|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
611-804 |
2.68e-107 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 327.02 E-value: 2.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 611 YSQKDLDSAVEATQKENEV-------LRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQL 683
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEkeleineLKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 684 TADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQT 763
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 151556340 764 DALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLI 804
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
127-417 |
8.89e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 55.95 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 127 EPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSsqipesvenpeasrgPAPGSPECAREEHVHPWPSEESMPLGPMAPEQ- 205
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPS---------------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 206 PSGVVSQDTAEDPLSGTGGDSEGV--PGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHP 283
Cdd:PHA03307 163 ASDAASSRQAALPLSSPEETARAPssPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 284 GAQG------EETCGQAASSLRSGPVRLEFDFSDATGKRSPPLRKRGKalglkPPSRRPEARPGKatleagkgceltlrg 357
Cdd:PHA03307 243 ESSGcgwgpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS-----PRERSPSPSPSS--------------- 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 358 sdgpswdkPDDPDCNPAADSGEARPLEHPQSGQATEALSLSRQACSDDTPGTRAPARTPG 417
Cdd:PHA03307 303 --------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS 354
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-810 |
9.65e-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: 55.84 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLlemgkimdsfegtvYQVMEE-SQKQKELT--KAEMQKVLKEKAQ 682
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDlSSLEQEIEnvKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 683 LTADLHSMEKSFSDLFKRF--EKQKEVIEGYRTNEESLKKcVEDYIERVEKEAQKYQALKAQAEEKLRQASEEI----AQ 756
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVSR-IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRidlkEQ 848
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 151556340 757 VRSKAQTDALaLQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:TIGR02169 849 IKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
606-810 |
2.96e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 606 VDVLQYSQKDLDSAVEATQKEnevlrgkcaaLQERLLEMGKIMDsfegtvyQVMEESQKQKELTKAemQKVLKEKAQ-LT 684
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKE----------LKSKEKELKKLNE-------EKKELEEKVKDLTKK--ISSLKEKIEkLE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 685 ADLHSMEKSFSDLFKRFEKQKEVIegyrtNEESLKKCVEDYIERVEKEAQKYQALKA---QAEEKLRQASEEIAQVRSKa 761
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIKE- 604
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 151556340 762 qtdalalqavLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:TIGR04523 605 ----------IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
657-775 |
8.06e-07 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 49.12 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 657 QVMEESqkqkELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIegyrtNEESLKKCVEDYiervEKEAQKY 736
Cdd:smart00935 8 KILQES----PAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATL-----SEAAREKKEKEL----QKKVQEF 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 151556340 737 QALKAQAEEKLRQAS-EEIAQVRSKAQTdalALQAVLRKE 775
Cdd:smart00935 75 QRKQQKLQQDLQKRQqEELQKILDKINK---AIKEVAKKK 111
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
657-775 |
1.62e-06 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 49.06 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 657 QVMEESQKqkelTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIegyrTNEESLKKcvEDYIERVEKEAQKY 736
Cdd:COG2825 33 RILQESPE----GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATL----SEEERQKK--ERELQKKQQELQRK 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 151556340 737 QAlKAQAEEKLRQAsEEIAQVRSKAQTdalALQAVLRKE 775
Cdd:COG2825 103 QQ-EAQQDLQKRQQ-ELLQPILEKIQK---AIKEVAKEE 136
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-806 |
1.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 611 YSQKDLDSAVEATQKENEVLRGkcaalqERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVL------------K 678
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKA------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaeeakkaeedK 1674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 679 EKAQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVR 758
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 151556340 759 SKAQTDALALQAVLRKEQMRVHSlEKVVEQKTKENDELTRICDDLISK 806
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEK-EAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
135-603 |
3.02e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.94 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 135 PVSEDQPPGGPPSAPLVSLGPSSSSQI---PESVENPEASRGPAPGSPECAREEHVHPWPSEESMPLGPMAPEQPsgvvs 211
Cdd:PHA03307 35 LLSGSQGQLVSDSAELAAVTVVAGAAAcdrFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPP----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 212 qdtaedplsgtGGDSEGVPGPPARPASPcGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHPgaqgeetc 291
Cdd:PHA03307 110 -----------GPSSPDPPPPTPPPASP-PPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASS-------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 292 GQAASSLRSGPvrlefdfsDATGKRSPPLRKRGKALGLKPPSRRPEARPGKATLEAGKGCELTLRGSDGPSWDKPDDPDC 371
Cdd:PHA03307 170 RQAALPLSSPE--------ETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 372 NPAADSGEARPLEHPQSGQATEAL-SLSRQACSDDTPGTRAPARTPGAAgegwtTGSLGGSAPLSSPSSEPPTAPTNPTP 450
Cdd:PHA03307 242 SESSGCGWGPENECPLPRPAPITLpTRIWEASGWNGPSSRPGPASSSSS-----PRERSPSPSPSSPGSGPAPSSPRASS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 451 PTERGPEPTLDLNGEQ-FRDPAEVLGAGAELDYLEQFGAPSfkesalrkqslylnfdpllqDSPQGLTPSSSGRPRGLPV 529
Cdd:PHA03307 317 SSSSSRESSSSSTSSSsESSRGAAVSPGPSPSRSPSPSRPP--------------------PPADPSSPRKRPRPSRAPS 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 530 PSAGPLASEESPglmqtAGGFSLGLRARSVDKPSS---GSPPEAQLLDLDFPGAPGIPIPGLAPC-DLGPGAPLLPVG 603
Cdd:PHA03307 377 SPAASAGRPTRR-----RARAAVAGRARRRDATGRfpaGRPRPSPLDAGAASGAFYARYPLLTPSgEPWPGSPPPPPG 449
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
660-798 |
4.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 660 EESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDY-----IERVEKEAQ 734
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkkadeLKKAAAAKK 1418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151556340 735 KYQALKAQAEEKlRQASEEIAQVRSKAQTDALALQAvlrKEQMRVHSLEKVVEQKTKEnDELTR 798
Cdd:PTZ00121 1419 KADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKA---EEAKKAEEAKKKAEEAKKA-DEAKK 1477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
660-810 |
5.35e-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: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 660 EESQKQKELTKA--EMQKVLKEKAQLTADLHSMEKSFSDL---FKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQ 734
Cdd:TIGR02168 692 KIAELEKALAELrkELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151556340 735 KYQALKAQAEEKLRQASEEIAQVRS--KAQTDAL-ALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEelKALREALdELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
601-798 |
6.27e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 49.64 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 601 PVGPIVDVLQYSQKDLDsavEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQkQKELTKAEMQKVLKEK 680
Cdd:pfam05667 314 AATSSPPTKVETEEELQ---QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE-ELKEQNEELEKQYKVK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 681 AQLTADLHSMEksfsdlfkrfekqkeviegyrTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSK 760
Cdd:pfam05667 390 KKTLDLLPDAE---------------------ENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE 448
|
170 180 190
....*....|....*....|....*....|....*....
gi 151556340 761 AQtdalalqavLRKEQMRV-HSLEKVVEQKTKENDELTR 798
Cdd:pfam05667 449 SQ---------RKLEEIKElREKIKEVAEEAKQKEELYK 478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
606-810 |
8.12e-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: 49.73 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERllEMGKIMDSFEGtvYQVMEESQKQKELTKAEMQKVLKEKAQLTA 685
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER--QMAAIQGKNES--LEKVSSLTAQLESTKEMLRKVVEELTAKKM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 686 DLHSMEKSFSDLFKRFEKQKEVIEGyrTNEESLK---------------KCVEDYIERVEKEAqkyQALKAQAEEK---- 746
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEA--TNAEITKlrsrvdlklqelqhlKNEGDHLRNVQTEC---EALKLQMAEKdkvi 564
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151556340 747 --LRQASEEIAQVRSKAQTDALALQ---AVLRKE----QMRVHSLEKVVEQKTKENDEL-TRICDDLISKMKRI 810
Cdd:pfam15921 565 eiLRQQIENMTQLVGQHGRTAGAMQvekAQLEKEindrRLELQEFKILKDKKDAKIRELeARVSDLELEKVKLV 638
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
660-808 |
1.01e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 660 EESQKQKELTK--AEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEV-------IEGYRTNEESLKKCVEDYIERVE 730
Cdd:TIGR04523 357 ENSEKQRELEEkqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLnqqkdeqIKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 731 KEAQKYQALKAQAEEKlRQASEEIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMK 808
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVK-ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
722-775 |
2.00e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 44.74 E-value: 2.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 151556340 722 VEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKE 775
Cdd:cd06503 35 IAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAE 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
619-798 |
2.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 619 AVEATQKENEVLRgkcaALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLF 698
Cdd:PTZ00121 1232 AEEAKKDAEEAKK----AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 699 KRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLR--QASEEIAQVRSKAQTDALALQAVLRK-- 774
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeaEAAEEKAEAAEKKKEEAKKKADAAKKka 1387
|
170 180
....*....|....*....|....*
gi 151556340 775 -EQMRVHSLEKVVEQKTKENDELTR 798
Cdd:PTZ00121 1388 eEKKKADEAKKKAEEDKKKADELKK 1412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-798 |
4.02e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 659 MEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCvedyIERVEKEAQKYQA 738
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEE 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151556340 739 LKAQAEEKLRQASEEIAQVRSK---AQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTR 798
Cdd:COG1196 310 RRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
659-777 |
4.27e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.44 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 659 MEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSdlfKRFEKQKEVIEGY--------RTNEESL-------KKCVE 723
Cdd:pfam04012 20 AEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLE---RRLEQQTEQAKKLeekaqaalTKGNEELarealaeKKSLE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 151556340 724 DYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQM 777
Cdd:pfam04012 97 KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAV 150
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
662-810 |
4.85e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 662 SQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIEgyRTNEEslkkcvedyIERVEKEAQKYQALKA 741
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE--QLEEE---------LEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 151556340 742 QAEEKLRQASEEIAQVRS---KAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:COG4372 98 QAQEELESLQEEAEELQEeleELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
657-775 |
6.83e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 43.33 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 657 QVMEESQKqkelTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEEslkkcvedyiERVEKEAQKY 736
Cdd:pfam03938 9 KILEESPE----GKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKE----------QELQKKEQEL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 151556340 737 QALKAQAEEKLRQAS-EEIAQVRSKAQTdalALQAVLRKE 775
Cdd:pfam03938 75 QQLQQKAQQELQKKQqELLQPIQDKINK---AIKEVAKEK 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
614-754 |
7.50e-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: 44.92 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 614 KDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEE----SQKQKELTKA-EMQKVLKEKAQLTADLH 688
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNkEYEALQKEIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151556340 689 SMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEI 754
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
620-796 |
7.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 620 VEATQKENEvlrGKCAALQeRLLEMGKIMDSFEGTVYQVMEESQKQK--ELTKAEMQKVlkeKAQLTADLHSMEKSFSDL 697
Cdd:PTZ00121 1566 AEEAKKAEE---DKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKaeEAKKAEEAKI---KAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 698 FKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKA------QAEEKLRQASEE---IAQVRSKAQTDALAL 768
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKaeedekKAAEALKKEAEEakkAEELKKKEAEEKKKA 1718
|
170 180 190
....*....|....*....|....*....|.
gi 151556340 769 QAVLRKEQMR---VHSLEKVVEQKTKENDEL 796
Cdd:PTZ00121 1719 EELKKAEEENkikAEEAKKEAEEDKKKAEEA 1749
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
621-792 |
9.55e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 621 EATQKENEVLRGKCAALQERLLEMGKImdsfEGTVYQVMEESQKQKELTKAEMQKV----LKEKAQLTADLHSMEKSFSD 696
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKA----DEAKKKAEEDKKKADELKKAAAAKKkadeAKKKAEEKKKADEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 697 LfKRFEKQKEVIEGYRTNEESLKKCVE----DYIERVEKEAQKYQALKAQAEEKLRQASEeiaqVRSKAQTDALALQAVL 772
Cdd:PTZ00121 1443 A-KKADEAKKKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKKADE----AKKAAEAKKKADEAKK 1517
|
170 180
....*....|....*....|
gi 151556340 773 RKEQMRVHSLEKVVEQKTKE 792
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKAD 1537
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
121-289 |
1.17e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.75 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 121 PVPVNTEPPSEDMRPVSEDQP-------PGGPPSAPLVSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWPSE 193
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPaapaapaPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 194 ESMPLGPMAPEQPSGVVSQDTAED----PLSGTGGDSEGV-PGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSRED 268
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPApaatPPAGQADDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760
|
170 180
....*....|....*....|.
gi 151556340 269 TALTGPGEAAGATHPGAQGEE 289
Cdd:PRK07764 761 PPAPAPAAAPAAAPPPSPPSE 781
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
143-338 |
1.23e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.75 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 143 GGPPSAPLVSLGPSSSSQIPESVENPEASrgPAPGSPECAREEHVHPWPSEESmplGPMAPEQPSGVVSQDTAEDPLSGT 222
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAP--AAPAAPAAPAPAGAAAAPAEAS---AAPAPGVAAPEHHPKHVAVPDASD 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 223 GGDSEGVPGPPARPASPCGAPPGEKPlvdlPGAAPVGSMDATSREDTALTGPGEAAGATHPGAQGEETCGQAASSLRSGP 302
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAP----AAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740
|
170 180 190
....*....|....*....|....*....|....*.
gi 151556340 303 VRLEFDFSDATGKRSPPLRKRGKALGLKPPSRRPEA 338
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
614-799 |
1.42e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 614 KDLDSAVEATQKENEVLRGKCAALQERLLEMgkimDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKS 693
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLL----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 694 FSDL----------FKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQT 763
Cdd:TIGR02168 861 IEELeelieeleseLEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 151556340 764 --DALA------LQAVLRKEQMRVHSLEKVVEQKTKENDELTRI 799
Cdd:TIGR02168 941 lqERLSeeysltLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
607-799 |
1.75e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 607 DVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGkimdsfegtvyQVMEESQKQKELTKAEMQKVLKEKAQLTAD 686
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELR-----------LELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 687 LHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKA---QAEEKLRQASEEIAQVRSKAQT 763
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelaEAEEALLEAEAELAEAEEELEE 383
|
170 180 190
....*....|....*....|....*....|....*.
gi 151556340 764 DALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRI 799
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
618-810 |
2.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 618 SAVEATQKENEVLRGKCAALQERLLEMGKImdsfEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDL 697
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 698 FKRFEKQKEVIEG-----YRTNEES--------------------LKKCVEDYIERVEKEAQKYQALKAQAEEkLRQASE 752
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAE-LEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 753 EIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
614-798 |
2.61e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 614 KDLDSAVEATQKENEVLRGKCAALQERLLEmgkIMDSFEGTVYQVMEESQKQKEL-------------------TKAEMQ 674
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRE---LEERIEELKKEIEELEEKVKELkelkekaeeyiklsefyeeYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 675 KVLKEKAQLTADLHSMEKSFSDLFK---RFEKQKEVIEGYRTNEESLKKCVEDY---------------------IERVE 730
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYeeakakkeelerlkkrltgltPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 731 KEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVL-----------------RKEQMRVHSLE-KVVEQKTKE 792
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteehRKELLEEYTAElKRIEKELKE 470
|
....*.
gi 151556340 793 NDELTR 798
Cdd:PRK03918 471 IEEKER 476
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
144-244 |
2.87e-04 |
|
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.
Pssm-ID: 435117 [Multi-domain] Cd Length: 288 Bit Score: 43.59 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 144 GPPSAPLVSLGPSSSSQIPESVENPEASRGPA-----PGSPECAREEHVHPWPSEESMPLGPMAPEQPSGVVSQDTAEDP 218
Cdd:pfam16072 144 GPPGSVTTTSAGSGTTVINAGGQQPAAPAAPAypvapAAYPAQAPAAAPAPAPGAPQTPLAPLNPVAAAPAAAAGAAAAP 223
|
90 100
....*....|....*....|....*.
gi 151556340 219 LSGTGGDSEGVPGPPARPASPCGAPP 244
Cdd:pfam16072 224 VVAAAAPAAAAPPPPAPAAPPADAAP 249
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
121-283 |
2.88e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 121 PVPVNTEPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWpseESMPLGP 200
Cdd:PRK12323 430 PEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPW---EELPPEF 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 201 MAPEQPSGVVSQDTAEDPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGA 280
Cdd:PRK12323 507 ASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAA 586
|
...
gi 151556340 281 THP 283
Cdd:PRK12323 587 RLP 589
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
608-806 |
2.97e-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: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 608 VLQYSQKDLDSAVEATQKENEVLRGKcaalQERLLEMGKIMDSFEGTVYQVMEE-----SQKQKELTKA---EMQKVLKE 679
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKElksELKNQEKK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 680 KAQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVE---DYIERVEKEAQKY----QALKAQA---EEKLRQ 749
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqNEIEKLKKENQSYkqeiKNLESQIndlESKIQN 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 151556340 750 ASEEIAQVRSKAQTDALALQaVLRKEQmrvhslEKVVEQKTKENDELtricDDLISK 806
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKE-LLEKEI------ERLKETIIKNNSEI----KDLTNQ 448
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
610-799 |
3.06e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 610 QYSQKDLDSAVEATQKENEVLRGKCA--ALQERLLEMGKIMDSFEGTVyQVMEESQKQKELTKAEMQKVLKEKAQLTA-- 685
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKKEK-EEIEELEKELKELEIKREAEEEEEEELEKlq 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 686 -----DLHSMEKSFSDLFKRFEKQKEVIEGYRT--NEESLKKCVEDYIERVE----KEAQKYQALKAQAEEKLRQASEEI 754
Cdd:pfam02463 366 ekleqLEEELLAKKKLESERLSSAAKLKEEELElkSEEEKEAQLLLELARQLedllKEEKKEELEILEEEEESIELKQGK 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 151556340 755 AQVRSKAQTDALALQAVLRKEQMRVHSL---EKVVEQKTKENDELTRI 799
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLlkeTQLVKLQEQLELLLSRQ 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
607-810 |
3.09e-04 |
|
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: 44.65 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 607 DVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEG-----TVYQVMEESQKQkeltkaeMQKVLKEKA 681
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvclTDVTIMERFQME-------LKDVERKIA 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 682 QLTADLHS--MEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVE-----------------KEAQKYQALKAQ 742
Cdd:TIGR00606 810 QQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksktnelkseklqigTNLQRRQQFEEQ 889
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151556340 743 AEEKLRQASE---EIAQVRSKAQTDALALQAVLRKEQMRVHSLEkvvEQKTKENDELTRI---CDDLISKMKRI 810
Cdd:TIGR00606 890 LVELSTEVQSlirEIKDAKEQDSPLETFLEKDQQEKEELISSKE---TSNKKAQDKVNDIkekVKNIHGYMKDI 960
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
659-809 |
3.21e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 659 MEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSfsdlfkrfEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQA 738
Cdd:COG1340 121 LEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKA--------LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 739 LKAQ------AEEKLRQASEEIAQ--VRSKAQTDAL-----ALQAVLRK--EQMRVHSLEKVVEQKTKENDELTRICDDL 803
Cdd:COG1340 193 LHEEmielykEADELRKEADELHKeiVEAQEKADELheeiiELQKELRElrKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
....*.
gi 151556340 804 ISKMKR 809
Cdd:COG1340 273 FEKLKK 278
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
652-810 |
3.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 652 EGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfsdLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVeK 731
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK----EVKELEELKEEIEELEKELESLEGSKRKLEEKI-R 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151556340 732 EAQKYQALKAQAEEKLRQASEEIAQVRSKAQTdALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKELKELKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
|
| FCH_F-BAR |
cd07610 |
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ... |
658-796 |
4.84e-04 |
|
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.
Pssm-ID: 153294 [Multi-domain] Cd Length: 191 Bit Score: 41.94 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 658 VMEESQKQKELTKaEMQKVLKEKAQLTAD----LHSMEKSFSDL--------------FKRFEK-------------QKE 706
Cdd:cd07610 5 LEKRTELGLDLLK-DLREFLKKRAAIEEEyaknLQKLAKKFSKKpesgktslgtswnsLREETEsaatvheelseklSQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 707 VIEGYRT----NEESLKKCVEDyIERVEKEAQK-YQALKAQAEEKLRQASEEIAQVRSKA-QTDALALQAVLRKEQMRVH 780
Cdd:cd07610 84 IREPLEKvkedKEQARKKELAE-GEKLKKKLQElWAKLAKKADEEYREQVEKLNPAQSEYeEEKLNKIQAEQEREEERLE 162
|
170
....*....|....*.
gi 151556340 781 SLEKVVEQKTKENDEL 796
Cdd:cd07610 163 ILKDNLKNYINAIKEI 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
609-760 |
5.21e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 609 LQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEgtvyQVMEESQKQ-------KELTKAEMQKVLKEKA 681
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESEleallneRASLEEALALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 682 QLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERV----EKEAQKYQALKAQAEEKLRQASEEIAQV 757
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRL 977
|
...
gi 151556340 758 RSK 760
Cdd:TIGR02168 978 ENK 980
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
613-796 |
5.49e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 613 QKDLDSAVEATQKENEVLRGKCAALQERLLEMgkimdsfegtvyqvmeesQKQKELTKAEMQKVLKEKAQLTADLHSMEK 692
Cdd:pfam15905 179 QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST------------------EKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 693 SFSDLFkrfeKQKEVIEGYRTNEESLKKCVEdyiervekeaQKYQALKAQAE---EKLRQASEEIAQVRSKAQTDALALQ 769
Cdd:pfam15905 241 YKLDIA----QLEELLKEKNDEIESLKQSLE----------EKEQELSKQIKdlnEKCKLLESEKEELLREYEEKEQTLN 306
|
170 180
....*....|....*....|....*..
gi 151556340 770 AVLRkeqmrvhSLEKVVEQKTKENDEL 796
Cdd:pfam15905 307 AELE-------ELKEKLTLEEQEHQKL 326
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
609-755 |
5.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 609 LQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKImdsfegtvYQVMEESQKQKELTKAEmqkvlKEKAQLTADLH 688
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--------YSEEEYEELREEYLELS-----RELAGLRAELE 683
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 689 SMEKSFSDLFKRFEK---QKEVIEGYRTNEESLKKCvedyIERVEKEAQKYQALKAQAEEKLRQASEEIA 755
Cdd:PRK03918 684 ELEKRREEIKKTLEKlkeELEEREKAKKELEKLEKA----LERVEELREKVKKYKALLKERALSKVGEIA 749
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
636-793 |
6.23e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 636 ALQERLLEMGKIMDSFEgTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNE 715
Cdd:COG4372 32 QLRKALFELDKLQEELE-QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 716 ESLKKcvedYIERVEKEaqkYQALKAQaEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKEN 793
Cdd:COG4372 111 EELQE----ELEELQKE---RQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
614-806 |
6.27e-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: 43.52 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 614 KDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEgtvyQVMEESQKQ-KELTKAEMQKVLKEKAQLTADLHSMEK 692
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE----QLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 693 SFSD--------------LFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEE------------- 745
Cdd:TIGR02169 309 SIAEkereledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaetrdelk 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 746 ----KLRQASEEIAQVrskaQTDALALQAVLRKEQMRVHSLE---KVVEQKTKENDELTRICDDLISK 806
Cdd:TIGR02169 389 dyreKLEKLKREINEL----KRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKK 452
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
647-803 |
6.89e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 42.25 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 647 IMDSFEgtvyQVMEESQKQKELTKAE---------MQKVLKEKAQLTADLHSMEKSFSDLFK--RFE------KQK--EV 707
Cdd:pfam15934 36 IMDMFE----NKNEQEQQLKEFTVQNqrlacqidnLHETLKDRDHQIKQLQSMITGYSDISEnnRLKeeihdlKQKncVQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 708 IEGYRTNEESLKKCVEDYIERVEkeaqKYQALKAQAEEKlrqaSEEIAQVRSKAQT------DALALQAVLRKEQMRVHs 781
Cdd:pfam15934 112 ARVVRKMGLELKGQEEQRVELCD----KYESLLGSFEEQ----CQELKRANRRVQSlqtrlsQVEKLQEELRTERKILR- 182
|
170 180
....*....|....*....|....*
gi 151556340 782 lEKVVEQKTKENDELTR---ICDDL 803
Cdd:pfam15934 183 -EEVIALKEKDAKSNGReraLQDQL 206
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
135-340 |
6.97e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 43.30 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 135 PVSEDQPPGGPPS-APLVSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWPSEESMPlGPMAPEQPSGVVSQD 213
Cdd:PRK07003 391 VGASAVPAVTAVTgAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKAN-ARASADSRCDERDAQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 214 TAEDPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVgsmdATSREDtALTGPGEAAGATHPGAQGEetcgq 293
Cdd:PRK07003 470 PPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA----AASRED-APAAAAPPAPEARPPTPAA----- 539
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 151556340 294 AASSLRSGPVRLEFDFSDATGKRSPPLRKRGKALGLKPPSRRPEARP 340
Cdd:PRK07003 540 AAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPK 586
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
610-799 |
7.37e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 610 QYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSF------------EGTVYQVMEESQKQKELTKAEMQKVL 677
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlseeAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 678 KEKAQLTADLHSMEKSFSDLFkrfekQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQV 757
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 151556340 758 RSKAQTDALALQAvlrkeqmRVHSLEKVVEQKTKENDELTRI 799
Cdd:COG3206 315 LASLEAELEALQA-------REASLQAQLAQLEARLAELPEL 349
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
660-798 |
8.63e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 660 EESQKQKELTKAEMQKV---LKEKAQ-------LTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERV 729
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKadeAKKKAEeakkadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 730 E-------KEAQKYQALKAQAEEKlRQASEeiaqVRSKAQTDALALQAVLRK--EQMRVHSLEKVVEQKTKEnDELTR 798
Cdd:PTZ00121 1367 EaaekkkeEAKKKADAAKKKAEEK-KKADE----AKKKAEEDKKKADELKKAaaAKKKADEAKKKAEEKKKA-DEAKK 1438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
615-806 |
9.12e-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: 43.13 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 615 DLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVyqvmEESQKQKEltkaEMQKVLKEKAQLTADLhsmEKSF 694
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI----ENLNGKKE----ELEEELEELEAALRDL---ESRL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 695 SDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALK---AQAEEKLRQASEEIAQVRSKAQtdalaLQAV 771
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEIPEEELSLED-----VQAE 959
|
170 180 190
....*....|....*....|....*....|....*
gi 151556340 772 LRKEQMRVHSLEKVVEQKTKENDELTRICDDLISK 806
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
619-783 |
9.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 619 AVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAemQKVLKEKAQLTADLHSMEKSFSDLF 698
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 699 KRFEKQKEVIEGYRTNEESLKKC--------------VEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRskAQTD 764
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELqeeleelleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELE--EELE 230
|
170
....*....|....*....
gi 151556340 765 ALALQAVLRKEQMRVHSLE 783
Cdd:COG4717 231 QLENELEAAALEERLKEAR 249
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
609-767 |
9.63e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 609 LQYSQKDLDSAVEATQKENEV----LRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTK--AEMQKVLKEKAQ 682
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQqaeeLQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKqaEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 683 LTADlhSMEKSFSDLFKRFEKQKEVIEgyrtNEESLKKCVEDYIERVEKEAQkyQALKAQAEEKLRQASEEIAQVRSKAQ 762
Cdd:PRK09510 147 AKAE--AEAKRAAAAAKKAAAEAKKKA----EAEAAKKAAAEAKKKAEAEAA--AKAAAEAKKKAEAEAKKKAAAEAKKK 218
|
....*
gi 151556340 763 TDALA 767
Cdd:PRK09510 219 AAAEA 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
615-798 |
1.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 615 DLDSAVEATQKENEVlrgKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEK-----AQLTADLHS 689
Cdd:PTZ00121 1501 EAKKAAEAKKKADEA---KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKkkaeeAKKAEEDKN 1577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 690 MEKSFSDLFKRFEKQK--EVIEGYRTNE----ESLKKCVEDYIE-----RVEKEAQKYQALKAQAEEKLRQAsEEIAQVR 758
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARieEVMKLYEEEKkmkaEEAKKAEEAKIKaeelkKAEEEKKKVEQLKKKEAEEKKKA-EELKKAE 1656
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 151556340 759 SKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTR 798
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
622-754 |
1.05e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.97 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 622 ATQKENEVLRGKCAALqERLLEMgkIMDSFEGTVYQvMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRF 701
Cdd:pfam10473 14 ESERKADSLKDKVENL-ERELEM--SEENQELAILE-AENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKEL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 151556340 702 EKQKEVIegyrtneESLKKCVEDYIERVEKEAQKyqalKAQAEEKLRQASEEI 754
Cdd:pfam10473 90 QKKQERV-------SELESLNSSLENLLEEKEQE----KVQMKEESKTAVEML 131
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
614-806 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 614 KDLDSAVEATQKENEV--LRGKCAALQERLLEMGKIMDSFEGTVyqvmEESQKQKELTKAEMQKvlKEKAQLTADLHSME 691
Cdd:PRK02224 496 ERLERAEDLVEAEDRIerLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAEAEE--KREAAAEAEEEAEE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 692 K--SFSDLFKRFEKQKEVIEGYRTNEESLKKcVEDYIERVEKEAQKYQALKA---QAEEKLRQASEEIAQVRSKAQTDAL 766
Cdd:PRK02224 570 AreEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAElndERRERLAEKRERKRELEAEFDEARI 648
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 151556340 767 AlQAVLRKEQmrvhsLEKVVEQKTKENDELTRICDDLISK 806
Cdd:PRK02224 649 E-EAREDKER-----AEEYLEQVEEKLDELREERDDLQAE 682
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
595-809 |
1.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 595 PGAPLLPVGPIVDVLQY---SQKDLDSAVEATQKENEVLRGKCAALQERLLEMG---KIMDSFEGTVYQVMEE-----SQ 663
Cdd:COG4717 276 AGVLFLVLGLLALLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGlppDLSPEELLELLDRIEElqellRE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 664 KQKELTKAEMQKVLKEKAQLTADLH-SMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYI--------ERVEKEAQ 734
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeEELEEELE 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151556340 735 KYQALKAQAEEKLRQASEEIAQVrsKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELtRICDDLISKMKR 809
Cdd:COG4717 436 ELEEELEELEEELEELREELAEL--EAELEQLEEDGELAELLQELEELKAELRELAEEWAAL-KLALELLEEARE 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
621-810 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 621 EATQKENEV---------LRGKCAALQERLLEMGKIMDSFEgtvyqvmeESQKQKEltkaemqKVLKEKAQLTADLHSME 691
Cdd:PRK03918 201 ELEEVLREIneisselpeLREELEKLEKEVKELEELKEEIE--------ELEKELE-------SLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 692 KSFSDLFKRFEKQKEV------IEGYRTNEESLKKCVEDY--------------------IERVEKEAQKYQALKAQAEE 745
Cdd:PRK03918 266 ERIEELKKEIEELEEKvkelkeLKEKAEEYIKLSEFYEEYldelreiekrlsrleeeingIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 151556340 746 KLRQASEEIAQVRSKAQT--DALALQAVLRKEQMR-----VHSLEKVVEQKTKENDELTRICDDLISKMKRI 810
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltgltPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
722-775 |
1.50e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.77 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 151556340 722 VEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKE 775
Cdd:COG0711 36 IADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAE 89
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
672-792 |
1.53e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 672 EMQKVLKEK-AQLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYiervEKEAQKYQALKAQAEE----- 745
Cdd:pfam13851 26 ELIKSLKEEiAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY----EKDKQSLKNLKARLKVlekel 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151556340 746 -KLRQASEEIAQVRSKAQT--DAL------ALQAVLRK--------EQmRVHSLEKVVEQKTKE 792
Cdd:pfam13851 102 kDLKWEHEVLEQRFEKVERerDELydkfeaAIQDVQQKtglknlllEK-KLQALGETLEKKEAQ 164
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
621-798 |
1.69e-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: 42.27 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 621 EATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKR 700
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 701 FEKQKEVIEgYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQmrvh 780
Cdd:pfam02463 260 IEKEEEKLA-QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK---- 334
|
170
....*....|....*...
gi 151556340 781 sleKVVEQKTKENDELTR 798
Cdd:pfam02463 335 ---EEIEELEKELKELEI 349
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
706-810 |
1.82e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 706 EVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEkLRQASEEIaqvRSKAQTDALALQAVLRKEQMRVHSLEKV 785
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQ-LKQLEDEL---EDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100
....*....|....*....|....*
gi 151556340 786 VEQKTKENDELTRICDDLISKMKRI 810
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSEL 251
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
702-796 |
1.99e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 39.91 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 702 EKQKEVIEGYRTNE---ESLKKCVEDYIERVEKEAQKYQALKAQAEEKLR-QASEEIAQVRSKA---QTDALA-----LQ 769
Cdd:PRK14473 39 ERTRRIEESLRDAEkvrEQLANAKRDYEAELAKARQEAAKIVAQAQERARaQEAEIIAQARREAekiKEEARAqaeqeRQ 118
|
90 100 110
....*....|....*....|....*....|....
gi 151556340 770 AVLRKEQMRVHSL-----EKVV--EQKTKENDEL 796
Cdd:PRK14473 119 RMLSELKSQIADLvtltaSRVLgaELQARGHDAL 152
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
607-799 |
2.11e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 607 DVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLL-EMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTA 685
Cdd:NF041483 375 EVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRgEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 686 D-LHSMEKSFSDlfKRFEKQKEVIEGYRTNEESLKKCVEDY----------IERVEKEA-QKYQALKAQAEEKLRQASEE 753
Cdd:NF041483 455 EaVAEGERIRGE--ARREAVQQIEEAARTAEELLTKAKADAdelrstataeSERVRTEAiERATTLRRQAEETLERTRAE 532
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 151556340 754 IAQVRSKA--QTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRI 799
Cdd:NF041483 533 AERLRAEAeeQAEEVRAAAERAARELREETERAIAARQAEAAEELTRL 580
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
620-764 |
2.13e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 620 VEATQKENEVLRGKCAALQERL-LEMGKIMDSFEGTVyqvmEESQKQKELTKAEmqkvlkeKAQLTADLHSMEKSFSDLF 698
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEI----EDLRRQLDTLTVE-------RARLQLELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151556340 699 KRFEKQKevieGYRTNEES----LKKCVED-YIERVEKEAqKYQALKAQAEEKLRQASEEIAQVRSKAQTD 764
Cdd:pfam00038 89 QKYEDEL----NLRTSAENdlvgLRKDLDEaTLARVDLEA-KIESLKEELAFLKKNHEEEVRELQAQVSDT 154
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
702-799 |
2.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 702 EKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQA---EEKLRQASEEIAQVRSKAqtdalalQAVLRKEQMR 778
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAaelEEKQQELEAQLEQLQEKA-------AETSQERKQK 217
|
90 100
....*....|....*....|.
gi 151556340 779 VHSLEKVVEQKTKENDELTRI 799
Cdd:PRK11448 218 RKEITDQAAKRLELSEEETRI 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
606-779 |
2.24e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQV---MEESQKQKELTKAEMQKVLKEKAQ 682
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 683 LTADLHSMEKSFSDLFKRFEK----QKEVIEGYRTNEESLKKC---VEDYIERVEKEAQKYQALKAQaeeklrQASEEIA 755
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQleaqIAELQSEIAEREEELKELeeqLESLQEELAALEQELQALSEA------EAEQALD 186
|
170 180
....*....|....*....|....
gi 151556340 756 QVRSKAQTDALALQAVLRKEQMRV 779
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIE 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
606-760 |
2.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTA 685
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151556340 686 DLH----SMEKSFSDLFKRFEKQKEVIEGYRtneeslkkcvedyiERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSK 760
Cdd:COG4913 370 ALGlplpASAEEFAALRAEAAALLEALEEEL--------------EALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
613-792 |
2.60e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 613 QKDLDSAVEATQKENEVLRgkcaaLQERLLEMgKIMdsfegtvyQVMEESQKQKELTKAEMQKVLKEKAQLTADLhsmek 692
Cdd:pfam13868 129 REEIDEFNEEQAEWKELEK-----EEEREEDE-RIL--------EYLKEKAEREEEREAEREEIEEEKEREIARL----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 693 sfsdlfkrfEKQKEVIEGYRTNEESL--KKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEiaQVRSKAQTDALALQa 770
Cdd:pfam13868 190 ---------RAQQEKAQDEKAERDELraKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAE- 257
|
170 180
....*....|....*....|..
gi 151556340 771 vlRKEQMRVHSLEKVVEQKTKE 792
Cdd:pfam13868 258 --REEEEFERMLRKQAEDEEIE 277
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
154-427 |
2.82e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.44 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 154 GPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWPSEESMPLGPMAPE-QPSGVVSQDTAEDPLSGTggdsEGVPGP 232
Cdd:pfam05109 441 APNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSpSPRDNGTESKAPDMTSPT----SAVTTP 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 233 PARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHPGAQGEETCGQAASSLRSGPVrlEFDFSDA 312
Cdd:pfam05109 517 TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPT--PNATSPT 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 313 TGKRSPPLRKRGKALG--------LKPPSRRPEA-RPGKATLEAGKGCELTLRGSDGPSWDKPDDPDcnpaaDSGEARPL 383
Cdd:pfam05109 595 VGETSPQANTTNHTLGgtsstpvvTSPPKNATSAvTTGQHNITSSSTSSMSLRPSSISETLSPSTSD-----NSTSHMPL 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 151556340 384 ---EHPQSG----QATEAlSLSRQACSDDTPGTRaPARTPGAAGEGWTTGS 427
Cdd:pfam05109 670 ltsAHPTGGenitQVTPA-STSTHHVSTSSPAPR-PGTTSQASGPGNSSTS 718
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
613-768 |
3.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 613 QKDLDSAVEATQKENEVLRgkcaalQERLLEmgkimdsfegtvyqVMEESQKQKEltkaEMQKVLKEKaqlTADLHSMEK 692
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIK------KEALLE--------------AKEEIHKLRN----EFEKELRER---RNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 693 SFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQAS----EE-----IAQVRSKAQT 763
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaEEakeilLEKVEEEARH 169
|
....*
gi 151556340 764 DALAL 768
Cdd:PRK12704 170 EAAVL 174
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
121-280 |
3.40e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 121 PVPVNTEPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSSQIPESVENP--EASRGPAPGSPECAREEHVHPWPSEESMPL 198
Cdd:PRK07764 646 GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPagAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 199 GPMAPEQPSGVVSQDTAEDPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAA 278
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVA 805
|
..
gi 151556340 279 GA 280
Cdd:PRK07764 806 ME 807
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
691-799 |
3.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 691 EKSFSDLFKRFEKQKEVI----EGYRTNEESLKKcVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDAL 766
Cdd:COG4372 9 GKARLSLFGLRPKTGILIaalsEQLRKALFELDK-LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110
....*....|....*....|....*....|...
gi 151556340 767 ALQAVLRKEQMRVHSLEKVVEQKTKENDELTRI 799
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
659-798 |
3.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 659 MEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfsdlfkRFEKQKEVIEGYRTNEESLKKCVEDYIERVEKEAQKYQA 738
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARS-------ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 739 LKAQAEEkLRQASEEIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTR 798
Cdd:COG4372 113 LQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
625-795 |
3.77e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 625 KENEVLRGKCAA---------LQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfs 695
Cdd:pfam15905 136 RVNELLKAKFSEdgtqkkmssLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 696 dlfkrfEKQKEviegyrtNEESLKkcVEDYIER---VEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVL 772
Cdd:pfam15905 213 ------EKIEE-------KSETEK--LLEYITElscVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQI 277
|
170 180
....*....|....*....|...
gi 151556340 773 RKEQMRVHSLEKVVEQKTKENDE 795
Cdd:pfam15905 278 KDLNEKCKLLESEKEELLREYEE 300
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
606-792 |
4.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLlemgkimdsfegtvyqvmeeSQKQKELTK--AEMQKVLKEKAQL 683
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI--------------------EERREELGEraRALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 684 TADLHSmeKSFSDLFKRF-------EKQKEVIEGYrtneESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQ 756
Cdd:COG3883 106 DVLLGS--ESFSDFLDRLsalskiaDADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 151556340 757 VRSKAQtdalALQAVLRKEQMRVHSLEKVVEQKTKE 792
Cdd:COG3883 180 QEALLA----QLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
657-807 |
4.85e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.23 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 657 QVMEESQK--QKELTKAEmqkVLKEKAQLtadlhsMEKSFSDLFKRFEKQKEVIegyrtneeslkkcVEDYIERVEKEAQ 734
Cdd:COG0711 27 KALDERQEkiADGLAEAE---RAKEEAEA------ALAEYEEKLAEARAEAAEI-------------IAEARKEAEAIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 735 KYQA-LKAQAEEKLRQASEEIAQVRSKAQTD------ALALQAVlrkeqmrvhslEKVVEQKTKENDElTRICDDLISKM 807
Cdd:COG0711 85 EAKAeAEAEAERIIAQAEAEIEQERAKALAElraevaDLAVAIA-----------EKILGKELDAAAQ-AALVDRFIAEL 152
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
670-810 |
4.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 670 KAEMQKVLKEKAQLTADLHSMEKSFSDLFK------RFEKQKEVIEGYRTNEESLKKCvedYIERVEKEAQKYQALKaqa 743
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKvlkkesELIKLKELAEQLKELEEKLKKY---NLEELEKKAEEYEKLK--- 531
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 744 eEKLRQASEEIAQVRSKAQTDAlALQAVLRKEQMRVHSLEKVVEQKTKENDELTRIC-DDLISKMKRI 810
Cdd:PRK03918 532 -EKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKEL 597
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
621-810 |
4.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 621 EATQKENEV--LRGKCAALQERLLEMGKIMDSFEgTVYQVMEESQK-QKELTKAEMQKVLKEkaqltadLHSMEKSFSDL 697
Cdd:PRK03918 332 ELEEKEERLeeLKKKLKELEKRLEELEERHELYE-EAKAKKEELERlKKRLTGLTPEKLEKE-------LEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 698 FKRFEKQKEVIEGYRTNEESLKKCVE----------------------DYIERVEKEAQKYQALKAQAEEKLRQASEEIA 755
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 151556340 756 QVRS--KAQTDALALQAVLR-----KEQMRVHSLEKvVEQKTKENDELTRICDDLISKMKRI 810
Cdd:PRK03918 484 ELEKvlKKESELIKLKELAEqlkelEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSL 544
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
137-290 |
5.02e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.95 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 137 SEDQPPGGPPSAPLVSLGPSSSSQIPESVENPEASRGPAPGSPecAREEHVHPWPSEESMPLGPMAPEQPSGVVSQDTAE 216
Cdd:PHA03169 99 SVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPP--SHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151556340 217 DPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHPGAQGEET 290
Cdd:PHA03169 177 EPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGH 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
612-794 |
5.03e-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: 40.42 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 612 SQKDLDSAVEATQKENEVLRGKCAALQERllemGKIMDSFegtVYQVMEESQK-----QKEL-TKAEMQKVLKEKAQLTA 685
Cdd:TIGR00606 633 GSQDEESDLERLKEEIEKSSKQRAMLAGA----TAVYSQF---ITQLTDENQSccpvcQRVFqTEAELQEFISDLQSKLR 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 686 DLHSMEKSFSDLFKRFEKQKEVIEGY---RTNEESLK-KCVEDYIERVEKEAQKYQALKAQAEEKLRQ-----ASEEIAQ 756
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLapgRQSIIDLKeKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimPEEESAK 785
|
170 180 190
....*....|....*....|....*....|....*...
gi 151556340 757 VrskAQTDAlalqAVLRKEQMRVHSLEKVVEQKTKEND 794
Cdd:TIGR00606 786 V---CLTDV----TIMERFQMELKDVERKIAQQAAKLQ 816
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
122-273 |
5.35e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 40.29 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 122 VPVNTEPPSED---MRPVS-----ED-QPPGGP-PSAPlvSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWP 191
Cdd:PLN03209 354 PPIEEEPPQPKavvPRPLSpytayEDlKPPTSPiPTPP--SSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 192 SEESMPLGPMA------------PEQPSGVVSQDTAEDPLSGTG--------GDSEGVPGPPARPASPCGAPPGEKPLVD 251
Cdd:PLN03209 432 AKKTRPLSPYAryedlkpptspsPTAPTGVSPSVSSTSSVPAVPdtapataaTDAAAPPPANMRPLSPYAVYDDLKPPTS 511
|
170 180
....*....|....*....|..
gi 151556340 252 LPGAAPVGSMDATSREDTALTG 273
Cdd:PLN03209 512 PSPAAPVGKVAPSSTNEVVKVG 533
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
639-799 |
5.52e-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: 40.44 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 639 ERLLEMGKIMDSFEGTvyqvmeESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEVIEgyrTNEESL 718
Cdd:TIGR02169 211 ERYQALLKEKREYEGY------ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 719 KKCVEDYIERVEKE----------AQKYQALKA----QAEEKLRQASEEIAQVRSKAQtdalALQAVLRKEQMRVHSL-E 783
Cdd:TIGR02169 282 KDLGEEEQLRVKEKigeleaeiasLERSIAEKEreleDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLtE 357
|
170
....*....|....*.
gi 151556340 784 KVVEQKTKENDELTRI 799
Cdd:TIGR02169 358 EYAELKEELEDLRAEL 373
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
624-753 |
6.79e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 39.96 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 624 QKENEVLRGKCAA----LQERLLEMGKIMD-----SFEGTVYQVMEESQKQ--KELTKaeMQKVLKEKAQLTadlhsmEK 692
Cdd:pfam14643 269 RAEYEEVWQECLArvqkLKQELLDYKVCSEeeaeaLVNEEFLPLVGKLQRDaeDELEK--LDKFLEELAKQT------EA 340
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151556340 693 SFSDLFKRFEKQKEVIEGYRTNeesLKKCVEDYIERVEKEAQKY----QALKA---QAEEKLRQASEE 753
Cdd:pfam14643 341 QSEDLFKFFREAAQLWDVHQTE---LAKQELELEKKLEQCRQKHdqenQAKEAaldKKLDQLRQASTE 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
631-809 |
6.88e-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: 40.05 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 631 RGKCAALQErLLEMGKIMDSFEGTVYQVMEESQK-QKELTKAE-MQKVLKEKAQLTADLHSMEKsfsdlfKRFEKQKEVI 708
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERlRREREKAErYQALLKEKREYEGYELLKEK------EALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 709 EGYRtneESLkkcvEDYIERVEKEAQKYQALKAQAEEKLRQASEEIaqvRSKAQTDALALQAVLRKEQMRVHSLE---KV 785
Cdd:TIGR02169 243 ERQL---ASL----EEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLErsiAE 312
|
170 180
....*....|....*....|....
gi 151556340 786 VEQKTKENDELTRICDDLISKMKR 809
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLA 336
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
663-760 |
7.58e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 663 QKQKELTKAEMQKVLKEKA-QLTADLHSMEKSFSDLFKRFEKQKEVIEGYRTNEESLKKCVEDyIERVEKEAQKYQALKA 741
Cdd:COG0542 424 EIEKEALKKEQDEASFERLaELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK-IPELEKELAELEEELA 502
|
90 100
....*....|....*....|.
gi 151556340 742 QAEEKLRQA--SEEIAQVRSK 760
Cdd:COG0542 503 ELAPLLREEvtEEDIAEVVSR 523
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
617-796 |
8.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 617 DSAVEATQKENEVLRGKCAALQERLLEMgkimdsfegtvyqvmeesQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSD 696
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL------------------QAELEELNEEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151556340 697 LFKRFEKQKEVIEG-----YRT-----------NEESLkkcvEDYIERVE----------KEAQKYQALKAQAEEK---L 747
Cdd:COG3883 77 AEAEIEERREELGEraralYRSggsvsyldvllGSESF----SDFLDRLSalskiadadaDLLEELKADKAELEAKkaeL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 151556340 748 RQASEEIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDEL 796
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| |
