|
Name |
Accession |
Description |
Interval |
E-value |
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
10-180 |
3.20e-73 |
|
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: 238.58 E-value: 3.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 10 RDFLSGSLATWALGLAGLVGEAEDSEGEEEEEEEEPPLWLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMlRGLDGPAAW 89
Cdd:cd22230 1 EEFMSGALVTWALGFEGLVGEEEDSLGFPEEEEEEGTLDAEKRFLRLSNGDLLNRVMGIIDPSPRGGPRM-RGDDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 90 RVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQS 169
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEELQQLILSPPPDLQVMGRDPFTEEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQA 159
|
170
....*....|.
gi 1034573209 170 ELAAAIQEVTQ 180
Cdd:cd22230 160 ELAEAIQEVTQ 170
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-180 |
3.54e-49 |
|
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: 170.85 E-value: 3.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 12 FLSGSLATWALGLAGLVGeaedsegeeeeeeeepplwLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMlRGLDGPAAWRV 91
Cdd:cd22223 1 FLSSPLVTWAKTFADDGS-------------------AELSYTDLVDGVFLNNVMLQIDPRPFSEVSN-RNVDDDVNARI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 92 WNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSEL 171
Cdd:cd22223 61 QNLDLLLRNIKSFYQEVLQQLIVMKLPDILTIGREPESEQSLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHAL 140
|
....*....
gi 1034573209 172 AAAIQEVTQ 180
Cdd:cd22223 141 VACIQEVTD 149
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
53-180 |
4.71e-23 |
|
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: 96.40 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 53 FLRLSDGALLLRVLGIIAPSSRGgPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEA 132
Cdd:cd22229 30 YVALVDGVFLNEVMLQINPKSSN-QRVNKKVNNDASLRIQNLSILVKQIKLYYQETLQQLIMMSLPNVLVLGRNPLSEQG 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034573209 133 VEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ 180
Cdd:cd22229 109 TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEVTH 156
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
53-180 |
1.36e-20 |
|
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: 89.21 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 53 FLRLSDGALLLRVLGIIAPSSRGgPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEA 132
Cdd:cd22228 27 YMDLVDGVFLNKIMLQIDPRPTN-QRVNKHVNNDVNLRIQNLTILVRHIKTYYQEVLQQLIVMNLPNVLMIGKDPLSGKS 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034573209 133 VEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ 180
Cdd:cd22228 106 MEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEVTH 153
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
56-180 |
1.82e-19 |
|
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: 85.79 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 56 LSDGALLLRVLGIIAPSSRGGPRmLRGLDGPAAWRV-W-NLNHLWGRLRDFYQEEL-QLLILSPPPDLQTLGFDPlSEEA 132
Cdd:cd22211 23 LSDGVVLAEILSQIDPSYFDSEW-LESRDSSDNWVLkLnNLKKLYRSLSKYYREVLgQQLSDLPLPDLSAIARDG-DEEE 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034573209 133 VEQLegvLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ 180
Cdd:cd22211 101 IVKL---LELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
56-178 |
3.46e-14 |
|
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: 70.74 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 56 LSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAA-WR--VWNLNHLWGRLRDFYQEEL-QLLILSPPPDLQTLGfdplSEE 131
Cdd:cd22222 23 LSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDnWRlkVSNLKKILKGIVDYYSEVLgQQISGFTMPDVNAIA----EKE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034573209 132 AVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEV 178
Cdd:cd22222 99 DPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQEL 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
718-952 |
6.42e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV 797
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 798 EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEka 877
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE-- 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034573209 878 vvrgkELGDRLEHLQRELEQAALERQEFLREKESQHQRyQGLEQRLEAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:COG1196 411 -----ALLERLERLEEELEELEEALAELEEEEEEEEEA-LEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-952 |
3.39e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 259 QLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAG-RLPRLQEELR 337
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 338 RCRERLQAAEAyksQLEEERVLSGVLEASKALLEEQLEAARercARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAE 417
Cdd:TIGR02168 348 ELKEELESLEA---ELEELEAELEELESRLEELEEQLETLR---SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 418 ENVELELELQR------SLEPPPGSPGEAPLAGAAPSLQDEVREAEAgRLRTLERENRELRGLLQVLQGQPGGQHPLLEA 491
Cdd:TIGR02168 422 EIEELLKKLEEaelkelQAELEELEEELEELQEELERLEEALEELRE-ELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 492 PRE--DPVLPVLEEAPQTPVAFDHSPQGLvqKARDGGPQALDLA-PPALDSVLEASAECPQAPDSDPQEAESPLQAAAMD 568
Cdd:TIGR02168 501 LEGfsEGVKALLKNQSGLSGILGVLSELI--SVDEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 569 PQASDWSPQESGSPVETQEsPEKAGRRSSLQSPASVAPPQGPG--------TKIQAPQLLGGETEGREA---PQGELVpe 637
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYllggvlvvDDLDNALELAKKLRPGYRivtLDGDLV-- 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 638 AWGLRQEGpehkpGPSEPSSVQLEEQegpnqgldlatgqAEAREHDQRLEGTvrdpawqkpqqksegalevqvwegpipG 717
Cdd:TIGR02168 656 RPGGVITG-----GSAKTNSSILERR-------------REIEELEEKIEEL---------------------------E 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV 797
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 798 EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKA 877
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034573209 878 VVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEaELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSEELRELESKRSELRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
725-952 |
3.47e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 725 AEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQEL 804
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 805 ESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKEL 884
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034573209 885 GDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALmELKTRALQLEEEL 952
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELL 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
738-952 |
1.47e-11 |
|
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: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 738 RRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEA 817
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 818 LAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQ 897
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034573209 898 AALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
725-951 |
5.33e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 725 AEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQEL 804
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 805 ESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKEL 884
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034573209 885 GDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEE 951
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
718-952 |
7.07e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREaeaqawEQARLREAV 797
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA------EIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 798 EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEgrqhleeaererreKEALQAELEKA 877
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE--------------LEDLRAELEEV 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034573209 878 VVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLeAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
256-805 |
9.11e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 256 LALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALS--GQAKRAELYREEAEALRERAGRLP--- 330
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEleLEEAQAEEYELLAELARLEQDIARlee 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 331 ----------RLQEELRRCRERLQAAEAYKSQLEEER-VLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLG 399
Cdd:COG1196 310 rrreleerleELEEELAELEEELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 400 EAHAELDSLRHQVDQLAEENVELELELQRSLEpppGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQ 479
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 480 gQPGGQHPLLEAPREDPVLPVLEEAPQtpvafdHSPQGLVQKARDGGPQA--LDLAPPALDSVLEASAECPQAPDSDPQE 557
Cdd:COG1196 467 -ELLEEAALLEAALAELLEELAEAAAR------LLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 558 AESPLQAAAMDPQASDWspqESGSPVETQESPEKAGRRSSLqspasvappqgPGTKIQAPQLLggetegREAPQGELVPE 637
Cdd:COG1196 540 LEAALAAALQNIVVEDD---EVAAAAIEYLKAAKAGRATFL-----------PLDKIRARAAL------AAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 638 AWGLRQEGPEHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKPQQKSEGALEVQvwegpipg 717
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL-------- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV 797
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
....*...
gi 1034573209 798 EAAGQELE 805
Cdd:COG1196 752 ALEELPEP 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
725-947 |
2.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 725 AEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQEL 804
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 805 ESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKEL 884
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034573209 885 GDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQ 947
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
717-952 |
1.54e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 717 GESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREA 796
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 797 VEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEK 876
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034573209 877 AVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-480 |
2.94e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 255 HLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQAL-----SGQAKRAELYREEAEALRERAGRL 329
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 330 PRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLR 409
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034573209 410 HQVDQLAEENVELELELQRSLEpppgsPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQG 480
Cdd:COG1196 466 AELLEEAALLEAALAELLEELA-----EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-481 |
6.21e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 283 DSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEE---LRRCRERLQAAEAYKSQLEEErvl 359
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDAS--- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 360 SGVLEAskalLEEQLEAARERCARLHETQREnllLRTRLGEAHAELDSLRHQVDQlaeenveleleLQRSLEPPPGSPGE 439
Cdd:COG4913 684 SDDLAA----LEEQLEELEAELEELEEELDE---LKGEIGRLEKELEQAEEELDE-----------LQDRLEAAEDLARL 745
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034573209 440 APLAGAAPSLQDEVREAEAGRLR-TLERENRELRGLLQVLQGQ 481
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELReNLEERIDALRARLNRAEEE 788
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
56-178 |
1.56e-06 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 48.94 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 56 LSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAA-WR--VWNLNHLWGRLRDFYQEELQLLILSPP-PDLQTLG--FDPls 129
Cdd:pfam19047 25 LTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDnWRlkVSNLKKILQSVVDYYQDVLGQQISDFLlPDVNLIGehSDP-- 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034573209 130 eeavEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEV 178
Cdd:pfam19047 103 ----AELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQEL 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
746-952 |
1.80e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 746 DELEAQARKLEAQNTEAAR---LSKELAQARRAEAEAHREAEAQawEQARLREAVEAAGQELESASQEREALVEALAAAG 822
Cdd:COG1196 196 GELERQLEPLERQAEKAERyreLKEELKELEAELLLLKLRELEA--ELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 823 RERRQWEREGSRLRAQSEAAEERMQVLEsEGRQHLEEAERERRE-KEALQAELEKAVVRGKELGDRLEHLQRELEQAALE 901
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEErLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034573209 902 RQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
89-178 |
5.58e-06 |
|
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: 47.15 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 89 WR--VWNLNHLWGRLRDFYQEELQLLILSPP-PDLQTLG--FDPLseeaveQLEGVLRLLLGASVQCEHRELFIRHIQGL 163
Cdd:cd22225 58 WRikMSNLKKILQGIVDYYHEFLDQQISEFLlPDLNRIAehSDPV------ELGRLLQLILGCAVNCEKKQEHIQNIMTL 131
|
90
....*....|....*
gi 1034573209 164 SLEVQSELAAAIQEV 178
Cdd:cd22225 132 EESVQHVVMTAIQEL 146
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-414 |
7.88e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 166 EVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPS 245
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 246 RAPAEGPSHHLALQ---------LANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYR 316
Cdd:TIGR02168 775 EELAEAEAEIEELEaqieqlkeeLKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 317 EEAEALRERagrlprLQEELRRCRERLQAAEAYKSQLEEERVLsgvLEASKALLEEQLEAARERcarLHETQRENLLLRT 396
Cdd:TIGR02168 855 ESLAAEIEE------LEELIEELESELEALLNERASLEEALAL---LRSELEELSEELRELESK---RSELRRELEELRE 922
|
250
....*....|....*...
gi 1034573209 397 RLGEAHAELDSLRHQVDQ 414
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDN 940
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
256-427 |
1.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 256 LALQLANAKAQLRRLRQELEEKAELlldsQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEE 335
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 336 LRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENL-LLRTRLGEAHAELDSLRHQVDQ 414
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaELEEELEEAQEELEELEEELEQ 231
|
170
....*....|...
gi 1034573209 415 LAEENVELELELQ 427
Cdd:COG4717 232 LENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-404 |
1.09e-05 |
|
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: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 262 NAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSG--------------QAKRAELyREEAEALRERAG 327
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaEREIAEL-EAELERLDASSD 685
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034573209 328 RLPRLQEELRRCRERLQAAEAYKSQLEEERvlsGVLEASKALLEEQLEAARERCARLHETQRE--NLLLRTRLGEAHAE 404
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERFAAALGD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
728-947 |
1.37e-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: 49.28 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 728 EALREEVAQLRR-KAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELES 806
Cdd:TIGR02168 213 ERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 807 ASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGD 886
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034573209 887 RLEHLQRELEQAALERQEFLREKESQHQRYQGLE---QRLEAELQAAATSKEEALMELKTRALQ 947
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
487-666 |
1.98e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 487 PLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQAlDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAA 566
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR-RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 567 MDPQASDWSPQES-GSPVETQESPEKAGRRSSLQSPASVAP---------PQGPGTKIQAPQLLGGETEGREAPQGElvP 636
Cdd:PHA03247 2818 LPPAASPAGPLPPpTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRS--T 2895
|
170 180 190
....*....|....*....|....*....|
gi 1034573209 637 EAWGLRQEGPEHKPGPSEPSSVQLEEQEGP 666
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
725-952 |
2.07e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 725 AEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQ------------AR 792
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeevSR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 793 LREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMqvlesegrqhleeaererrekEALQA 872
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK---------------------EELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 873 ELEKAVVRGKELGDRLEHLQRELEqaalERQEFLREkesqhqryqgLEQRLEaELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERD----ELEAQLRE----------LERKIE-ELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
724-954 |
2.20e-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: 48.51 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 724 VAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQE 803
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 804 LESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVL-----ESEGRQHLEEAERERREKEALQAELEKAV 878
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 879 VRGK--ELGDRLEHLQRELEQAALERQEFLREKESQ----HQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:TIGR02168 398 LNNEieRLEARLERLEDRRERLQQEIEELLKKLEEAelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
..
gi 1034573209 953 FQ 954
Cdd:TIGR02168 478 DA 479
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-411 |
2.98e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 257 ALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAK---RAELYREEAEaLRERAGRLPRLQ 333
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeqlEREIERLERE-LEERERRRARLE 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034573209 334 EELRRCRERLQA-AEAYKSQLEEervlsgvLEASKALLEEQLEAARERCARLHETQREnllLRTRLGEAHAELDSLRHQ 411
Cdd:COG4913 366 ALLAALGLPLPAsAEEFAALRAE-------AAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
292-956 |
3.32e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 292 EAEIRRLRQEAQALSGQAKRAELYREEAEALR---------ERAGRLPRLQEELRRCRERLQAAEAYKsqLEEERVLSGV 362
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKaeearkaedAKRVEIARKAEDARKAEEARKAEDAKK--AEAARKAEEV 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 363 LEASKalLEEQLEAARERCARLHETQRENLLLR----TRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSP- 437
Cdd:PTZ00121 1188 RKAEE--LRKAEDARKAEAARKAEEERKAEEARkaedAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHf 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 438 --GEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPggqhpllEAPREDPVLPVLEEAPQTPVAFDHSP 515
Cdd:PTZ00121 1266 arRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE-------EAKKADEAKKKAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 516 QGLVQKARDGGPQAldlapPALDSVLEASAECPQAPDSDPQEAESplQAAAMDPQAsdwspQESGSPVETQESPEKAGRR 595
Cdd:PTZ00121 1339 EEAKKAAEAAKAEA-----EAAADEAEAAEEKAEAAEKKKEEAKK--KADAAKKKA-----EEKKKADEAKKKAEEDKKK 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 596 SSLQSPASVAPPQGPGTKIQAPQLLGGETEGREAPQGELVPEAwglRQEGPEHKPgpSEPSSVQLEEQEGPNQGLDLATG 675
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKK--AEEAKKKAEEAKKADEAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 676 QAEAREHDQRLEGTVR--DPAWQKPQQKSEgALEVQVWEGPIPGESLASGVAEQEALREEVAQLRRKAEAL--GDELEA- 750
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKkaDEAKKAAEAKKK-ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKa 1560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 751 -------QARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAW----EQARLREAVEAAGQELESASQEREALVEALA 819
Cdd:PTZ00121 1561 eekkkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 820 AAGRERRQWER-----EGSRLRAQSEA---------------AEERMQVLESEGRQHLEEAERERREKEALQAELEKAVV 879
Cdd:PTZ00121 1641 KEAEEKKKAEElkkaeEENKIKAAEEAkkaeedkkkaeeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 880 RGKELGDR---LEHLQRELEQAALERQEFLREKES----QHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLE--- 949
Cdd:PTZ00121 1721 LKKAEEENkikAEEAKKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkki 1800
|
....*..
gi 1034573209 950 EELFQNF 956
Cdd:PTZ00121 1801 KDIFDNF 1807
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-901 |
4.15e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 726 EQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELE 805
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 806 SASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELG 885
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170
....*....|....*.
gi 1034573209 886 DRLEHLQRELEQAALE 901
Cdd:TIGR02169 476 EEYDRVEKELSKLQRE 491
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
429-689 |
7.36e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.98 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 429 SLEPPPGSPGEAPLAGAAPSLQDEVREAeAGRLR------TLERENRELRGLLQVLQGQPGGQHPLLEA------PREDP 496
Cdd:PHA03378 693 TMQPPPRAPTPMRPPAAPPGRAQRPAAA-TGRARppaaapGRARPPAAAPGRARPPAAAPGRARPPAAApgrarpPAAAP 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 497 VLPVLEEAPQTPVAFDHSPQG--LVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESP---LQAAAMDPQA 571
Cdd:PHA03378 772 GAPTPQPPPQAPPAPQQRPRGapTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPslkKPAALERQAA 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 572 SDWSPQ-ESGSPVETQESP---EKAGRRSSLQSPASVAPPQGPGTKIQAPQLLGGETEG-REAPQGELVPEAWGLRQEGP 646
Cdd:PHA03378 852 AGPTPSpGSGTSDKIVQAPvfyPPVLQPIQVMRQLGSVRAAAASTVTQAPTEYTGERRGvGPMHPTDIPPSKRAKTDAYV 931
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034573209 647 EHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGT 689
Cdd:PHA03378 932 ESQPPHGGQSHSFSVIWENVSQGQQQTLECGGTTKQERAMLGT 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-471 |
9.02e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 130 EEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ--PGAGVVLALSGPDPGELAPAELEMLSR 207
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaaARLLLLLEAEADYEGFLEGVKAALLLA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 208 SLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAE 287
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 288 VQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEE-ERVLSGVLEAS 366
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGsRRELLAALLEA 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 367 KALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGspgEAPLAGAA 446
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE---LLEEEALE 754
|
330 340
....*....|....*....|....*
gi 1034573209 447 PSLQDEVREAEAGRLRTLERENREL 471
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEAL 779
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
286-398 |
1.31e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 286 AEVQGLEAEIRRLRQEAQALSgqakraelyREEAEALRERAGrlpRLQEELRRCRERLQAAEAyksQLEEERVLSGVLEA 365
Cdd:COG0542 411 EELDELERRLEQLEIEKEALK---------KEQDEASFERLA---ELRDELAELEEELEALKA---RWEAEKELIEEIQE 475
|
90 100 110
....*....|....*....|....*....|...
gi 1034573209 366 SKALLEEQLEAARERCARLHETQRENLLLRTRL 398
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
216-620 |
1.37e-04 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 46.00 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 216 LARERDLGAQRLA--------ELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAE 287
Cdd:COG1020 904 VAREDAPGDKRLVayvvpeagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 288 VQGLEAEIRRLRQEAQALSGQAKRAE----------LYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEER 357
Cdd:COG1020 984 AEEEEEEAALALLLLLVVVVGDDDFFffggglglllLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPL 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 358 VLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSP 437
Cdd:COG1020 1064 AAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVA 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 438 GEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQG 517
Cdd:COG1020 1144 LAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 518 LVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQASDWSPQESGSPVETQESPEKAGRRSS 597
Cdd:COG1020 1224 LAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLAL 1303
|
410 420
....*....|....*....|...
gi 1034573209 598 LQSPASVAPPQGPGTKIQAPQLL 620
Cdd:COG1020 1304 LLLLALALALLLLLLLLLALLLL 1326
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-951 |
1.63e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 261 ANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEirrlrQEAQALSGQAKRAELYREEAEALRERAGRLP---RLQEELR 337
Cdd:PTZ00121 1060 AEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEAT-----EEAFGKAEEAKKTETGKAEEARKAEEAKKKAedaRKAEEAR 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 338 RCRERLQAAEAYKSqlEEERVLSGVLEASKALLEEQLEAARErcARLHETQRENLLLRtRLGEAHAELDSLRhqVDQLAE 417
Cdd:PTZ00121 1135 KAEDARKAEEARKA--EDAKRVEIARKAEDARKAEEARKAED--AKKAEAARKAEEVR-KAEELRKAEDARK--AEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 418 ENVELELELQRSLEpppgspgEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEA--PRED 495
Cdd:PTZ00121 1208 AEEERKAEEARKAE-------DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAeeARKA 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 496 PVLPVLEE---APQTPVAFDHSPQGLVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQAS 572
Cdd:PTZ00121 1281 DELKKAEEkkkADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 573 DWSPQESGSPVETQESPEKA---GRRSSLQSPASVAPPQGPGTKIQAPQLLGGETEGREAPQ----GELVPEAWGLRQEG 645
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKAdaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEakkkAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 646 PEHKPgpSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVR-DPAWQKPQQKSEGALEvqvwegpipgeslASGV 724
Cdd:PTZ00121 1441 EEAKK--ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADE-------------AKKA 1505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 725 AEQEALREEV--AQLRRKAEALGDELEAQaRKLEAQNTEAARLSKELAQARRAEAEAHREAEaqawEQAR---------L 793
Cdd:PTZ00121 1506 AEAKKKADEAkkAEEAKKADEAKKAEEAK-KADEAKKAEEKKKADELKKAEELKKAEEKKKA----EEAKkaeedknmaL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 794 REAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQV--LESEGRQHLEEAERERREKEALQ 871
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 872 AELEKAVVRGKELGDRLEHLQRElEQAALERQEFLREKESQHQRYQGLEQRLEAEL-QAAATSKEEALMELKTRALQLEE 950
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkKAEELKKAEEENKIKAEEAKKEA 1739
|
.
gi 1034573209 951 E 951
Cdd:PTZ00121 1740 E 1740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
259-441 |
2.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 259 QLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALsgQAKRAELYREEAEALRE--RAGRLPRLQ--- 333
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLRAlyRLGRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 334 ------EELRR-------CRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARL--HETQRENLL--LRT 396
Cdd:COG4942 127 spedflDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeaLKAERQKLLarLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034573209 397 RLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAP 441
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-951 |
3.99e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 719 SLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVE 798
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 799 AAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAV 878
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034573209 879 VRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQgleQRLeAELQAAATSKEEALMELKTRALQLEEE 951
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELA---AEL-AELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
722-952 |
6.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 722 SGVAEQEalrEEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAG 801
Cdd:TIGR02169 163 AGVAEFD---RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 802 QELES--ASQEREALVEALAAAGRERRQWERE------GSRLRAQSE----AAEERMQVLESEGRQHLEEAERERREKEA 869
Cdd:TIGR02169 240 EAIERqlASLEEELEKLTEEISELEKRLEEIEqlleelNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 870 LQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEaLMELKTRALQLE 949
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEKLK 398
|
...
gi 1034573209 950 EEL 952
Cdd:TIGR02169 399 REI 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-908 |
7.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 728 EALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQ------------ARLRE 795
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAelerldassddlAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 796 AVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELE 875
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
170 180 190
....*....|....*....|....*....|...
gi 1034573209 876 KAVvrgKELGDRLEHLQRELEQAaleRQEFLRE 908
Cdd:COG4913 773 ERI---DALRARLNRAEEELERA---MRAFNRE 799
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-481 |
8.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 252 PSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEA-LRERAGRLP 330
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 331 RLQEELRRCRERL--QAAEAYKSQLEEERVL----SGVLEASKAL--LEEQLEAARERCARLHETQRENLLLRTRLGEAH 402
Cdd:COG4942 94 ELRAELEAQKEELaeLLRALYRLGRQPPLALllspEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034573209 403 AELDSLRHQVDQLAEENVELELELQRSLEpppgspgeaplagaapSLQDEVREAEAgRLRTLERENRELRGLLQVLQGQ 481
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLA----------------RLEKELAELAA-ELAELQQEAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-932 |
1.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 728 EALREEVAQLRRKAEAL------GDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQawEQARLREAVEAAG 801
Cdd:COG4913 238 ERAHEALEDAREQIELLepirelAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA--ELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 802 QELESASQEREALVEALAAAG--------RERRQWEREGSRLRAQSEAAEERMQVLE----SEGRQHLEEAERERREKEA 869
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034573209 870 LQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAAT 932
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-504 |
1.09e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 130 EEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSL 209
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 210 MGTLSKLARERDLGAQRLAELLLEREPLCLRpeapsRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQ 289
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 290 GLEAEIRRLRQEAQALSGQAKRA--ELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASK 367
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 368 ALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAP 447
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034573209 448 SLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEA 504
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
89-178 |
1.10e-03 |
|
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: 40.72 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 89 WR--VWNLNHLWGRLRDFYQEEL-QLLILSPPPDLQTLGfdplSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSL 165
Cdd:cd22226 62 WRlkISNLKKILKGILDYNHEILgQQINDFTLPDVNLIG----EHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEE 137
|
90
....*....|...
gi 1034573209 166 EVQSELAAAIQEV 178
Cdd:cd22226 138 SVQHVVMTAIQEL 150
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
283-377 |
2.82e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 283 DSQAEVQGLEAEIRRLRQE----AQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERV 358
Cdd:PRK11448 139 DPENLLHALQQEVLTLKQQlelqAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218
|
90 100
....*....|....*....|....*....
gi 1034573209 359 LSGVLEASK----------ALLEEQLEAA 377
Cdd:PRK11448 219 KEITDQAAKrlelseeetrILIDQQLRKA 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-407 |
3.37e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 213 LSKLARERDLGAQRLAELLLEREPLCLRPEAPSrapaEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLE 292
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLG----EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 293 AEIRRLRQEAQALSGQakraelyreeaeaLRERAGRLPRLQEELRRCRERLqaaEAYKSQLEEERVLSGVLEASKALLEE 372
Cdd:TIGR02169 329 AEIDKLLAEIEELERE-------------IEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190
....*....|....*....|....*....|....*
gi 1034573209 373 QLEAARERcarLHETQREnlllRTRLGEAHAELDS 407
Cdd:TIGR02169 393 KLEKLKRE---INELKRE----LDRLQEELQRLSE 420
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-414 |
3.61e-03 |
|
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: 40.29 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 258 LQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERA-GRLPRL--QE 334
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeEQLGNVrnNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 335 ELRRCRERLQAAEAYKSQLEEE-RVLSGVLEASKALLEEQLEAARERCARLHETQREnllLRTRLGEAHAELDSLRHQVD 413
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAERE 166
|
.
gi 1034573209 414 Q 414
Cdd:COG1579 167 E 167
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
283-409 |
3.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 283 DSQAEVQGLEAEIR-RLRQEAQALSGQAKRAELYREEAEALRERAgrlprlqEELRrcrerlQAAEAYKSQLEEERVLSG 361
Cdd:PRK02224 314 ARREELEDRDEELRdRLEECRVAAQAHNEEAESLREDADDLEERA-------EELR------EEAAELESELEEAREAVE 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034573209 362 VLEASKALLEEQLEAARERCARLhETQRENL-----LLRTRLGEAHAELDSLR 409
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDA-PVDLGNAedfleELREERDELREREAELE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
249-414 |
4.43e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 249 AEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAK--RAEL--YREEAEALRE 324
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetRDELkdYREKLEKLKR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 325 RAGRL----PRLQEELRRCRER-------LQAAEAYKSQLEEER-VLSGVLEASKALLE---EQLEAARERCARLHETQR 389
Cdd:TIGR02169 400 EINELkrelDRLQEELQRLSEEladlnaaIAGIEAKINELEEEKeDKALEIKKQEWKLEqlaADLSKYEQELYDLKEEYD 479
|
170 180
....*....|....*....|....*
gi 1034573209 390 EnllLRTRLGEAHAELDSLRHQVDQ 414
Cdd:TIGR02169 480 R---VEKELSKLQRELAEAEAQARA 501
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
172-571 |
4.98e-03 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 41.00 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 172 AAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSL----MGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRA 247
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALllppYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 248 PAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLR------------QEAQALSGQAKRAELY 315
Cdd:COG1020 981 APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLlllllllflaaaAAAAAAAAAAAAAAAA 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 316 REEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLR 395
Cdd:COG1020 1061 APLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRL 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 396 TRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLL 475
Cdd:COG1020 1141 LVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 476 QVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDP 555
Cdd:COG1020 1221 LLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLL 1300
|
410
....*....|....*.
gi 1034573209 556 QEAESPLQAAAMDPQA 571
Cdd:COG1020 1301 LALLLLLALALALLLL 1316
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-390 |
5.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 252 PSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALsGQAKRAELYREEAEALRERAGRLPR 331
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL-EKKYSEEEYEELREEYLELSRELAG 677
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 332 LQEELRRCRERLQAAEAYKSQLEEERVlsgvlEASKALLE-EQLEAARERCARLHETQRE 390
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELE-----EREKAKKElEKLEKALERVEELREKVKK 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
256-380 |
7.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 256 LALQLANAKAQLRRLRQEL---EEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRL 332
Cdd:COG4913 666 AEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034573209 333 QEELrRCRERLQAAEAYKSQLEEERVLSGVLEASKAL---LEEQLEAARER 380
Cdd:COG4913 746 ELRA-LLEERFAAALGDAVERELRENLEERIDALRARlnrAEEELERAMRA 795
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
256-414 |
8.31e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 256 LALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEE 335
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPN 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 336 ---LRRCRERLQAAEAYKSQlEEERVLSG------VLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELD 406
Cdd:COG3206 290 hpdVIALRAQIAALRAQLQQ-EAQRILASleaeleALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
....*...
gi 1034573209 407 SLRHQVDQ 414
Cdd:COG3206 369 SLLQRLEE 376
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
256-414 |
9.38e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 39.33 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 256 LALQLANAKAQLRRLrqeleekaellldsQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALREragRLPRLQEE 335
Cdd:pfam00529 56 YQAALDSAEAQLAKA--------------QAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA---AVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 336 LRRCRERLQAAEAY-------KSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQREnlLLRTRLGEAHAELDSL 408
Cdd:pfam00529 119 LAQAQIDLARRRVLapiggisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQA--EVRSELSGAQLQIAEA 196
|
....*.
gi 1034573209 409 RHQVDQ 414
Cdd:pfam00529 197 EAELKL 202
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
789-947 |
9.93e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.55 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 789 EQARLR----EAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRA-QSEAAEERMQVLESEGRQHLEEAERE 863
Cdd:pfam15709 359 EQRRLQqeqlERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRlQLQAAQERARQQQEEFRRKLQELQRK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034573209 864 RREKEALQAELEKAvvRGKELGDRL-EHLQRELEQAALERQEFLREK-ESQHQRYQGLEQRLEAELQAAATSKEEALMEL 941
Cdd:pfam15709 439 KQQEEAERAEAEKQ--RQKELEMQLaEEQKRLMEMAEEERLEYQRQKqEAEEKARLEAEERRQKEEEAARLALEEAMKQA 516
|
....*.
gi 1034573209 942 KTRALQ 947
Cdd:pfam15709 517 QEQARQ 522
|
|
| |
