|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
178-705 |
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: 680.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 178 ELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 257
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 258 AKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEK 337
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 338 NTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKET 417
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 418 IEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRK 497
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 498 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaiSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFN-NSS 576
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 577 LKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQREM 656
Cdd:pfam05622 399 QKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622960298 657 EEKYIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSSRRSYP 705
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
14-154 |
7.58e-94 |
|
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: 288.02 E-value: 7.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 93
Cdd:cd22226 13 IQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960298 94 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 154
Cdd:cd22226 93 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
14-155 |
3.58e-88 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 273.13 E-value: 3.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 93
Cdd:pfam19047 10 LQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLGQQISDFL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960298 94 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 155
Cdd:pfam19047 90 LPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
14-153 |
1.01e-84 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 263.72 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 93
Cdd:cd22222 8 LQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQQISGFT 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 94 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 153
Cdd:cd22222 88 MPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
14-155 |
2.92e-75 |
|
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: 238.98 E-value: 2.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 93
Cdd:cd22225 9 LQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLDQQISEFL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960298 94 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 155
Cdd:cd22225 89 LPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
14-154 |
2.39e-64 |
|
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: 210.12 E-value: 2.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 93
Cdd:cd22227 10 LQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLGHQVSEDH 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960298 94 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 154
Cdd:cd22227 90 LPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
14-153 |
6.14e-50 |
|
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: 171.30 E-value: 6.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 93
Cdd:cd22211 8 INTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQLSDLP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 94 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 153
Cdd:cd22211 86 LPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
14-151 |
5.26e-23 |
|
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: 95.74 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 14 IQTFNVDAPWQ-TVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINdF 92
Cdd:cd22223 10 AKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQLIV-M 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960298 93 TLPDVNLIGEHSDA----AELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 151
Cdd:cd22223 85 KLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
28-151 |
1.11e-15 |
|
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: 74.96 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 28 DLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH---- 103
Cdd:cd22228 29 DLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEVL-QQLIVMNLPNVLMIGKDplsg 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622960298 104 SDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 151
Cdd:cd22228 104 KSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-629 |
7.26e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDY---RIRCEELEKEISELRQQndelTTLADEAQSLKDEIDVLrhssdkvsKLEGQVESYKKKLEDLGDLRRQ 330
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQ----AEKAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 331 VKLLEEKNTVYMQNTVSLEEELRKANAARSQLEtykRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTE 410
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 411 RDSLKETIEELrcvQAQEGQLTTQGLMplgSQESSDSLAAEIVtpEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLL 490
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEELEE---AEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 491 DDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllKKKLEEHLEKLHEANNELQKKRAIIEDLEP 570
Cdd:COG1196 397 ELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960298 571 RFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 629
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-659 |
7.46e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 124 EQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAqrchELDMQVAAL 203
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 204 QEEKSSLLAENQVLMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 273
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 274 SELRQQNDELTTLADEAQSLKDEIDVLRHSS---DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTvymqntvSL 348
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 349 EEELRKANAARSQLET----YKRQVVELQ-------------------NRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 405
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 406 RLRTERD------SLKETIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKlnqegSD 479
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK-----------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 480 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANNE 557
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 558 LQKKRAIIEDLEPRFNNSSLKIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERD 637
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIK 693
|
570 580
....*....|....*....|..
gi 1622960298 638 RLFHSLEKEYEKTKSQREMEEK 659
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEK 715
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-655 |
1.65e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 147 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDS 226
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 227 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkdeiDVLRHSSDK 306
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 307 VSKLEGQVESYKKKLEDLgdlrrqvkllEEKNTVYMQNTVSLEEELRkanAARSQLETYKRQVVELQNRLSEESKKADKL 386
Cdd:PRK02224 337 AQAHNEEAESLREDADDL----------EERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 387 DFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQH 466
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 467 ENKMLKLNQEGSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAEDAISVLLK 541
Cdd:PRK02224 483 ELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 542 KKL--EEHLEKLHEANNELQKKRAIIEDLEpRFNNSSLKIEELQ---EALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 616
Cdd:PRK02224 563 AEEeaEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEdeiERLREKREALAELNDERRERLAEKRERKRELEA 641
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622960298 617 KQNQGAAPEIQalknqlQERDRLFHSLEKEYEKTKSQRE 655
Cdd:PRK02224 642 EFDEARIEEAR------EDKERAEEYLEQVEEKLDELRE 674
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
28-151 |
2.08e-11 |
|
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: 62.50 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 28 DLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH--SD 105
Cdd:cd22229 32 ALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQETL-QQLIMMSLPNVLVLGRNplSE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622960298 106 AA--ELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 151
Cdd:cd22229 107 QGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-587 |
7.79e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDK-VSKLEGQVESYKKKLEDL----GDLR 328
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 329 RQVKLLEEKNTVYMQNTVSLEEEL----RKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEK 404
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 405 DRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDN---- 480
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 481 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQS----QVEELQKSLQDQGSKAEDAIsvllkKKLEEHLEKLHEANN 556
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRL-----KRLENKIKELGPVNL 989
|
330 340 350
....*....|....*....|....*....|...
gi 1622960298 557 ElqkkrAI--IEDLEPRFNNSSLKIEELQEALR 587
Cdd:TIGR02168 990 A-----AIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-655 |
4.84e-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: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 365 YKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDR------LRTERDSLKETIEELRCVQAQEGQLTTQGLMp 438
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELEELQEEL- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 439 LGSQESSDSLAAEIVTPEIREKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQV 518
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 519 EELQKSLQDQGSKAED--AISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQM 596
Cdd:TIGR02168 319 EELEAQLEELESKLDElaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960298 597 EERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRE 655
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-651 |
1.16e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 147 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSds 226
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 227 iEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQ----SLKDEIDVLRH 302
Cdd:TIGR02168 315 -ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 303 ssdKVSKLEGQVESYKKKLEDLGdlRRQVKLLEEKNTVYMqntvslEEELRKANAARSQLETYKRQVVELQNRLSEESKK 382
Cdd:TIGR02168 394 ---QIASLNNEIERLEARLERLE--DRRERLQQEIEELLK------KLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 383 ADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQ-----GLMPLGSQ----ESSDSLAAEIV 453
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglsGILGVLSElisvDEGYEAAIEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 454 TPEIREKLI---------------------------------RLQHENKMLKLNQEG----------SDNEKIALLQSLL 490
Cdd:TIGR02168 543 LGGRLQAVVvenlnaakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 491 ---------DDANLRKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLK 541
Cdd:TIGR02168 623 ggvlvvddlDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE-----LE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 542 KKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEEL---QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQ 618
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
570 580 590
....*....|....*....|....*....|....*....
gi 1622960298 619 NQGAA------PEIQALKNQLQERDRLFHSLEKEYEKTK 651
Cdd:TIGR02168 778 AEAEAeieeleAQIEQLKEELKALREALDELRAELTLLN 816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-571 |
6.00e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 162 NDAYVDLDRQLKKtteelneaLSAKEEIAQRCHELDMQVAALQeeKSSLLAENQVLMERLNQSDSIEDpnspagrrhlql 241
Cdd:TIGR02168 192 EDILNELERQLKS--------LERQAEKAERYKELKAELRELE--LALLVLRLEELREELEELQEELK------------ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 242 qtqleQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlkdeidvlrhssdKVSKLEGQVESYKKKL 321
Cdd:TIGR02168 250 -----EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------------EISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 322 EdlgDLRRQVKLLEEkntvymqntvSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQ 401
Cdd:TIGR02168 312 A---NLERQLEELEA----------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 402 KEKDRLRTERDSLKETIEelrcvqaqegqlttqglmplgsqessdSLAAEIVtpEIREKLIRLQHENKMLKLNQEGSDNE 481
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 482 ----KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANN 556
Cdd:TIGR02168 430 leeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLERLQENLEGFSEGVK 509
|
410
....*....|....*
gi 1622960298 557 ELQKKRAIIEDLEPR 571
Cdd:TIGR02168 510 ALLKNQSGLSGILGV 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
124-648 |
1.00e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 124 EQKQEYIQAIMMMEESVQHVVMT--AIQELMSKEspvsagNDAYVDLDRQLKKTTEELNEALSAKEEIaqrcheLDMQVA 201
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 202 ALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEISELRQQ-- 279
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 280 --NDELTTLADEAQSlKDEIdVLRHSSDKVSKLEGQVEsykkkLEDLGDLRRQVKLLEEKNTVYMQNTVSLEEelrkana 357
Cdd:pfam15921 242 pvEDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 358 ARSQLETYKRQVVELQNRLSEESKKADkldfEYKRLKE-KVDSLQK-------EKDRLRTERDSLketieelrcvqaqeg 429
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQF--------------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 430 qlttqglmplgSQES---SDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETenrL 506
Cdd:pfam15921 369 -----------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---L 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 507 VNQRLLEVQSQVEELQKSLQDQGSKAEDAISvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEAL 586
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960298 587 RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRLFHSLEKEYE 648
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
29-151 |
1.34e-08 |
|
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: 54.84 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 29 LTNGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----S 104
Cdd:cd22230 47 LSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAHRVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622960298 105 DAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 151
Cdd:cd22230 122 AVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-526 |
1.72e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 167 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLaENQVLMERLnqsdsIEDPNSPAGRRHLQLQTQLE 246
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 247 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT-----LADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKL 321
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 322 EDLGdlRRQVKLLEEKNTVYMQNTvSLEEELRKANAARSQLET----YKRQVVELQNRLSEESKKADKLDFEYKRLKEKV 397
Cdd:TIGR02169 318 EDAE--ERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 398 DSLQKEKDRLRTERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGSQESSDSLAAEIvtPEIREKLIRLQheNKMLKLNQE 476
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLA--ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622960298 477 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 526
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-702 |
3.14e-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: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLkdeidvLRHSSDKVSKLEGQVESYKKKLEDLgdLRRQVKL 333
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 334 LEEkntvymqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDS 413
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 414 LKETIEELRcvqaqegqlttqglmplgSQESSDSLAAEivtpEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDA 493
Cdd:COG1196 391 ALRAAAELA------------------AQLEELEEAEE----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 494 NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLE-------KLHEANNELQKKRAIIE 566
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 567 DLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRLFHSLEK 645
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 646 EYEKTKSQREME---EKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSSRR 702
Cdd:COG1196 609 READARYYVLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
298-599 |
3.79e-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: 56.99 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 298 DVLRHSSDKVSKLEGQVES------YKKKLEDL------GDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETY 365
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerykeLKAELRELelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 366 KRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESS 445
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 446 DSLAAEIVtpEIREKLIRLQHENKMLKlnqegsdnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 525
Cdd:TIGR02168 347 EELKEELE--SLEAELEELEAELEELE--------SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622960298 526 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEER 599
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-465 |
7.34e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 168 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDsiedpnspagRRHLQLQTQLEQ 247
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 248 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEDLgD 326
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNRL-T 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 327 LRRQvkLLEEKntvyMQNTVSLEEELR-KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 405
Cdd:TIGR02169 826 LEKE--YLEKE----IQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960298 406 RLRTERDSLKETIEELRC--------VQAQEGQLTTQG-LMPLGSQESSDSLAAEIVTPEIREKLIRLQ 465
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKrlselkakLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-658 |
7.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 167 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAEnqvLMERLNQSDSIEDPNSPAGRRHLQLQTQLE 246
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 247 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI--DVLRHSSDKVSKLEGQVESYKKKLEDL 324
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAeeELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 325 GDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEK 404
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 405 DRLRTERDSLKETIEE----LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPE---------IREKLIRLQHENKML 471
Cdd:COG1196 487 AEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAIEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 472 KLNQEGsdneKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKL 551
Cdd:COG1196 567 KAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 552 HEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKN 631
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
490 500
....*....|....*....|....*..
gi 1622960298 632 QLQERDRLFHSLEKEYEKTKSQREMEE 658
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLE 749
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-661 |
9.75e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 263 RIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHS----SDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKN 338
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 339 TVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLdfeyKRLKEKVDSLQKEKDRLRT---ERDSLK 415
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEErheLYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 416 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLN---------------QEGSDN 480
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgRELTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 481 EKIALLQS-LLDDANLRKNELETENRL--VNQRLLEVQSQVEEL-----QKSLQDQGSKAEDAISVLLKKKLE---EHLE 549
Cdd:PRK03918 449 HRKELLEEyTAELKRIEKELKEIEEKErkLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELEkkaEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 550 KLHEANNELQKKRAIIED----LEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ----- 620
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKelekLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelk 608
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1622960298 621 GAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQREMEEKYI 661
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-662 |
1.74e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 232 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD------ 305
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElealea 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 306 KVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKntvYMQNTVSLEEELRK-ANAARSQLETYKRQVVELQNRLSEESKKAD 384
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAE---LAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 385 KLDFEYKRLKEKVDSLQKEKdrlrtERDSLKETIEELR----------CVQAQEGQLTTQGLMPLGSQESSDSLAAEIVT 454
Cdd:COG4717 217 EAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 455 PEIREKLIRLQHENKMLKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGskAE 533
Cdd:COG4717 292 LLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE--LE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 534 DAISVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALrkkeeemkqMEERYKKYLEKAKSV 610
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622960298 611 IRTLDPKQNQgAAPEIQALKNQLQ--ERDRLFHSLEKEYEKTKSQ-REMEEKYIV 662
Cdd:COG4717 441 LEELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAElRELAEEWAA 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-421 |
3.18e-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: 53.92 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 167 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQVLMERLNQSDSIEDPNSP 233
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 234 AGRRHLQLQTQLEQLQEETFRLEAAKDdyriRCEELEKEISELRQQNDELTTLADEAQ-SLKDEIDVLRHSSDKVSKLEG 312
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 313 QVESYKKKLEDLG----DLRRQVKLLEEKNTVYMQNTVSLEEELRK---ANAARSQLETYKRQVVELQNRLSEESKKADK 385
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622960298 386 LDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 421
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-587 |
9.61e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 298 DVLRHSSDKVSKLEGQVESYKkkleDLGDLRRQVK--LLEEKNTvyMQNTVSLEEELRKANAARSQLETYKRQV------ 369
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDT--FEAADALVEHFDDLERAHEALEDAREQIellepi 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 370 VELQNRLSEESKKADKLD-----FEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLttqglmplgsqes 444
Cdd:COG4913 258 RELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL---EARLDAL------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 445 sdslaaeivtpeiREKLIRLQHEnkmlklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKS 524
Cdd:COG4913 322 -------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960298 525 LQDQGSKAEDAISVL------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 587
Cdd:COG4913 382 FAALRAEAAALLEALeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-586 |
1.11e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 344 NTVSLEEELRKANAarsQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRc 423
Cdd:TIGR02169 668 FSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 424 vqaQEGQLTTQGLmpLGSQESSDSLAAEIvtPEIREKLIRLQHE-----------------NKMLKLNQEGSDNE----- 481
Cdd:TIGR02169 744 ---EDLSSLEQEI--ENVKSELKELEARI--EELEEDLHKLEEAlndlearlshsripeiqAELSKLEEEVSRIEarlre 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 482 -----------------KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKL 544
Cdd:TIGR02169 817 ieqklnrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKER 891
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622960298 545 EEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEAL 586
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
348-534 |
1.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 348 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcVQAQ 427
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL--LRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 428 EGQLTTQGLMPLGSQESSDSLAA-----EIVTPEIREKLIRLQHENKMLKLNQEGSDNEKiALLQSLLDDANLRKNELET 502
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAER-AELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|..
gi 1622960298 503 ENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 534
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
267-587 |
1.80e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 267 EELEKEISELRQQNDELTTLADEAQSLKDE-------IDVLRHSSD----KVSKLEGQVESYKKKLEdlGDLRRQVKLLE 335
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 336 EKN------TVYMQNTVSLEEELRKA----NAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 405
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 406 RLRTERDSLKETieelrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKI-- 483
Cdd:pfam15921 535 HLKNEGDHLRNV------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 484 --ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ---KSLQDQGSKAEDAISVlLKKKLEEHLEKLHEANNEL 558
Cdd:pfam15921 591 ekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNEL 669
|
330 340
....*....|....*....|....*....
gi 1622960298 559 QKKRAIIEDLEPRFNNSSLKIEELQEALR 587
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-610 |
1.99e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 263 RIRCEELEKEISELRQQNDELTTLADEA-QSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEKNTVY 341
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 342 MQNTVSLEEELrkaNAARSQLETYKRQVVELQNRLSEE-----SKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKE 416
Cdd:TIGR02169 757 KSELKELEARI---EELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 417 TIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRL-QHENKMLKLNQEGSDNEK-IALLQSLLDDAN 494
Cdd:TIGR02169 834 EIQELQEQRID-----------LKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRLGDLKKeRDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 495 LRKNELETENRLVNQRLLEVQSQVEELQkslqDQGSKAEDAISVLLKKKLEE-HLEKLHEannELQKKRAIIEDLEP--- 570
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALE----EELSEIEDPKGEDEEIPEEElSLEDVQA---ELQRVEEEIRALEPvnm 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622960298 571 ----RFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 610
Cdd:TIGR02169 976 laiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-505 |
2.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD-------------EAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 320
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 321 LEDL----GDLRRQVKLLEEKNTvymqntvSLEEELRKANAARSQLETYKRQVV--ELQNRLSEESKKAdkldfeykRLK 394
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 395 EKVDSLQKEKDRLRTERDSLKETIEELRcvqaqegqLTTQGLMPLGSQESSDSLAAEivtPEIREKLIRLQ------HEN 468
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM--------RAFNREWPAETADLDADLESL---PEYLALLDRLEedglpeYEE 834
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622960298 469 KMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENR 505
Cdd:COG4913 835 RFKELLNENSIEFVADLLSKLRRAIREIKERIDPLND 871
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
177-652 |
3.67e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 177 EELNEaLSAKEEIAQRcheLDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLE 256
Cdd:PRK01156 239 SALNE-LSSLEDMKNR---YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 257 AAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDlgdlrrqvkllEE 336
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE-----------YS 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 337 KNTVYMQNTVSLEEELRKANAArsqletykrqvvELQNRLSEESKKADKLDfeykrlkEKVDSLQKEKDRLRTERDSLKE 416
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPD------------AIKKELNEINVKLQDIS-------SKVSSLNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 417 TIEelrcvqaqegQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLqhENKMLKLNQEGSD-NEKIALLQSLLDDANL 495
Cdd:PRK01156 445 NME----------MLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRL--EEKIREIEIEVKDiDEKIVDLKKRKEYLES 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 496 RK-NELETENRLVNQRLLEVQsQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI-IEDLEPRFN 573
Cdd:PRK01156 512 EEiNKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdIETNRSRSN 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960298 574 NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRLFHSLEKEYEKTKS 652
Cdd:PRK01156 591 EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-664 |
4.25e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 349 EEELRKANAARSQLETYKRQVVEL---QNRLSEESKKADKldfeYKRLKEKVDSLQK-----EKDRLRTERDSLKETIEE 420
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 421 LrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNEL 500
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 501 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKaedaisvllKKKLEEHLEKLHEANNELQKKraiiedleprfnnsslkIE 580
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEE-----------------LE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 581 ELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgaapeIQALKNQLQERDRLFHSLEKEYEKTKSQREMEEKY 660
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-----IASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
....
gi 1622960298 661 IVSA 664
Cdd:TIGR02168 430 LEEA 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-664 |
4.94e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 253 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI--DVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQ 330
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 331 vklleekntvYMQNTVSLEEElrkANAARSQLETYKRQVVELQNRLSEESKKA----DKLDFEYKRLKEKVDSLQKEKDR 406
Cdd:COG4913 364 ----------LEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 407 LRTERDSLKETIEELRCVQAQE---------------------------------------------------------- 428
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhl 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 429 -GQLTTQGLMPLGSQE-----SSDSLAAEIVT------PEIREKLIR------------LQHENK------MLKLNQE-- 476
Cdd:COG4913 511 rGRLVYERVRTGLPDPerprlDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNGTrh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 477 --------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDAISVLLK 541
Cdd:COG4913 591 ekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 542 -KKLEEHLEKLHEANNELQKKRAIIEDLEprfnnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 620
Cdd:COG4913 670 iAELEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622960298 621 GAAPEIQALKNQLQE------RDRLFHSLEKEYEKTKSQREMEEKYIVSA 664
Cdd:COG4913 743 ARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
353-664 |
6.55e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 353 RKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEyKRLKEKVDSLQKEKDRLR-TERDSLKETIEELRcvQAQEGQL 431
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgYELLKEKEALERQK--EAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 432 TTQGLMPLGSQESSDSLAAEIVTPEIR----EKLIRLQHENKMLKLNQE-GSDNEKIALLQSLLDDANLRKNELETENRL 506
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLleelNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 507 VNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL---------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSL 577
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkeeledLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 578 KIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRLFHSLEKEYEKTKSQREME 657
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
....*..
gi 1622960298 658 EKYIVSA 664
Cdd:TIGR02169 482 EKELSKL 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-637 |
7.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 358 ARSQLETYKRQVVELQNRLSEeskkadkldfeykrLKEKVDSLQKEKDRLRTERDSLkETIEELRcvqaqegqlttqglm 437
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 438 plgsqessdslAAEIVTPEIREKLIRLQHENKMLKlnqegSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQ 517
Cdd:COG4913 658 -----------WDEIDVASAEREIAELEAELERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 518 V---EELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI---IEDLEPRFNNSSLKIEELQEAlrkkee 591
Cdd:COG4913 722 LeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeerIDALRARLNRAEEELERAMRA------ 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622960298 592 emkqmeerykkYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 637
Cdd:COG4913 796 -----------FNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
148-419 |
7.22e-06 |
|
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: 49.35 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 148 IQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQV 216
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 217 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEISELRQQNDEL 283
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 284 TTLADEAQSLKDEIDVLRHSSDKV--------------SKLEGQVESYKKKLEDLG-------DLRRQVKLLEEKNTVYM 342
Cdd:pfam05557 217 NENIENKLLLKEEVEDLKRKLEREekyreeaatlelekEKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960298 343 QNTVSLEEELRKANAARSQLETYKRQVVelqnrlseesKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIE 419
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
293-581 |
7.99e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 293 LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTVYMQNTVSLEEEL-RKANAARSQLETYKRQVVE 371
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 372 LQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAE 451
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL------------EQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 452 IVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 531
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622960298 532 AEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEE 581
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-635 |
8.20e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 167 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDpnsPAGRRHLQLQTQLE 246
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 247 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDEL-TTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLG 325
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 326 DLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLE--TYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKE 403
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 404 KDRLRTERDsLKETIEELRcvQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKmLKLNQEGSDNEKI 483
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD-ARYYVLGDTLLGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 484 ALLQSLLDDANLRKNELETENRLVNQ--RLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKK 561
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622960298 562 RAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQE 635
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-679 |
1.07e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 165 YVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDsiedpnspagrrHLQLQTQ 244
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE------------DRRERLQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 245 LEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLED 323
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQEN 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 324 LGDLRRQVKLLEEKNTVY------MQNTVSLEEELRKA-----------------NAARSQLETYKRQVVELQNRLSEES 380
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLsgilgvLSELISVDEGYEAAieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDS 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 381 KKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL--RCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTP--- 455
Cdd:TIGR02168 581 IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggv 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 456 ----EIREKLIRLQHENKMLKLNQEGSDNE-KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGS 530
Cdd:TIGR02168 661 itggSAKTNSSILERRREIEELEEKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 531 KAE----------------DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMK 594
Cdd:TIGR02168 741 EVEqleeriaqlskeltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 595 QMEERYKKYLEKAKSVIRTLDPKQNQgaapeiqaLKNQLQERDRLFHSLEK-EYEKTKSQREMEEKYIVSAWYNMGMTLH 673
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQ--------IEELSEDIESLAAEIEElEELIEELESELEALLNERASLEEALALL 892
|
....*.
gi 1622960298 674 KKAAED 679
Cdd:TIGR02168 893 RSELEE 898
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
254-655 |
1.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDdyriRCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLEG---QVESYKKKLEDLGDL 327
Cdd:PTZ00121 1358 EAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAakkKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 328 RRQVKLLEEKNTVymQNTVSLEEELRKANAARSQLETyKRQVVELQNRlSEESKKADKLDFEYKRLKEKVDSLQKeKDRL 407
Cdd:PTZ00121 1434 DEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 408 RTERDSLKETIEELRCVQAQEGQLTTQglmplgsqessdslAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKiallQ 487
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKK--------------ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----K 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 488 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDA-ISVLLKKKLEEHLEKLHEANNELQKKRAIIE 566
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 567 DLEPRFNNSSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQER 636
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEEN 1728
|
410
....*....|....*....
gi 1622960298 637 DRLFHSLEKEYEKTKSQRE 655
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAE 1747
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-425 |
1.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 173 KKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIedpnspagRRHLQLQTQLEQLQEET 252
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK--------KKAEEAKKAEEDKNMAL 1580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 253 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL----- 327
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenk 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 328 --RRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 405
Cdd:PTZ00121 1661 ikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
250 260
....*....|....*....|
gi 1622960298 406 RLRTERDSLKETIEELRCVQ 425
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIA 1760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
167-421 |
2.52e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 167 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQ-----------SDSIEDPNSPAG 235
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 236 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDE-IDVLRHSSDKVSKLEGQV 314
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 315 ESYKKKLEDLgDLRRQ---VKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSE---------Eskk 382
Cdd:TIGR02168 918 EELREKLAQL-ELRLEgleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE--- 993
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622960298 383 adkldfEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 421
Cdd:TIGR02168 994 ------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
255-422 |
3.42e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 255 LEAAKDDYRIRCEELEKEISELRQQNDeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLL 334
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAAL---RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 335 EEKNTVYMQNTV--SLEEELRKANAARSQLET-----------YKRQVVELQNRLSEESKKA-DKLDFEYKRLKEKVDSL 400
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1622960298 401 QKEKDRLRTERDSLKETIEELR 422
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
348-422 |
3.67e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 348 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLK----------EKVDSLQKEKDRLRTERDSLKET 417
Cdd:COG2433 408 LTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREISRLDREIERLERELEEERER 487
|
....*
gi 1622960298 418 IEELR 422
Cdd:COG2433 488 IEELK 492
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
354-537 |
3.89e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 354 KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCV-------QA 426
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 427 QEGQLTTQGLMPLGSQESSD----SLAAEIVTPEIREKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELET 502
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622960298 503 ---ENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAIS 537
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
254-420 |
4.68e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDV-LRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 332
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 333 LLEEKNTVYMQNTVsLEEELRKANAarsQLETYKRQVVELQNRLSEeskKADKLDFEYKRLKEKVDSLQKEKDRLRTERD 412
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 1622960298 413 SLKETIEE 420
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
254-661 |
6.12e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 333
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 334 LEEKNTVymqntvsleEELRKANAARSQLETYKRQVVELQNRlSEESKKAD--------KLDFEYKRLKEKVDSLQKEKD 405
Cdd:PTZ00121 1305 DEAKKKA---------EEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 406 RLRTERDSLKETIEELRcvQAQEGQLTTQGLMPlGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIAL 485
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 486 LQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllkKKLEEHLEKLHEANNELQKKRAI 564
Cdd:PTZ00121 1452 KAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA------KKAAEAKKKADEAKKAEEAKKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 565 iedlEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLE 644
Cdd:PTZ00121 1526 ----EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410
....*....|....*....
gi 1622960298 645 KEYEKTKSQ--REMEEKYI 661
Cdd:PTZ00121 1602 EEEKKMKAEeaKKAEEAKI 1620
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
345-587 |
6.24e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 345 TVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTE----RDSLKETIEE 420
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 421 LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIvtpeirEKLIRlQHENKMLKLNQEGSDNEKIALLQSLLDDAnLRKNEL 500
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 501 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAE--DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLK 578
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQelHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 1622960298 579 IEELQEALR 587
Cdd:COG1340 239 LRELRKELK 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-586 |
6.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 295 DEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTVYMQNTVSLEEELRkanAARSQLETYKRQVVELQN 374
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK---EKEKELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 375 RLSEESKKADKLDFEYKRL---KEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQegqlTTQGLMPLGSQESSDSLAAE 451
Cdd:PRK03918 215 ELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 452 IVTPEIREKLIRLQHENKMLKLNQEGSD-NEKIALLQSLLDDANLRKNEL-ETENRL--VNQRLLEVQSQVEELQ--KSL 525
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRlEEEINGIEERIKELEEKEERLeELKKKLkeLEKRLEELEERHELYEeaKAK 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960298 526 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKraiIEDLEPRFNNSSLKIEELQEAL 586
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAI 428
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
257-422 |
9.09e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 257 AAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKK--KLEDLGDL----RR 329
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 330 QVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRT 409
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 1622960298 410 ERDSLKETIEELR 422
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
187-433 |
1.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 187 EEIAQRCHELDMQVAALQEEKSSL---LAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR 263
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 264 IRCEELEKEISELRQQNDE----LTTLADEAQSLKDEIDVL---RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK-LLE 335
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReRLA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 336 EKNTVYMQNTVSLEEE-LRKANAARSQLETYKRQVvelqnrlseeskkADKLDfeykRLKEKVDSLQ----------KEK 404
Cdd:PRK02224 631 EKRERKRELEAEFDEArIEEAREDKERAEEYLEQV-------------EEKLD----ELREERDDLQaeigavenelEEL 693
|
250 260
....*....|....*....|....*....
gi 1622960298 405 DRLRTERDSLKETIEELRCVQAQEGQLTT 433
Cdd:PRK02224 694 EELRERREALENRVEALEALYDEAEELES 722
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
284-421 |
2.13e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 284 TTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKlEDLGDLRRQVKLLEEKNtvymqntVSLEEELRKANAARSQLE 363
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE-EEIRRLEEQVERLEAEV-------EELEAELEEKDERIERLE 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960298 364 TYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 421
Cdd:COG2433 448 RELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
184-434 |
2.37e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 184 SAKEEIAQRCHELD-MQVAALQEEKSS-----LLAENQVLMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEA 257
Cdd:PRK05771 16 SYKDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 258 AKDDYRIRCEELEKEISELrqqNDELTTLADEAQSLKDEIDVLR------------HSSDKVSKLEGQVESYKKKLEDLG 325
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERLEpwgnfdldlsllLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 326 DLRRQVKLLEE-KNTVYM------QNTVSLEEELRKANAARSQLEtykrqvvelqnrlseESKKADKLdfeYKRLKEKVD 398
Cdd:PRK05771 164 SDVENVEYISTdKGYVYVvvvvlkELSDEVEEELKKLGFERLELE---------------EEGTPSEL---IREIKEELE 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622960298 399 SLQKEKDRLRTERDSLKETIEELrcVQAQEGQLTTQ 434
Cdd:PRK05771 226 EIEKERESLLEELKELAKKYLEE--LLALYEYLEIE 259
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-568 |
2.85e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 267 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRH--SSDKVSKLEGQVESYKKKLEDL-----------GDLRRQVKL 333
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 334 LEEKNTVYMQNTVSLEEELRKANAA-----------RSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQK 402
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 403 EKDRLRTERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHE-----NKMLKLNQEG 477
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 478 SD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdaisvllKKKLEEHLEKLHEANN 556
Cdd:TIGR04523 506 KElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNKEIEELKQTQK 578
|
330
....*....|..
gi 1622960298 557 ELQKKRAIIEDL 568
Cdd:TIGR04523 579 SLKKKQEEKQEL 590
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
292-571 |
3.03e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 292 SLKDEID-VLR--HSSDKVsklegQVESYKKKLEDLgdlrrQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKrq 368
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 369 VVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGQLTTQGLMPLGSQESS 445
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 446 DSLAAEIVTPEIREKlirlqHENKMLKLNQEGSDNEKIAllqSLLDDANLRKNELETENRL------VNQRLLEVQSQVE 519
Cdd:PRK05771 161 KLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEEGTPselireIKEELEEIEKERE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960298 520 ELQKSLQDQGSKAEDAISVL------LKKKLE--------------------EHLEKLHEANNELQKKRAIIEDLEPR 571
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALyeyleiELERAEalskflktdktfaiegwvpeDRVKKLKELIDKATGGSAYVEFVEPD 310
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-661 |
3.69e-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: 43.86 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 267 EELEKEI----SELRQQNDELTTLADeaqSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED----LGDLRRQVKLLEEKN 338
Cdd:TIGR04523 36 KQLEKKLktikNELKNKEKELKNLDK---NLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 339 TVYMQNTVSLEEELRKAnaaRSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETI 418
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKL---EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 419 EELRcvqAQEGQLTTQGLMPLGSQESSDSLAAEIVtpEIREKLIRLqhENKMLKLNQEgsDNEKIALLQSLLDDANLRKN 498
Cdd:TIGR04523 190 DKIK---NKLLKLELLLSNLKKKIQKNKSLESQIS--ELKKQNNQL--KDNIEKKQQE--INEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 499 ELETENRLVNQRLLEVQsQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLEPRFNNSSLK 578
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELE-QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS---ELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 579 IEELQEA---LRKKEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERDRLF--------------- 640
Cdd:TIGR04523 337 ISQLNEQisqLKKELTNSESENSEKQRELEEKQNEIEKLK-KENQSYKQEIKNLESQINDLESKIqnqeklnqqkdeqik 415
|
410 420
....*....|....*....|....*..
gi 1622960298 641 ------HSLEKEYEKTKSQREMEEKYI 661
Cdd:TIGR04523 416 klqqekELLEKEIERLKETIIKNNSEI 442
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
268-611 |
4.88e-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: 43.81 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 268 ELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLgdlrrQVKLLEEKNTVYMQNTVS 347
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-----EELLADRVQEAQDKINEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 348 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQ 427
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 428 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLV 507
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 508 NQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 587
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 1622960298 588 KKEEEMKQMEERYKKYLEKAKSVI 611
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
265-668 |
5.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 265 RCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLE--GQVESYKKKLEDLGDLRRQVKLLEEKNT 339
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 340 VymQNTVSLEEELRKANAARSQLETYKRQVVELQN-----------RLSEESKKADKLdfEYKRLKEKVDSLQKEKDRLR 408
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaeakkkadeaKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 409 TERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQS 488
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 489 LLDD----ANLRKNELETENRLVNQRLLEVQSQV--EELQKSLQDQGSKAEDAisvllkKKLEEHLEKLHEANNELQKKR 562
Cdd:PTZ00121 1628 AEEEkkkvEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEA------KKAEEDEKKAAEALKKEAEEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 563 AIIEDLEPRFNNSSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQ 632
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKkaeeenkikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL--KKEEEKKAEEIRKEKEA 1779
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622960298 633 LQERDrlfhsLEKEYEKTKSQREMEEKYIVSAWYNM 668
Cdd:PTZ00121 1780 VIEEE-----LDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
259-525 |
9.10e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 259 KDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEidvlrhssdkvskLEGQVESYKkklEDLGDLRRQVKLLEEKN 338
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-------------LNGELSAAD---AAVAKDRSELEALEDQH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 339 TVYmqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDS-LQKEKDRLRTERDSLKET 417
Cdd:pfam12128 332 GAF------LDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 418 IEELRCV-----QAQEGQLTTQ---GLMPLGSQESSDSLAAE---------IVTPEIREKLIRLQHENKMLKLNQEGSdN 480
Cdd:pfam12128 406 RDRQLAVaeddlQALESELREQleaGKLEFNEEEYRLKSRLGelklrlnqaTATPELLLQLENFDERIERAREEQEAA-N 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622960298 481 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 525
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-659 |
9.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 256 EAAKDDYRIRCEELEKEISELRQQnDELTTLADEAQSLKDEIDvlRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLE 335
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 336 EKNtvymqntvslEEELRKANAARSQLETyKRQVVELQNRLSEESKKADKLDfEYKRLKEKVDSLQKEKDRLRtERDSLK 415
Cdd:PTZ00121 1371 KKK----------EEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 416 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDA-- 493
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkk 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 494 --NLRKNE----LETENRLVNQRLLEVQSQVEELQKSlqDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQK--KRAII 565
Cdd:PTZ00121 1518 aeEAKKADeakkAEEAKKADEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 566 EDLEPRFNNSSLKIEELQEALRK--------KEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERD 637
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAkikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDK 1674
|
410 420
....*....|....*....|..
gi 1622960298 638 RLFHSLEKEYEKTKSQREMEEK 659
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKK 1696
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-573 |
1.08e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 167 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQ---------------SDSIEDPN 231
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieklkkenqsyKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 232 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD----KV 307
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsletQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 308 SKLEGQVESYKKKLED-----------LGDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLEtykrqvvelqNRL 376
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQkqkelkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----------SKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 377 SEESKKADKLDFEYKR--LKEKVDSLQKEKDRLRTERDSLKETIEELrcvqaqegqlttqglmplgsQESSDSLAAEI-- 452
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEK--------------------QELIDQKEKEKkd 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 453 VTPEIREKLIRLQHENKMLKLNQEgsDNEKialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKA 532
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKK--ENEK---LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960298 533 EDAISVLLK----------------------KKLEEHLEKLHEANNELQKKRAIIEDLEPRFN 573
Cdd:TIGR04523 676 DDIIELMKDwlkelslhykkyitrmirikdlPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-432 |
1.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 254 RLEAAKDDYRIRCEELEKEISELRQQ----NDELTTLADEAQSLKDEIDVLRhssdkvSKLEGQVESYKKKL-------- 321
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELR------AELEAQKEELAELLralyrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 322 ----------EDLGDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFE-- 389
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAErq 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622960298 390 --YKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLT 432
Cdd:COG4942 199 klLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-633 |
1.45e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 354 KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtt 433
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 434 qglmplgsqessdslaaeivtpeiREKLIRLQHE-NKMLKLNQEGSDNEKIALL--QSLLDDANLRKNELETENRLVNQR 510
Cdd:COG4942 96 ------------------------RAELEAQKEElAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 511 LLEVQSQVEELQKslqdqgskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEprfNNSSLKIEELQEALRKKE 590
Cdd:COG4942 152 AEELRADLAELAA----------------LRAELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622960298 591 EEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQL 633
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-659 |
1.79e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 495 LRKNELETENRLVN-----QRLLEVQSQVEELQKSLQDQGSKAEDAISV----------LLKKKLEEHLEKLHEANNELQ 559
Cdd:TIGR02168 170 YKERRKETERKLERtrenlDRLEDILNELERQLKSLERQAEKAERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 560 KKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERY----------KKYLEKAKSVIRTLDPKQNQGAApEIQAL 629
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrlEQQKQILRERLANLERQLEELEA-QLEEL 328
|
170 180 190
....*....|....*....|....*....|
gi 1622960298 630 KNQLQERDRLFHSLEKEYEKTKSQREMEEK 659
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEA 358
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-421 |
2.30e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 162 NDAYVDLDRQLKKTTEELNEALSAKEEIAQrchELDMQVAALQEEKSSLLAENQVLM-ERLNQSDSIEDPNSPAGRRHLQ 240
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 241 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 320
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 321 LED-LGDLRRQVKLLEEKNTVYMQNTVSLE-----EELRKANAA----------------------RSQLETYKRQVVEL 372
Cdd:TIGR04523 536 KESkISDLEDELNKDDFELKKENLEKEIDEknkeiEELKQTQKSlkkkqeekqelidqkekekkdlIKEIEEKEKKISSL 615
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622960298 373 QNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 421
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
260-370 |
2.76e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 260 DDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNt 339
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1622960298 340 vymQNTVSLEEELRKANAARSQLETYKRQVV 370
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
482-659 |
2.91e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 482 KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHLEKLHEANNELQKK 561
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 562 RAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERykkyLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRLFH 641
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELA 375
|
170
....*....|....*...
gi 1622960298 642 SLEKEYEKTKSQREMEEK 659
Cdd:COG1196 376 EAEEELEELAEELLEALR 393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
267-657 |
3.85e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 267 EELEKEISELRQQNDELTTLADEAQSLKD----EIDVLRHSSDKVS----KLEGQVESYKKKLEDLGDLRRQVKLLEEKN 338
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNrdiqRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 339 TVYMQNTVSLEEELRKANAARSQLetykrQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETI 418
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKL-----QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 419 EELRCVQAQEGQLTTQglmplgsqessdslaAEIVTPEIREKLIRLQHENKMLKlnqegSDNEKIALLQSLLDDANLRKN 498
Cdd:TIGR00606 867 NELKSEKLQIGTNLQR---------------RQQFEEQLVELSTEVQSLIREIK-----DAKEQDSPLETFLEKDQQEKE 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 499 EL----ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKlEEHLEKLHEANNELQKKRAIIEDlEPRFNN 574
Cdd:TIGR00606 927 ELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINE-DMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 575 SSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDR---LFHSLEKEYEKTK 651
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvLALGRQKGYEKEI 1084
|
....*.
gi 1622960298 652 SQREME 657
Cdd:TIGR00606 1085 KHFKKE 1090
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
263-574 |
4.34e-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: 40.73 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 263 RIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTVYM 342
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 343 QNTVSLEEELRKANAARSQLEtYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELR 422
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELK-EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 423 CVQAQEGQLTTQglmplgsQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELET 502
Cdd:pfam02463 870 QELLLKEEELEE-------QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960298 503 ENRLVNQRLLEVQSQVEELQKSLQDQGSKAE-------DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNN 574
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGkvnlmaiEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
374-569 |
4.39e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.07 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 374 NRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEE------LRCVQAQEGQLTTQGLMPLGSQESSDS 447
Cdd:COG5414 200 IEIEEVEKKVDDLLEKDMKAESVSVVLKDEKELARQERVSSWENFKEepgeplSRPALKKEKQGAEEEGEEGMSEEDLDV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 448 LAAEIVTPEIREKLIRLQHENKMlklNQEGSDNEKiallQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQD 527
Cdd:COG5414 280 GAAEIENKEVSEGDKEQQQEEVE---NAEAHKEEV----QSDRPDEIGEEKEEDDENEENERHTELLADELNELEKGIEE 352
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622960298 528 QGSKAEDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLE 569
Cdd:COG5414 353 KRRQMESATNPILQKRFESQLNVLLK---ELELKRKQLEMEE 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
278-553 |
5.39e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 278 QQNDELTTLADEAQ----SLKDEIDVLRHSSDKVSKLEgqvesyKKKLEDLGDLRrqvKLLEEKNTVYMQNTVsLEEELR 353
Cdd:PLN02939 111 IDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNILLLN------QARLQALEDLE---KILTEKEALQGKINI-LEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 354 KANAaRSQLETYKRQVVELQNRLSEesKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTT 433
Cdd:PLN02939 181 ETDA-RIKLAAQEKIHVEILEEQLE--KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-AELIEVAETE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 434 QGLMPLGSQESsdslAAEIVTPEIREKLIRLQHEnkMLKLNQEGSDN--EKIALLQSLLDDAnlrKNELEtENRLVNQRL 511
Cdd:PLN02939 257 ERVFKLEKERS----LLDASLRELESKFIVAQED--VSKLSPLQYDCwwEKVENLQDLLDRA---TNQVE-KAALVLDQN 326
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622960298 512 LEVQSQVEELQKSLQDQG-SKAEDAISVLLKKK---LEEHLEKLHE 553
Cdd:PLN02939 327 QDLRDKVDKLEASLKEANvSKFSSYKVELLQQKlklLEERLQASDH 372
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
160-403 |
5.77e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 160 AGNDAYVDLDRQLKKTTEELNEALSA-KEEIAQR-------CHELDMQVAALQEEKSSLLAENQVLMERLnqsDSIEDPN 231
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKlRNELLIRgateglcVHSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 232 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR----IRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhssDKV 307
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 308 SKLEGQVES---YKKKLEDLGDLRRQVKLLEEKNTVYMQNTvsleeelrkanaaRSQLETYKRQVVELQ---NRLSEESK 381
Cdd:PLN02939 334 DKLEASLKEanvSKFSSYKVELLQQKLKLLEERLQASDHEI-------------HSYIQLYQESIKEFQdtlSKLKEESK 400
|
250 260
....*....|....*....|..
gi 1622960298 382 KadkldfeyKRLKEKVDSLQKE 403
Cdd:PLN02939 401 K--------RSLEHPADDMPSE 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
133-661 |
8.62e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 133 IMMMEESVQHVVMTAIQELMSK----ESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKS 208
Cdd:TIGR02169 281 IKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 209 SLLAENQVLMERLNQSDSiedpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD 288
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDK------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 289 EAQSLKDEIDVLRhssDKVSKLEGQVESYKkklEDLGDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQ 368
Cdd:TIGR02169 435 KINELEEEKEDKA---LEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 369 vvelqNRLSEESKKAD------------KLDFEYKRLKEKVDSLQKEKDRLRTERDSlKETIEELRCVQAqeGQLTTQGL 436
Cdd:TIGR02169 509 -----GRAVEEVLKASiqgvhgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVA-KEAIELLKRRKA--GRATFLPL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 437 MPLGSQESSDSLAAE-------------------IVTPEIREKLI--------RLQHENKMLKLNQE----------GSD 479
Cdd:TIGR02169 581 NKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYVFGDTLVvedieaarRLMGKYRMVTLEGElfeksgamtgGSR 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 480 NEKIALLQSLLDDANL-----RKNELETENRLVNQRLLEVQSQVEELQKSLQDqgskaedaisvlLKKKLEEHLEKLHEA 554
Cdd:TIGR02169 661 APRGGILFSRSEPAELqrlreRLEGLKRELSSLQSELRRIENRLDELSQELSD------------ASRKIGEIEKEIEQL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960298 555 NNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQ 634
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS 808
|
570 580
....*....|....*....|....*..
gi 1622960298 635 ERDRLFHSLEKEYEKTKSQREMEEKYI 661
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEI 835
|
|
| |
