSESKRADTLAFEMKRLEEKhealLKEKERLIEQrdtLKETNEELRcSQVQQDH 397
Cdd:COG3206 147 PElaAAVANALAEAYLEQNLEL--RREEARKALEFLEEQLPELRKE----LEEAEAALEE---FRQKNGLVD-LSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 398 LNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQqEGSENERIEELQEQLEQKHRKMNELEteQRLSKE--RI 475
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAELEAELAELS--ARYTPNhpDV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 476 RELQQQIEDLQKSLQEQGSKsegessskLKQKLEAHMEKLTEVHEELQKKQEliedlqpDINQNVQKINELEAALQKKDE 555
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQR--------ILASLEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLER 358
|
330
....*....|....*..
gi 1370453384 556 DMKAMEERYKMYLEKAR 572
Cdd:COG3206 359 EVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-549 |
2.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 363 KHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEImpveyREVFIRLQHENKMLRLQQEGS 442
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-----EKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 443 ENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgsksEGESSSKLKQKLEAHMEKLTEVHEEL 522
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA----TEEELQDLAEELEELQQRLAELEEEL 215
|
170 180
....*....|....*....|....*..
gi 1370453384 523 QKKQELIEDLQPDINQNVQKINELEAA 549
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-558 |
2.82e-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: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 268 RATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSes 347
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERYAAARERLAELEYLRAALRLWFAQ-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 348 KRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKEtneelrcsqvqqdhlnqtdasatksyenlaaeimpvEYREvfir 427
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALRE------------------------------------ELDE---- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 428 lqhenkmLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgSKSEGESSSKLKQK 507
Cdd:COG4913 328 -------LEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL-RAEAAALLEALEEE 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453384 508 LEAHMEKLTEVHEELQKKQELIEDLQPDIN----------QNVQKI-NELEAALQKKDEDMK 558
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIAslerrksnipARLLALrDALAEALGLDEAELP 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-609 |
2.88e-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: 47.07 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 442 SENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEE 521
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA------------LARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 522 LQKKQELIEDLQPDINQNVQKINELEAALQK-----------KDEDMKAMEERYkMYLEKARNVIKTLDPKLNPASAEIM 590
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELA 163
|
170
....*....|....*....
gi 1370453384 591 LLRKQLAEKERRIEILESE 609
Cdd:COG4942 164 ALRAELEAERAELEALLAE 182
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-567 |
3.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 136 QQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvVAKKYFHAQLQLEQL 215
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP---------LYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 216 QEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIdvLRATSDKANKLESTVEIYRQKLQD----L 291
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEaqeeL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 292 NDLRKQVKTLQETNMMY-MHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 370
Cdd:COG4717 223 EELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 371 KERLIEQRDTLKETNEELRCSQVQQDHLNQTDAsaTKSYENLAAEImpVEYREVFIRLQHENKmlRLQQEGSENERIEEL 450
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLS--PEELLELLDRI--EELQELLREAEELEE--ELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 451 Q-------EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQ 523
Cdd:COG4717 377 AeagvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1370453384 524 KKQELIEDLQPDinqnvQKINELEAALQKKDEDMKAMEERYKMY 567
Cdd:COG4717 457 ELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAAL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-527 |
4.19e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 285 RQKLQDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 364
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 365 EALlkeKERLIEQRDTLKETNeelrcsQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHEnkmlRLQQEGSEN 444
Cdd:COG4942 93 AEL---RAELEAQKEELAELL------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE----QAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 445 ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESssklkQKLEAHMEKLTEVHEELQK 524
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIARLEA 234
|
...
gi 1370453384 525 KQE 527
Cdd:COG4942 235 EAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-491 |
6.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 135 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLvsenemmnEKLDQLDGSFDDpntvvakkyfhaqlqleq 214
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEID------------------ 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 215 lqeenfrleaakddyrvhceelekqliefqhrndeLTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDL 294
Cdd:COG4913 663 -----------------------------------VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 295 RKQvktlqetnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE-KER 373
Cdd:COG4913 708 LDE-----------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElREN 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 374 LIEQRDTLKETNEELRcsqvqqDHLNQTDASATKSYENLAAEIMPV-----EYREVFIRLQ------HENKMLRLQQEgS 442
Cdd:COG4913 771 LEERIDALRARLNRAE------EELERAMRAFNREWPAETADLDADleslpEYLALLDRLEedglpeYEERFKELLNE-N 843
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370453384 443 ENERIEELQEQLEQKhrkmneleteqrlskerIRELQQQIEDLQKSLQE 491
Cdd:COG4913 844 SIEFVADLLSKLRRA-----------------IREIKERIDPLNDSLKR 875
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
312-573 |
8.54e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 312 TVSLEEELKKANAARTQLETYKR-------QVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKET 384
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEkrdelneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 385 NEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYRevfirlqHENKMLRLQQEGSENERIEELQEQLE------QKH 458
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-------QQTEVLSPEEEKELVEKIKELEKELEkakkalEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 459 RKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQ 538
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQE-----LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1370453384 539 NVQKINELEAALQ---------KKDEDMKAMEERYKMYLEKARN 573
Cdd:COG1340 235 LQKELRELRKELKklrkkqralKREKEKEELEEKAEEIFEKLKK 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
445-609 |
8.80e-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: 45.53 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 445 ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQK 524
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-----EQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 525 KQELIEDLQPDInQNVQKINELEAALQKKD-EDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRI 603
Cdd:COG4942 102 QKEELAELLRAL-YRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
....*.
gi 1370453384 604 EILESE 609
Cdd:COG4942 181 AELEEE 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
445-622 |
1.48e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 445 ERIEELQEQLEqkhRKMNELETeQRLSKERIRELQQQIEDLQKSL-------QEQGSKSEGESSSKLKQKLEAHMEKLTE 517
Cdd:TIGR02168 189 DRLEDILNELE---RQLKSLER-QAEKAERYKELKAELRELELALlvlrleeLREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 518 VHEEL-------QKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMY----------LEKARNVIKTLDP 580
Cdd:TIGR02168 265 LEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELeaqleeleskLDELAEELAELEE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370453384 581 KLNPASAEIMLLRKQLAEKERRIEILESeckvaKFRDYEEKL 622
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELES-----RLEELEEQL 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
350-586 |
1.85e-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: 44.37 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 350 ADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ 429
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 430 HEN------KMLRLQQEGSENERIEELQEQleqkhRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegesSSK 503
Cdd:COG4942 99 LEAqkeelaELLRALYRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAE---------LAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 504 LKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLN 583
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 1370453384 584 PAS 586
Cdd:COG4942 245 AAG 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
315-510 |
1.94e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 315 LEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE----KERLIEQRDTLKEtneelRC 390
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGE-----RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 391 SQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRlqHENKMLRLQQEgsENERIEELQEQLEQKHRKMNELETEQRL 470
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIAD--ADADLLEELKA--DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1370453384 471 SKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEA 510
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
238-609 |
2.42e-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: 44.56 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 238 KQLIEFQHR----NDELTSLAEETRALKDEidvLRATSDKANKLESTV------EIYRQKLQDLN-DLRKQVKTLQETNM 306
Cdd:COG3096 299 RQLAEEQYRlvemARELEELSARESDLEQD---YQAASDHLNLVQTALrqqekiERYQEDLEELTeRLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 307 MYMHNTVSLEEELKKANAARTQLETYKRQVQDLHvklssesKRADTLAFEMKRLEEKhEALLKE--------KERLIEQR 378
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQ-------TRAIQYQQAVQALEKA-RALCGLpdltpenaEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 379 DTLKETNEELRcsqVQQDHLNQTDASAT---KSYENLAAEIMPVEYREVFirlQHENKMLRlqqEGSENERIEELQEQLE 455
Cdd:COG3096 448 AKEQQATEEVL---ELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAW---QTARELLR---RYRSQQALAQRLQQLR 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 456 QKHRkmnelETEQRLskERIRELQQQIEDLQKSLQEQGsksegesssklkqkleAHMEKLTEVHEELQkkqELIEDLQPD 535
Cdd:COG3096 519 AQLA-----ELEQRL--RQQQNAERLLEEFCQRIGQQL----------------DAAEELEELLAELE---AQLEELEEQ 572
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 536 INQNVQKINELEAALQKKDEDMKAMEERYKMYLeKARNVIKTLDPKLNPA---SAEIMLLRKQLAEKERRIEILESE 609
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKELAARAPAWL-AAQDALERLREQSGEAladSQEVTAAMQQLLEREREATVERDE 648
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
316-615 |
2.45e-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: 44.34 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 316 EEELKKANAARTQLETYKRQVQ---DLHVKLSSESKRadtlaFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQ 392
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQaemDRQAAIYAEQER-----MAMERERELERIRQEERKRELERIRQEEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 393 VQQDHLNQTDASATKSYENLAA---EIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQR 469
Cdd:pfam17380 380 LERLQMERQQKNERVRQELEAArkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 470 LSKERIRelQQQIEDLQKSLQEQGSKSEGESSSKLKQK-LEAHMEKLTEVHEELQKKQELIEdlqpdinqnvQKINELEA 548
Cdd:pfam17380 460 QQVERLR--QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLE----------KEMEERQK 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 549 ALQKKDEDMKAMEERYKMYLEKARNVIKTldpKLNPASAEIMLLRKQLAEKERRIEILESECKVAKF 615
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
365-604 |
3.32e-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: 44.17 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 365 EALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQtDASATKSYENLaaeimpveyreVFIRLQHENKMLRLQQEGSE- 443
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELEELSARESDLEQ-DYQAASDHLNL-----------VQTALRQQEKIERYQEDLEEl 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 444 NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSL--------QEQGSKSEGESSSKLKQKLEAHMEKL 515
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvqqtraiQYQQAVQALEKARALCGLPDLTPENA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 516 TEVHEELQKKQELIEDLQPDINqnvQKINELEAALQKKDEDMKAME------ERYKMYlEKARNVIKTLdPKLNPASAEI 589
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELE---QKLSVADAARRQFEKAYELVCkiagevERSQAW-QTARELLRRY-RSQQALAQRL 514
|
250
....*....|....*
gi 1370453384 590 MLLRKQLAEKERRIE 604
Cdd:COG3096 515 QQLRAQLAELEQRLR 529
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
422-575 |
4.54e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 422 REVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKslQEQGSKSEGESS 501
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ--KQQELEKKEEEL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453384 502 SKLKQKLEAHMEKLTEVHEElQKKQELIEDLQPDInqnvqkinELEAALQKKDEDMKAMEERYKmyleKARNVI 575
Cdd:PRK12704 134 EELIEEQLQELERISGLTAE-EAKEILLEKVEEEA--------RHEAAVLIKEIEEEAKEEADK----KAKEIL 194
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
358-492 |
4.97e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.44 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 358 KRLEEKHEALLKEKERLIEQRDTLKETnEELRcsQVQQDHLNQTdasATKSYENLAAEIMPVEYREVFIRLQHENKMLRL 437
Cdd:pfam13779 489 RRLRAAQERLSEALERGASDEEIAKLM-QELR--EALDDYMQAL---AEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDR 562
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 438 QQEGSENERIEELQEQLEQKHRKMNELETEQR--LSKERIRELQQQIEDLQKSLQEQ 492
Cdd:pfam13779 563 IEELARSGRRAEAQQMLSQLQQMLENLQAGQPqqQQQQGQSEMQQAMDELGDLLREQ 619
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-492 |
6.05e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 317 EELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLiEQRDTLKETNEELRCSQVQQD 396
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 397 HLNQTDasatKSYENLAAEImpVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIR 476
Cdd:COG4717 150 ELEERL----EELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*.
gi 1370453384 477 ELQQQIEDLQKSLQEQ 492
Cdd:COG4717 224 ELEEELEQLENELEAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
445-620 |
7.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 445 ERIEELQEQLEQKHRKMNELET--EQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEEL 522
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 523 QKKQELIEDLQPDINQNVQKINELEAALQKKDEDmkameerykmylekarnviktldpKLNPASAEIMLLRKQLAEKERR 602
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGD------------------------RLEQLEREIERLERELEERERR 360
|
170
....*....|....*...
gi 1370453384 603 IEILESECKVAKFRDYEE 620
Cdd:COG4913 361 RARLEALLAALGLPLPAS 378
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
478-623 |
7.43e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 478 LQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdinqnvQKINELEAALQKKDEDM 557
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLEREL 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453384 558 KAMEERYKMYLEKaRNVIKTLDpklnpasAEIMLLRKQLAEKERRIEILESecKVAKFRDYEEKLI 623
Cdd:COG2433 451 SEARSEERREIRK-DREISRLD-------REIERLERELEEERERIEELKR--KLERLKELWKLEH 506
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-539 |
7.92e-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: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 260 LKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEEL-KKANAARTQLETYKRQVQD 338
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 339 LHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYEnlaaeimp 418
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-------- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 419 vEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEG 498
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370453384 499 ESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQN 539
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
426-582 |
8.71e-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: 41.45 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 426 IRLQH-ENKMLRLQQE-GSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ---KSLQEQGSKSE--- 497
Cdd:COG1579 10 LDLQElDSELDRLEHRlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVRnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 498 -----GESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALqkkDEDMKAMEERYKMYLEKAR 572
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAERE 166
|
170
....*....|
gi 1370453384 573 NVIKTLDPKL 582
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
234-614 |
8.81e-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: 42.70 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 234 EELEKQLIEFQHRNDELTSLAEE--TRALKDEIDvlratsDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHN 311
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEQdwNKELKSELK------NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 312 TVSLEEELKKANAARTQL----ETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEE 387
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLkkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 388 LrcsQVQQDHLNQTDASATKSYENLaaeimpveyrEVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETE 467
Cdd:TIGR04523 438 N---NSEIKDLTNQDSVKELIIKNL----------DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 468 QRLSKERIRELQQQIEDLQKSLqeqgsksegesssklkQKLEAhmEKLTEVHEELQKKQELIEDlqpdinQNVQKINELE 547
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKI----------------EKLES--EKKEKESKISDLEDELNKD------DFELKKENLE 560
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453384 548 AALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKlnpaSAEIMLLRKQLAEKERRIEILESECKVAK 614
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK----EKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
249-621 |
9.08e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 249 ELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLN-----------DLRKQVKTLQETNMMYMHNTVSLEE 317
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKkqiaddekshsITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 318 ELKKANAARTQLETYKRQVQDLHVKLSSESKRADtlafEMKRLEEKH-----EALLKEKERLIE------QRDTLKETNE 386
Cdd:PRK01156 240 ALNELSSLEDMKNRYESEIKTAESDLSMELEKNN----YYKELEERHmkiinDPVYKNRNYINDyfkyknDIENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 387 ELRcSQVQQDHLNQTDASATKSYENlAAEIMPVEYREVfirlqhenKMLRLQQEGSENERIEELQEqLEQKHRKMNELET 466
Cdd:PRK01156 316 NID-AEINKYHAIIKKLSVLQKDYN-DYIKKKSRYDDL--------NNQILELEGYEMDYNSYLKS-IESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 467 EQ-RLSKERIRELQQQI---EDLQKSLQE--QGSKSEGESSSKLKQKLEAHMEKLTEVHEEL------------------ 522
Cdd:PRK01156 385 NIeRMSAFISEILKIQEidpDAIKKELNEinVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlge 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 523 QKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERyKMYLEKAR-NVIKTLDPKLNPASAEI---MLLRKQLAE 598
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR-KEYLESEEiNKSINEYNKIESARADLediKIKINELKD 543
|
410 420
....*....|....*....|...
gi 1370453384 599 KERRIEILESECKVAKFRDYEEK 621
Cdd:PRK01156 544 KHDKYEEIKNRYKSLKLEDLDSK 566
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
123-351 |
1.19e-03 |
|
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: 42.15 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 123 LSSPpnDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpNTVVA 202
Cdd:pfam09726 391 LSKP--DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLH---------NAVSA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 203 KKyfhaqlqleqlqeenfrleaaKDDYRVhcEELEKQLIEFQ-HRNDELTSLAEETRALKDEIDVL-RATSDKANKLEST 280
Cdd:pfam09726 460 KQ---------------------KDKQTV--QQLEKRLKAEQeARASAEKQLAEEKKRKKEEEATAaRAVALAAASRGEC 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370453384 281 VEIYRQKLQdlnDLRKQVKTLQetnmmymHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRAD 351
Cdd:pfam09726 517 TESLKQRKR---ELESEIKKLT-------HDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQD 577
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
464-550 |
1.20e-03 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 40.34 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 464 LETEQRLSKERIRELQQQIEDLQKSLQEqgsksegesssklkqkleahMEKLTEVHEELQKKQELIEDLQPDINQNVQKI 543
Cdd:COG3166 43 LQGQIAQQQARNAALQQEIAKLDKQIAE--------------------IKELKKQKAELLARLQVIEQLQQSRPPWVHLL 102
|
....*..
gi 1370453384 544 NELEAAL 550
Cdd:COG3166 103 DELARLL 109
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
128-617 |
1.34e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 128 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELD---MQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvvakk 204
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQSSLAEAEQRIKELE------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 205 YFHAQLQLEQLQEENFRLEAAKddyrvhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKANKL 277
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSELAR------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAATL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 278 ESTVEIYRQKLQ-----------DLN---DLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQdlhvkl 343
Cdd:pfam05557 251 ELEKEKLEQELQswvklaqdtglNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYL------ 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 344 ssesKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELrcsqvqQDHLNQTDASATKSYENLAAEIMPVEYRE 423
Cdd:pfam05557 325 ----KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESY------DKELTMSNYSPQLLERIEEAEDMTQKMQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 424 VFIRLQHENKMLrLQQEGSENERIEELQEQLeqKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKsegesssk 503
Cdd:pfam05557 395 HNEEMEAQLSVA-EEELGGYKQQAQTLEREL--QALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQ-------- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 504 lKQKLEAHMEkltevheelqkKQELIEDLQPDINQNVQ-KINELEAALQKKDEDMKAME---ERYKMYLEKARNVIKTLD 579
Cdd:pfam05557 464 -KNELEMELE-----------RRCLQGDYDPKKTKVLHlSMNPAAEAYQQRKNQLEKLQaeiERLKRLLKKLEDDLEQVL 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1370453384 580 ----PKLNPASAEIMLLRKQLAEKERRIEILESECKVA--KFRD 617
Cdd:pfam05557 532 rlpeTTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKiqEFRD 575
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
431-608 |
1.70e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 431 ENKMLRLQQEgsenERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESS--------- 501
Cdd:COG3206 195 EAALEEFRQK----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspviqqlra 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 502 --SKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKI-NELEAALQKKDEDMKAMEERYKMYLEKARNVIKtl 578
Cdd:COG3206 271 qlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE-- 348
|
170 180 190
....*....|....*....|....*....|
gi 1370453384 579 dpklnpasaeimlLRKQLAEKERRIEILES 608
Cdd:COG3206 349 -------------LEAELRRLEREVEVARE 365
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
65-300 |
2.20e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 65 QITECSDPVE---LGRLLQLilgcAINCEKKQEHIQNIMTLEESVQHVVMTaIQELMSKEILSSPpNDAVGELEQQLKRA 141
Cdd:PRK05771 32 HIEDLKEELSnerLRKLRSL----LTKLSEALDKLRSYLPKLNPLREEKKK-VSVKSLEELIKDV-EEELEKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 142 LEELQEALAEKEELRQRCEEL------DMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYfhaqlqleqL 215
Cdd:PRK05771 106 EEEISELENEIKELEQEIERLepwgnfDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTD---------K 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 216 QEENFRLEAAKDDYRVHCEELEK---QLIEFQHR---NDELTSLAEETRALKDEIDVLRAT-SDKANKLE----STVEIY 284
Cdd:PRK05771 177 GYVYVVVVVLKELSDEVEEELKKlgfERLELEEEgtpSELIREIKEELEEIEKERESLLEElKELAKKYLeellALYEYL 256
|
250
....*....|....*.
gi 1370453384 285 RQKLQDLNDLRKQVKT 300
Cdd:PRK05771 257 EIELERAEALSKFLKT 272
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
119-491 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 119 SKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPN 198
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 199 TVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSDKANKLE 278
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-------EKLKVEEEKEEKLKAQEEELRALE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 279 STVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMK 358
Cdd:pfam02463 808 EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 359 RLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ-HENKMLRL 437
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEeERNKRLLL 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1370453384 438 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 491
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
442-532 |
2.28e-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: 40.36 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 442 SENERIEELQEQLEQKhrkmneleteqrlsKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 521
Cdd:pfam03961 153 ELKEKLEELEKELEEL--------------EEELEKLKKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEE 218
|
90
....*....|.
gi 1370453384 522 LQKKQELIEDL 532
Cdd:pfam03961 219 LKELKEELESL 229
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
440-610 |
3.25e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 440 EGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKltevH 519
Cdd:COG2433 401 KEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE------------ARSEERREIRK----D 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 520 EELQKKQELIEDLQPDINQNVQKINELEAALQKKdEDMKAMEERYKMYLEKA-----RNVIKTLDPKLNPASAEIMLLRK 594
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHSGELVPVKVvekftKEAIRRLEEEYGLKEGDVVYLRD 543
|
170 180
....*....|....*....|....*.
gi 1370453384 595 ----------QLAEKERRIEILESEC 610
Cdd:COG2433 544 asgagrstaeLLAEAGPRAVIVPGEL 569
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
356-592 |
3.34e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 356 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPveyrEVFIRLQHENKML 435
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIE----NLEFKTELIARLK 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 436 RLQQEGS----------ENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE-----------QGS 494
Cdd:COG5022 935 KLLNNIDleegpsieyvKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKElaelskqygalQES 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 495 KSEGESSSKLKQKLEAHMEKLTEVHEELQKKQelieDLQPDINQNVQKINELEA---ALQKKDEDMKAMEERyKMYLEKA 571
Cdd:COG5022 1015 TKQLKELPVEVAELQSASKIISSESTELSILK----PLQKLKGLLLLENNQLQArykALKLRRENSLLDDKQ-LYQLEST 1089
|
250 260
....*....|....*....|.
gi 1370453384 572 RNVIKTLDPKLNPASAEIMLL 592
Cdd:COG5022 1090 ENLLKTINVKDLEVTNRNLVK 1110
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
315-607 |
3.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 315 LEEELKKANAARTQLETYKRQVQDLHVKLSS--ESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEElrcsq 392
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 393 vqqdhlnqtdasatksyenlaAEIMPVEYREvfirlqhenkmlrlqqegsENERIEELQEQLEQKHRKMNELETEQRLSK 472
Cdd:PRK02224 239 ---------------------ADEVLEEHEE-------------------RREELETLEAEIEDLRETIAETEREREELA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 473 ERIRELQQQIEDLQKSLQEQGSKSEGEsssklkqklEAHMEKLTEVHEELQKKQELIEDlqpDINQNVQKINELEAALQK 552
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLD---------DADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAES 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1370453384 553 KDEDMKAMEERYKmyleKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILE 607
Cdd:PRK02224 347 LREDADDLEERAE----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
465-560 |
4.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 465 ETEQRLSKERIRELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdinqnvQKIN 544
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDA------------LQAELEELNEEYNELQAELEALQAEIDKLQ-------AEIA 75
|
90
....*....|....*.
gi 1370453384 545 ELEAALQKKDEDMKAM 560
Cdd:COG3883 76 EAEAEIEERREELGER 91
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-486 |
4.73e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 260 LKDEIDVLRATSDKANK-LESTVEIYRQKLQDLndlRKQVKTLQETNmmymhNTVSLEEElkkANAARTQLETYKRQVQD 338
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEA---EAALEEFRQKN-----GLVDLSEE---AKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 339 LHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE--RLIEQRDTLKETNEELRcSQVQQDH--LNQTDASATKSYENLAA 414
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELS-ARYTPNHpdVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370453384 415 EImpveyREVFIRLQHENKMLRlQQEGSENERIEELQEQLE---QKHRKMNELETEQRLSKERIRELQQQIEDLQ 486
Cdd:COG3206 310 EA-----QRILASLEAELEALQ-AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
130-577 |
4.78e-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: 40.34 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 130 AVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLD--GSFDDPNTVVAKKYFH 207
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLTQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 208 AQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAeetRALKDEIDVLRATSDKANKLESTVEIYRQK 287
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 288 LQDLNDLRKQVKTLQEtNMMYMHNTVSLEEELKKANAARTQLET-----YKRQVQDLHVKLsSESKRADTLAFEMKRLEE 362
Cdd:TIGR00618 458 KIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLELQeepcpLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQ 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 363 KHEALLKEKERLIEQRDTLKETNEELRcsqvQQDHLNQTDASATKSYENLAAEIMPVEYREVfIRLQHENKM---LRLQQ 439
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLK----EQMQEIQQSFSILTQCDNRSKEDIPNLQNIT-VRLQDLTEKlseAEDML 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 440 EGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE------QGSKSEGESSSKLKQKLEAHME 513
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirVLPKELLASRQLALQKMQSEKE 690
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453384 514 KLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKT 577
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
|
| Med21 |
pfam11221 |
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ... |
131-168 |
6.18e-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: 37.57 E-value: 6.18e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1370453384 131 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTT 168
Cdd:pfam11221 97 IKELEEELREAEEERQEAVKEKEELLKKLDELIRSVAR 134
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
433-563 |
6.51e-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: 39.55 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 433 KMLRLQQEGSENERIEE---LQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDlQKSLQEQGSKSEGESSSKLKQKLE 509
Cdd:pfam15709 344 EMRRLEVERKRREQEEQrrlQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-ERQRQEEEERKQRLQLQAAQERAR 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370453384 510 AHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEER 563
Cdd:pfam15709 423 QQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEER 476
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
135-414 |
6.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 135 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGsfddpntvvakkyfhaqlqleq 214
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 215 lqeenfRLEAAKDDYRVHCEELEKQLIEFQhRNDELTSLAEEtralkdeidVLRATS-----DKANKLESTVEIYRQKLQ 289
Cdd:COG3883 73 ------EIAEAEAEIEERREELGERARALY-RSGGSVSYLDV---------LLGSESfsdflDRLSALSKIADADADLLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 290 DLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDlhvKLSSESKRADTLAFEMKRLEEKHEALLK 369
Cdd:COG3883 137 ELKADKAELEAKKA----------ELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370453384 370 EKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAA 414
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
249-565 |
6.96e-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: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 249 ELTSLAEETRALKDEIDVLRATSdkaNKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMymHNTVSLEEELKKANAARTQ 328
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQE---QQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 329 LETYKRQVQDLHVKLSSeskradtlafeMKRLEEKHEALLKEKERLIEQRDTLKETNEELrcSQVQQ--DHLNQTDASAt 406
Cdd:COG3096 912 IQQHGKALAQLEPLVAV-----------LQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL--SEVVQrrPHFSYEDAVG- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 407 ksyenlaaeiMPVEYREVFIRLQHenKMLRLQQEGSE-NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDL 485
Cdd:COG3096 978 ----------LLGENSDLNEKLRA--RLEQAEEARREaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 486 QKSLQEQGSKSegesssklkqkleAHMEKlTEVHEELqkkqeliedlqpdiNQNVQKINELEAALQKKDEDMKAMEERYK 565
Cdd:COG3096 1046 GVQADAEAEER-------------ARIRR-DELHEEL--------------SQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
234-515 |
7.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 234 EELEKQLIEFQHRNDELTSLAEETRALKDE-IDVLRATSDKANKLESTVEIYRQKLQDLNDLRK----QVKTLQEtnmmy 308
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEAQELREKRDelneKVKELKE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 309 mhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSEskraDTLAFEMKRLEEKHE--ALLKEKER-LIEQRDTLKETN 385
Cdd:COG1340 79 -----ERDELNEKLNELREELDELRKELAELNKAGGSI----DKLRKEIERLEWRQQteVLSPEEEKeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 386 EELRCSQVQQDHLNQTDASATKSYENLAAEIMPV-EYREvfIRLQHENKMLRLQQEGSE-NERIEELQEQLEQKHRKMNE 463
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIkELAE--EAQELHEEMIELYKEADElRKEADELHKEIVEAQEKADE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370453384 464 LETEQRLSKERIRELQQQIEDLQKslqEQGSKSEGESSSKLKQKLEAHMEKL 515
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRK---KQRALKREKEKEELEEKAEEIFEKL 276
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
93-621 |
7.75e-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: 39.57 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 93 QEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDE 172
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 173 KNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEfQHRNDELTS 252
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK-SEDLLKETQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 253 LAEETRALKDEIDV---------LRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKAN 323
Cdd:pfam02463 479 LVKLQEQLELLLSRqkleersqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 324 AARTQLETYKRQVQDLHVK-----LSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHL 398
Cdd:pfam02463 559 EVEERQKLVRALTELPLGArklrlLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 399 NQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgseNERIEELQEQLEQKHRKMNELETEQRLSKERIREL 478
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE---LQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 479 QQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQN--VQKINELEAALQKKDED 556
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaeEREKTEKLKVEEEKEEK 795
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370453384 557 MKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEK 621
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
134-387 |
8.19e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 134 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTVVAKKYFHAQ 209
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRLSE-TDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 210 LQLEQLQEENFRLeaaKDDyrvhCEELEKQLIEFQHRNDELTSLAEEtRALKD------EIDVLRATSDKANKLESTVEI 283
Cdd:PLN02939 226 KELDVLKEENMLL---KDD----IQFLKAELIEVAETEERVFKLEKE-RSLLDaslrelESKFIVAQEDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 284 YRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYkrqvqdlhvKLSSEskRADTLAFEMKRLEEK 363
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS---------KFSSY--KVELLQQKLKLLEER 366
|
250 260 270
....*....|....*....|....*....|..
gi 1370453384 364 HEALLKE--------KERLIEQRDTLKETNEE 387
Cdd:PLN02939 367 LQASDHEihsyiqlyQESIKEFQDTLSKLKEE 398
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
235-492 |
9.22e-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: 39.55 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 235 ELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRqklqdLNDLRKQVKTLQETNMMYMHNTVS 314
Cdd:COG3096 847 ELERELAQHR---AQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADR-----LEELREELDAAQEAQAFIQQHGKA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 315 LEEELKKANAART---QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLE----EKHEALLKE--------KERLIEQRD 379
Cdd:COG3096 919 LAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlneklRARLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 380 TLKETNEELRCSQVQQDHLNQTDASATKSYEnlAAEIMPVEYREVFIRLQhenkmLRLQQEGSENERIE--ELQEQLEQK 457
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRD--AKQQTLQELEQELEELG-----VQADAEAEERARIRrdELHEELSQN 1071
|
250 260 270
....*....|....*....|....*....|....*
gi 1370453384 458 HRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 492
Cdd:COG3096 1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-389 |
9.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 221 RLEAAKDDYRVHCEELEKQLIEFQHR-----NDELTSLAEETRALKDEIDVLRATSDKANKLESTVE--IYRQKLQDLND 293
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 294 LRKQVKTLQETNMMYMHNTVSLEEELK----KANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKR----LEEKHE 365
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdLRRELR 422
|
170 180
....*....|....*....|....
gi 1370453384 366 ALLKEKERLIEQRDTLKETNEELR 389
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALR 446
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
234-621 |
9.81e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 234 EELEKQLIEFQHRNDELTSLAE--------ETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQeTN 305
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPgrqsiidlKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCL-TD 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 306 MMYMHNtvsLEEELKKaNAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETN 385
Cdd:TIGR00606 791 VTIMER---FQMELKD-VERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 386 EELRCSQVQQDHLNQTDASATKSYENLAAEIMpveyrevfiRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKmnelE 465
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ---------SLIREIKDAKEQDSPLETFLEKDQQEKEELISSK----E 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 466 TEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKlEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINE 545
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453384 546 LEAALQ------KKDEDMKAMEERYKMYLE--------KARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECK 611
Cdd:TIGR00606 1013 QERWLQdnltlrKRENELKEVEEELKQHLKemgqmqvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
410
....*....|
gi 1370453384 612 VAKFRDYEEK 621
Cdd:TIGR00606 1093 EPQFRDAEEK 1102
|
|
| |
