|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
975-1077 |
3.97e-67 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 224.78 E-value: 3.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 975 VKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITP 1054
Cdd:cd03277 111 VKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITP 190
|
90 100
....*....|....*....|...
gi 358248335 1055 KLLQNLPYSEKMTVLFVYNGPHM 1077
Cdd:cd03277 191 KLLPGLNYHEKMTVLCVYNGPHI 213
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
51-196 |
1.15e-59 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 203.60 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 51 GSIVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIELFRT 130
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248335 131 SGnliitreidviknqsfwfinkkpvtqkiveeqvaalNIQVGNLCQFLPQDKVGEFAKLSKIELL 196
Cdd:cd03277 81 PG------------------------------------NIQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
991-1073 |
3.90e-28 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 112.02 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 991 QSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACkeNTSQYFFITPKLLQNLPYSEKMTVLF 1070
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAK--HTSQFIVITLKKEMFENADKLIGVLF 172
|
...
gi 358248335 1071 VYN 1073
Cdd:cd03239 173 VHG 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-1053 |
1.68e-22 |
|
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: 104.75 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 196 LEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLE-----------KMVQRNERYKQDVERFYE---RKRHLD 261
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQeleekleelrlEVSELEEEIEELQKELYAlanEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 262 L-IEMLEAKRPWVEYENVRQEYEGVKLIR--DRVKEEVRKLKEgqipmtrRIEEIDRQRHTLEVRIKEKSTDIKEASQKC 338
Cdd:TIGR02168 302 QqKQILRERLANLERQLEELEAQLEELESklDELAEELAELEE-------KLEELKEELESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 339 KQRQDLIERKDRQIKELQQALTVKQNE--ELDRQK-----RISNTRKMIEDLQSELKTAE------NCENLQPQIDTVTN 405
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEieRLEARLerledRRERLQQEIEELLKKLEEAElkelqaELEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 406 DLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKlrqryrdtYDAVLWLRNNRDRFKQRVcePI 485
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF--------SEGVKALLKNQSGLSGIL--GV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 486 MLTINMKDNKNAKYVENHISSNdLRAFVFESQEDMEIFLREVRDNKKLRVNAVIAPKISYADKAPSRSLNDLKQYGFFSY 565
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGR-LQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 566 LRELFDAPD---PVMSYLCCQYHI-----------------------------------------HEVPVGTERTRERIE 601
Cdd:TIGR02168 604 AKDLVKFDPklrKALSYLLGGVLVvddldnalelakklrpgyrivtldgdlvrpggvitggsaktNSSILERRREIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 602 RVIQE-------------TRLKQIYTAEEKYVLKTSVYSNKVISSNTSLKVAQFLTVTVD--LEQRRHLEEQLKEMNRQL 666
Cdd:TIGR02168 684 EKIEEleekiaelekalaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqlEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 667 EAVDSGLAALRDT-------------------------NRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLM 721
Cdd:TIGR02168 764 EELEERLEEAEEElaeaeaeieeleaqieqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 722 EQDTCNLEEEERKASTKIKEINVQKAKLVTELTGLVKictsfqiqkvdlilqnttvisEKNKLEADYMASSSQLRVTEQQ 801
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLN---------------------ERASLEEALALLRSELEELSEE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 802 FIELDDNRQRLLQKCKELMKKARQVCNlsADQAVPQEFQTQVPTIPNGHSSSPPMAFQDLPNTLDEIDAL------LTEE 875
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLEL--RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEArrrlkrLENK 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 876 RSRascFTGLNPSVVEEYSkrevEIQQLTEELQGKKVELDEYREN----ISQVKERWLNPLKELVEKINEKFSNFFSSMQ 951
Cdd:TIGR02168 981 IKE---LGPVNLAAIEEYE----ELKERYDFLTAQKEDLTEAKETleeaIEEIDREARERFKDTFDQVNENFQRVFPKLF 1053
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 952 CAGEVDLHTENEEDYDKYGIRIRVKF--RSSTQLHELtphhqSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPIN 1029
Cdd:TIGR02168 1054 GGGEAELRLTDPEDLLEAGIEIFAQPpgKKNQNLSLL-----SGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDAN 1128
|
970 980
....*....|....*....|....*.
gi 358248335 1030 ERRVFEMVvntacKE--NTSQYFFIT 1053
Cdd:TIGR02168 1129 VERFANLL-----KEfsKNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-1052 |
3.24e-20 |
|
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: 97.06 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSP-GPHLNMIIGANGTGKSSIVCAI--CLGLAGKPAFmgRADKVGFFV---KRGCSKGLVEIE 126
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPfSKGFTVISGPNGSGKSNIGDAIlfALGLSSSKAM--RAERLSDLIsngKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 127 LF------RTSGNLIITREIDVIKN--QSFWFINKKPVTQKIVEEQVAALNIQVGNLcQFLPQDKVGEFAKLSKIELLEA 198
Cdd:TIGR02169 80 VTfknddgKFPDELEVVRRLKVTDDgkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 199 TEKSVGPPEMHR----YHCELKNFREKEKQLETSCKEKTEYLEKM-VQRN--ERYK--QDVERFYERKRHLDLIEMLEAK 269
Cdd:TIGR02169 159 IDEIAGVAEFDRkkekALEELEEVEENIERLDLIIDEKRQQLERLrREREkaERYQalLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 270 RPWVEYE--NVRQEYEGVK-LIRDRVKE-------------EVRKLKEG-QIPMTRRIEEIDRQRHTLEVRIKEKSTDIK 332
Cdd:TIGR02169 239 KEAIERQlaSLEEELEKLTeEISELEKRleeieqlleelnkKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 333 EASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSEL---------------KTAENCENLQ 397
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaetrdelkDYREKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 398 PQIDTVTNDLRRVQEEKALCEGEI---------------------------IDKQREK-EMLEKQRRSVSDHITRFDNLM 449
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELadlnaaiagieakineleeekedkaleIKKQEWKlEQLAADLSKYEQELYDLKEEY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 450 NQKEDKLRQRYRDTYDAVLWLRNNRDRFKQRVCEPIMLTINMK------------DNKNAKYVENhISSNDLRAFVFESQ 517
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEV-AAGNRLNNVVVEDD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 518 EDMEIFLREVRDNKKLRVNAVIAPKIsyadKAPSRSLNDLKQYGFFSYLRELFDAPD---PVMSYLCCQYHIHE------ 588
Cdd:TIGR02169 558 AVAKEAIELLKRRKAGRATFLPLNKM----RDERRDLSILSEDGVIGFAVDLVEFDPkyePAFKYVFGDTLVVEdieaar 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 589 --------------------VPVGTERTRERIERVIQETRLKQIYTAEEKYVLKTSVYS---------NKVISSNTSLKV 639
Cdd:TIGR02169 634 rlmgkyrmvtlegelfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrrieNRLDELSQELSD 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 640 AQFLTVTVDLE------QRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLE--LKDNELRLKKKELLERKTRKRQLEQKI 711
Cdd:TIGR02169 714 ASRKIGEIEKEieqleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEarIEELEEDLHKLEEALNDLEARLSHSRI 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 712 SSKLASIRLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMAS 791
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 792 SSQLRVTEQQFIELDDNRQRLLQKCKELMKKARQV--------CNLSADQAVPQEFQTQVPTI--PNGHSSSPPMAFQDL 861
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqiekkrKRLSELKAKLEALEEELSEIedPKGEDEEIPEEELSL 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 862 PNTLDEIDALltEERSRAscFTGLNPSVVEEYSkrevEIQQLTEELQGKKVELDEYRENISQVKERwLNPLK-----ELV 936
Cdd:TIGR02169 954 EDVQAELQRV--EEEIRA--LEPVNMLAIQEYE----EVLKRLDELKEKRAKLEEERKAILERIEE-YEKKKrevfmEAF 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 937 EKINEKFSNFFSSMQcAGEVDLHTENEEDYDKYGIRIRVKFRSST--QLHELtphhqSGGERSVSTMLYLMALQELNRCP 1014
Cdd:TIGR02169 1025 EAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPvqRLEAM-----SGGEKSLTALSFIFAIQRYKPSP 1098
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 358248335 1015 FRVVDEINQGMDPINERRVFEMVvntacKENTSQYFFI 1052
Cdd:TIGR02169 1099 FYAFDEVDMFLDGVNVERVAKLI-----REKAGEAQFI 1131
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
53-127 |
2.18e-18 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 83.90 E-value: 2.18e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358248335 53 IVRIAMENFLTYDICEVSPGP-HLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKV---GFFVKRGCSKGLVEIEL 127
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITF 79
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
53-1053 |
2.46e-18 |
|
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: 91.19 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSP-GPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV----KRGCSKGLVEI-- 125
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPfSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEItf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 126 -----ELFRTSGNLIITREIdVIKNQSFWFINKKPVTQKIVEEQVAALNIQVGNLCQFLPQDKV---------------- 184
Cdd:pfam02463 82 dnedhELPIDKEEVSIRRRV-YRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIeiiammkperrleiee 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 185 ----GEFAKLSKIELLEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHL 260
Cdd:pfam02463 161 eaagSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 261 DLIEMLEAKRPWVEYENVRQEYEG-----VKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEAS 335
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEeklaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 336 QKCKQRQDLIERKDRQIKELQQALTVK------------------QNEELDRQKRISNTRKMIEDLQSELKTAEN---CE 394
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELeikreaeeeeeeeleklqEKLEQLEEELLAKKKLESERLSSAAKLKEEeleLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 395 NLQPQIDTVTNDLRRVQE-----------EKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRDT 463
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEdllkeekkeelEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 464 ------YDAVLWLRNNRDRFKQRVCEPimlTINMKDNKNAKYVENHISSNDLRAFVFESQEDME---IFLREVRDNKKLR 534
Cdd:pfam02463 481 klqeqlELLLSRQKLEERSQKESKARS---GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvaISTAVIVEVSATA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 535 VNAVIAPKISYADKAPSRSLNDLKQYGFFSYLRELFDAPDPVMSYL-CCQYHIHEVPVGTERTRERIERVIQETRLKQiy 613
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILnLAQLDKATLEADEDDKRAKVVEGILKDTELT-- 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 614 TAEEKYVLKTSVYSNKVISSNTSLKVAQFLTVTVDLEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLK 693
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 694 KKELLERKTRKRQLEQKISSKLASIRLMEQDTCNLEEEERKASTKIKEI---------------------NVQKAKLVTE 752
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEekselslkekelaeerektekLKVEEEKEEK 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 753 LTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFI------------------------ELDDN 808
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQkleklaeeelerleeeitkeellqELLLK 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 809 RQRLLQKC----------------KELMKKARQVCNLSADQAVPQEFQTQVPTIPNGHSSSPPMAFQDLPNTLDEIDALL 872
Cdd:pfam02463 876 EEELEEQKlkdeleskeekekeekKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 873 TEERSRASC-------FTGLNPSVVEEYSKREVEIQQLTEELQGKKVELDEYRENISQVKERWLNPLKELVEKINEKFSN 945
Cdd:pfam02463 956 EEEEERNKRlllakeeLGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNK 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 946 FFSSMQCAGEVDLHTENEEDYDKYGIRIRVKFRSSTQLHELTphhQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGM 1025
Cdd:pfam02463 1036 VFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDL---LSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAAL 1112
|
1130 1140
....*....|....*....|....*...
gi 358248335 1026 DPINERRVFEMVVNTAckeNTSQYFFIT 1053
Cdd:pfam02463 1113 DDQNVSRVANLLKELS---KNAQFIVIS 1137
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
989-1077 |
1.39e-17 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 81.25 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 989 HHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKenTSQYFFITPKLLQNLPYSEKMTV 1068
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
|
....*....
gi 358248335 1069 LFVYNGPHM 1077
Cdd:cd03227 154 KKVITGVYK 162
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
992-1069 |
2.19e-13 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 69.93 E-value: 2.19e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248335 992 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVL 1069
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
53-127 |
1.16e-12 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 68.01 E-value: 1.16e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248335 53 IVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIEL 127
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTL 75
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
56-238 |
2.80e-12 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 66.75 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 56 IAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFV------KRGCSKGLVEIELFR 129
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdirigLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 130 TSG--NLIITREIDVIKN------QSFWFINKKPVTQKIVEEQVAALNIQVgNLCQFLPQDKVGEFAKLSKIELLEATEK 201
Cdd:pfam13476 81 NDGryTYAIERSRELSKKkgktkkKEILEILEIDELQQFISELLKSDKIIL-PLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 358248335 202 SVGPPEmhryhcELKNFREKEKQLETSCKEKTEYLEK 238
Cdd:pfam13476 160 ALEEKE------DEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
53-138 |
1.97e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 58.48 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTY-DICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAfmGRADKVGFFVKRGCSKGLVEIELFRTS 131
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
....*..
gi 358248335 132 GNLIITR 138
Cdd:COG0419 80 KRYRIER 86
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
55-127 |
3.13e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 56.98 E-value: 3.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358248335 55 RIAMENFLTYDICE-VSPG-PHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRadkvGFFVKRGCSKGLVEIEL 127
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR----RSGVKAGCIVAAVSAEL 71
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-825 |
1.34e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 244 ERYKQDVERFYERKRHLDLIEmleakRPWVEYENVRQEYEGVKLIRDRVKEEVRKLKEGQIpmTRRIEEIDRQRHTLEVR 323
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-----ELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 324 IKEKSTDIKEASQKCKQ-RQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKT-----AENCENLQ 397
Cdd:COG4913 311 LERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeefAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 398 PQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSvsdhitrfdnlmnqkedkLRQRyRDTYDAvlWLRNNRDRF 477
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------------LERR-KSNIPA--RLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 478 KQR----------VCEpiMLTINMKDNK--NAkyVENHISSNDLRAFVFESQEDMeiFLREVRDNK-KLRVNAVIAPKIS 544
Cdd:COG4913 450 AEAlgldeaelpfVGE--LIEVRPEEERwrGA--IERVLGGFALTLLVPPEHYAA--ALRWVNRLHlRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 545 YADKAPSRSLNDL------KQYGFFSYLRELFDAPdpvMSYLCCQyhihevpvgTERTRERIERVIQETRL-KQIYTAEE 617
Cdd:COG4913 524 PDPERPRLDPDSLagkldfKPHPFRAWLEAELGRR---FDYVCVD---------SPEELRRHPRAITRAGQvKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 618 KYVlKTSVYSNKVISSNTSLKVAQFLTVTVDLEQRRH-LEEQLKEMNRQLEAVDSGLAALRdtnRHLELKDNELRLK--K 694
Cdd:COG4913 592 KDD-RRRIRSRYVLGFDNRAKLAALEAELAELEEELAeAEERLEALEAELDALQERREALQ---RLAEYSWDEIDVAsaE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 695 KELLERKTRKRQLEQKiSSKLASIRLMEQDtcnLEEEERKASTKIKEINVQKAKLVTELTGLVKictsfQIQKVDLILQN 774
Cdd:COG4913 668 REIAELEAELERLDAS-SDDLAALEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQAEE-----ELDELQDRLEA 738
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 358248335 775 TTVISEKNKLE------ADYMASSSQLRVTEQQFIELDDNRQRLLQKCKELMKKARQ 825
Cdd:COG4913 739 AEDLARLELRAlleerfAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
53-436 |
6.07e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIELFRTSG 132
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 133 NLIITREIDviKNQSFWFINKKPVTQKIVEEQVAALNIQVGNLCQFLPQDKV--GEFAKLskIELLEATEKSVGP-PEMH 209
Cdd:PRK03918 83 KYRIVRSFN--RGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLNAIYIrqGEIDAI--LESDESREKVVRQiLGLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 210 RYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPwVEYENVRQEYEGVKLIR 289
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 290 DRVkEEVRKLKEGQIPMTRRIEEIDRQrhtLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKelQQALTVKQNEELDR 369
Cdd:PRK03918 238 EEI-EELEKELESLEGSKRKLEEKIRE---LEERIEELKKEIEELEEKVKELKELKEKAEEYIK--LSEFYEEYLDELRE 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358248335 370 -QKRISNTRKMIEDLQSELKTAENCENlqpQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRR 436
Cdd:PRK03918 312 iEKRLSRLEEEINGIEERIKELEEKEE---RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
53-163 |
7.72e-08 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 54.90 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLglagkpAFMGRADKVgfFVKRGCSKGLVEIE------ 126
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSL------LLGGRASAD--LIRSGAEKAVVEGVfdisde 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 358248335 127 ----------LFRTSGNLIITREIDvIKNQSFWFINKKPVTQKIVEE 163
Cdd:cd03241 73 eeakalllelGIEDDDDLIIRREIS-RKGRSRYFINGQSVTLKLLRE 118
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-462 |
1.33e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 308 RRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSEL 387
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248335 388 K-TAENCENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRD 462
Cdd:COG1196 312 ReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
231-463 |
5.93e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 231 EKTEYLEKMvqRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEY----ENVRQEYEGVKLIRDRVKEEVRKLKEGQIPM 306
Cdd:pfam17380 345 ERERELERI--RQEERKRELERIRQEEIAMEISRMRELERLQMERqqknERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 307 TR-RIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQS 385
Cdd:pfam17380 423 EQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 386 ELKTA----ENCENL------QPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEK--QRRSVSDHITRFDNLMNQ-- 451
Cdd:pfam17380 503 ERKQAmieeERKRKLlekemeERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKatEERSRLEAMEREREMMRQiv 582
|
250
....*....|..
gi 358248335 452 KEDKLRQRYRDT 463
Cdd:pfam17380 583 ESEKARAEYEAT 594
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
53-459 |
2.41e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPafmgRADKVGFFVKRGCSKGLVEIELFRTSG 132
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 133 NLIITREIDV----IKNQSFWFINKKPVTQ------KIVEEQVAALNIQVGNLCQFLPQDKV-----GEFAKLSKI--EL 195
Cdd:PRK01156 79 VYQIRRSIERrgkgSRREAYIKKDGSIIAEgfddttKYIEKNILGISKDVFLNSIFVGQGEMdslisGDPAQRKKIldEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 196 LEATEKSVGPPEMHR----YHCELKNFREKEKQLETSCKEkTEYLEKMVQRNERYKQDVERfyerkrhldliemlEAKRP 271
Cdd:PRK01156 159 LEINSLERNYDKLKDvidmLRAEISNIDYLEEKLKSSNLE-LENIKKQIADDEKSHSITLK--------------EIERL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 272 WVEYENVRQEYegvklirDRVKEEVRKlkegqipMTRRIEEIDRqrhtLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQ 351
Cdd:PRK01156 224 SIEYNNAMDDY-------NNLKSALNE-------LSSLEDMKNR----YESEIKTAESDLSMELEKNNYYKELEERHMKI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 352 IKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKTAEncenlqpqidtvtnDLRRVQEEKALCEGEIIDKQREKEML 431
Cdd:PRK01156 286 INDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH--------------AIIKKLSVLQKDYNDYIKKKSRYDDL 351
|
410 420
....*....|....*....|....*...
gi 358248335 432 EKQRRSVSDHITRFDNLMNQKEDKLRQR 459
Cdd:PRK01156 352 NNQILELEGYEMDYNSYLKSIESLKKKI 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-459 |
4.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 219 REKEKQLETsckekteyLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRpwvEYENVRQEYEGVKLIRDRVKEEVRK 298
Cdd:COG1196 196 GELERQLEP--------LERQAEKAERYRELKEELKELEAELLLLKLRELEA---ELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 299 LKEgqipmtrRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQ--------RQDLIERKDRqIKELQQALTVKQNEELDRQ 370
Cdd:COG1196 265 LEA-------ELEELRLELEELELELEEAQAEEYELLAELARleqdiarlEERRRELEER-LEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 371 KRISNTRKMIEDLQSELKTAENcenlqpQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMN 450
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEA------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
....*....
gi 358248335 451 QKEDKLRQR 459
Cdd:COG1196 411 ALLERLERL 419
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
214-455 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 214 ELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDL---------------IEMLEAkrpwvEYENV 278
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESkiqnqeklnqqkdeqIKKLQQ-----EKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 279 RQEYEGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQA 358
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 359 LTVKQNEELDRQKRISNTRKMIEDLQSELKTAENcenlqpQIDTVTNDLRRVQEE--KALCEGEIIDKQREKEMLEKQRR 436
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKES------KISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQK 578
|
250
....*....|....*....
gi 358248335 437 SVSDHITRFDNLMNQKEDK 455
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKE 597
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-392 |
2.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 214 ELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDliEMLEAKRPWVEYENVRQEYEGVKLIRDRVK 293
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 294 EEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRqdlIERKDRQIKELQQALTVKQNEELDRQKRI 373
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE---LEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....*....
gi 358248335 374 SNTRKMIEDLQSELKTAEN 392
Cdd:COG4717 230 EQLENELEAAALEERLKEA 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-440 |
3.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 262 LIEMLEAKRPWVEYENVRQEYEGVKLIRDrVKEEVRKLKEGQ---IPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKC 338
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKE-LEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 339 KQRQDLIERKD--RQIKELQ---QALTVKQNEELDRQKRISNTRKMIEDLQSELKTAENCENLQ--PQIDTVTNDLRRVQ 411
Cdd:COG4717 126 QLLPLYQELEAleAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*....
gi 358248335 412 EEKALCEGEIIDKQREKEMLEKQRRSVSD 440
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
290-451 |
3.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 290 DRVKEEVRKLKEgqipMTRRIEEIDRQRHTLEvRIKEKSTDIKEASQKCKQRQDLIERkdRQIKELQQALTVKQNEeldr 369
Cdd:COG4913 228 DALVEHFDDLER----AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAE---- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 370 qkrisntrkmIEDLQSELKTAEN-CENLQPQIDTVTNDLRRVQEEKALCEGEIIDK-QREKEMLEKQRRSVSDHITRFDN 447
Cdd:COG4913 297 ----------LEELRAELARLEAeLERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEA 366
|
....
gi 358248335 448 LMNQ 451
Cdd:COG4913 367 LLAA 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
222-440 |
4.45e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 222 EKQLETSCKEKTEYLekmvQRNERYKQDVERfyERKRHLDLIEMLEAKRPWVEYENVRQEyEGVKLIRDRVKEEVRKLKE 301
Cdd:pfam07888 33 QNRLEECLQERAELL----QAQEAANRQREK--EKERYKRDREQWERQRRELESRVAELK-EELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 302 GQIPMTRRIEEID---RQRHTLEVRIKEKSTDIKEASQKCKQRQDLIER-KDRQikelQQALTVKQNEELDRQKRISNTR 377
Cdd:pfam07888 106 LSASSEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERmKERA----KKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358248335 378 KMIEDLQSELKTAENCENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSD 440
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQE 244
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
53-151 |
4.73e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLT-YDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAG-KPAFMGRADKVGFFVKRGCSKGLVEIELFRT 130
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGeLPPNSKGGAHDPKLIREGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|....*....
gi 358248335 131 SGN-LIITREIDVIKN-------QSFWFI 151
Cdd:cd03240 81 NGKkYTITRSLAILENvifchqgESNWPL 109
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
280-389 |
6.75e-05 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 45.20 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 280 QEYEGVKLIRDRVKE---EVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRqdlIERKDRQIKELQ 356
Cdd:pfam06785 80 LDAEGFKILEETLEElqsEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQ---LAEKQLLINEYQ 156
|
90 100 110
....*....|....*....|....*....|....
gi 358248335 357 QAlTVKQNEELD-RQKRISNTRKMIEDLQSELKT 389
Cdd:pfam06785 157 QT-IEEQRSVLEkRQDQIENLESKVRDLNYEIKT 189
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
311-386 |
9.28e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 9.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248335 311 EEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSE 386
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-458 |
1.71e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 289 RDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELD 368
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 369 R----QKRISNTRKMI----EDLQSELKTAENCENLQP----QIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRR 436
Cdd:COG4942 109 LlralYRLGRQPPLALllspEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180
....*....|....*....|..
gi 358248335 437 SVSDHITRFDNLMNQKEDKLRQ 458
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAE 210
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
53-368 |
1.76e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 45.28 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFmgraDKVGFFVKRGCSKGLVEIELFRTSG 132
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKF----FEDDFLVLYLKDVIKIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 133 NLIITREIDVIKnqsfWFINKKPVTQKIveeqvaalnIQVGNLCQFLPQDKVGEFAKLSKIELLEATEKSVGPPEMHRYh 212
Cdd:pfam13175 79 NISFSIDIEIDV----EFLLILFGYLEI---------KKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKY- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 213 ceLKNFREKEKQLETSCKEKteYLEKMVQRNERYKQDVERFYERKRHLDlIEMLEAKRPWVEYENVRQEYEGVKLIRDRV 292
Cdd:pfam13175 145 --LKQFKIYIYNNYYLDEKK--NVFDKKSKYELPSLKEEFLNSEKEEIK-VDKEDLKKLINELEKSINYHENVLENLQIK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248335 293 KEevrklkegqIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELD 368
Cdd:pfam13175 220 KL---------LISADRNASDEDSEKINSLLGALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILF 286
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
308-442 |
2.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 308 RRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQAL---------------TVKQNEELDR-QK 371
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeevearikkyeeqlgNVRNNKEYEAlQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358248335 372 RISNTRKMIEDLQSELKTA-ENCENLQPQIDTVTNDL----RRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHI 442
Cdd:COG1579 97 EIESLKRRISDLEDEILELmERIEELEEELAELEAELaeleAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-453 |
2.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 181 QDKVGEFAKLSKIELLEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQ---RNERYKQDVERFYERK 257
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 258 RHLDLIEMLEAKRPWVEYENVRQEYEGVKLIRDRVKEEVRKLkegqipmTRRIEEIDRQRHTLEVRIKEkstdIKEASQK 337
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI-------TARIGELKKEIKELKKAIEE----LKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 338 C---------KQRQDLIERKDRQIKELQ---QALTVKQNEELDRQKRISNTRKMIEDLQSELKTAEncenlqpQIDTVTN 405
Cdd:PRK03918 438 CpvcgrelteEHRKELLEEYTAELKRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-------QLKELEE 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 358248335 406 DLRRVQEEKALCEGEIIDKQREKEM-LEKQRRSVSDHITRFDNLMNQKE 453
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIkLKGEIKSLKKELEKLEELKKKLA 559
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
992-1053 |
2.67e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 2.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 358248335 992 SGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTAckeNTSQYFFIT 1053
Cdd:cd03278 115 SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS---KETQFIVIT 173
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
53-142 |
2.69e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTYDICEVSPGPhLNMIIGANGTGKSSIVCAICL-------GLAGKPAFMGRADKVgFFVKRGCSKGLVEI 125
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFlsdaargGLQDALARRGGLEEL-LWRGPRTITEPIRL 79
|
90
....*....|....*...
gi 358248335 126 EL-FRTSGNLIITREIDV 142
Cdd:COG4637 80 ELeFAEEDERDLRYELEL 97
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
214-450 |
3.00e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 214 ELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDV-------------ERFYERKRHLDLI--EMLEAKRPWV-EYEN 277
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVtellnkysalaikNKFAKTKKDSEIIikEIKDAHKKFIlEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 278 VRQEYEGVKLIRDRVKEEVRKLKEGQipmtRRIEEIDRQRHTLEVRIKeKSTDIKEASQKCKQRQDLIERKDRQIKELQQ 357
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIEDDAAKNDKSN----KAAIDIQLSLENFENKFL-KISDIKKKINDCLKETESIEKKISSFSIDSQ 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 358 ALTVKQNEELDRQ-----KRISNTRKMIEDLQSELktaencENLQPQIDTVTNDlrrVQEEKALCEGEIIDKQRE----- 427
Cdd:TIGR01612 1642 DTELKENGDNLNSlqeflESLKDQKKNIEDKKKEL------DELDSEIEKIEID---VDQHKKNYEIGIIEKIKEiaian 1712
|
250 260
....*....|....*....|...
gi 358248335 428 KEMLEKQRRSVSDHITRFDNLMN 450
Cdd:TIGR01612 1713 KEEIESIKELIEPTIENLISSFN 1735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
214-378 |
5.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 214 ELKNFREKEKQLEtscKEKTEYLEKMVQRNERYKQDVERFYERKRHLDLIEM-LEAKRPwveyENVRQEYEGVKLIRDRV 292
Cdd:COG3883 59 ELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYRSGGSVSYLDVlLGSESF----SDFLDRLSALSKIADAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 293 KEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKR 372
Cdd:COG3883 132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
....*.
gi 358248335 373 ISNTRK 378
Cdd:COG3883 212 AAAAAA 217
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
230-429 |
5.83e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 230 KEKTEYLEKMVQrnerykqDVERFYERKRH---LDLIEMLEA-KRPWVEYENVRQEYEGVKLIR----------DRVKEE 295
Cdd:NF033838 61 KEVESHLEKILS-------EIQKSLDKRKHtqnVALNKKLSDiKTEYLYELNVLKEKSEAELTSktkkeldaafEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 296 VRKLKEGQIPMTRRIEEI----------DRQRH------TLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQAL 359
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAekkakdqkeeDRRNYptntykTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKV 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358248335 360 TVKQnEELDRQKRISNTRKMIEDLQSELKTAENCENLQPQIDTVTND-LRRVQEEKALCEGEIIDKQREKE 429
Cdd:NF033838 214 ESKK-AEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDkPKRRAKRGVLGEPATPDKKENDA 283
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
649-926 |
6.81e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 649 LEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNL 728
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 729 EEEERKASTKIKEINvQKAKLVTELTGLVKictsfqiQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDN 808
Cdd:PRK03918 265 EERIEELKKEIEELE-EKVKELKELKEKAE-------EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 809 RQR---LLQKCKELMKKArqvcnlsadqavpqefqtqvptipnghsssppMAFQDLPNTLDEIDALLTEERSRASCFTGL 885
Cdd:PRK03918 337 EERleeLKKKLKELEKRL--------------------------------EELEERHELYEEAKAKKEELERLKKRLTGL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 358248335 886 NPSVV----EEYSKREVEIQQLTEELQGKKVELD----EYRENISQVKE 926
Cdd:PRK03918 385 TPEKLekelEELEKAKEEIEEEISKITARIGELKkeikELKKAIEELKK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
650-942 |
7.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 650 EQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNLE 729
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 730 EEERKASTKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDNR 809
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 810 QRLLQkckELMKKARQVCNLSADQAVPQEFQTQvptipnghsssppmAFQDLPNTLDEIDALLTEERSRAscftglnpSV 889
Cdd:COG1196 382 EELAE---ELLEALRAAAELAAQLEELEEAEEA--------------LLERLERLEEELEELEEALAELE--------EE 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 358248335 890 VEEYSKREVEIQQLTEELQGKKVELDEYRENISQVKERWLNPLKELVEKINEK 942
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
288-459 |
8.01e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 288 IRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEEL 367
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 368 DRQKRISNTRKMIEDLQSELktaencENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDN 447
Cdd:COG4372 98 QAQEELESLQEEAEELQEEL------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170
....*....|..
gi 358248335 448 LMNQKEDKLRQR 459
Cdd:COG4372 172 ELQALSEAEAEQ 183
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
208-440 |
8.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 208 MHRYHCELKNFREKEKQL---ETSCKEKTEYLEKMVQRNER---YKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQE 281
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIeekERKLRKELRELEKVLKKESElikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 282 YEGVKLIRDRVKEEVRKLKE---GQIPMTRRIEEIDRQRHTLEVRIKEKS------------------------------ 328
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneylelkdaeke 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 329 ------------TDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRisNTRKMIEDLQSELKTAENcenl 396
Cdd:PRK03918 614 lereekelkkleEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEK---- 687
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 358248335 397 qpQIDTVTNDLRRVQEEKalceGEIIDKQREKEMLEKQRRSVSD 440
Cdd:PRK03918 688 --RREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEE 725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-459 |
1.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 274 EYENVRQEYEGVKLIRDRVKEEVRKLKEgqipmtrRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIK 353
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 354 E--------------LQQALTVKQNEE-LDRQKRIS----NTRKMIEDLQSELKTAENCE-NLQPQIDTVTNDLRRVQEE 413
Cdd:COG3883 90 EraralyrsggsvsyLDVLLGSESFSDfLDRLSALSkiadADADLLEELKADKAELEAKKaELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 358248335 414 KALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQR 459
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
53-95 |
1.38e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 358248335 53 IVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICL 95
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRL 45
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
53-172 |
1.95e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 41.40 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 53 IVRIAMENFLTY-DICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMgRADKVGFFVKRGC------SKGLVEI 125
Cdd:cd03275 1 LKRLELENFKSYkGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHL-RSKNLKDLIYRARvgkpdsNSAYVTA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 358248335 126 ELFRTSGN-LIITREIdvIKNQSFWFINKKPVTQKIVEEQVAALNIQV 172
Cdd:cd03275 80 VYEDDDGEeKTFRRII--TGGSSSYRINGKVVSLKEYNEELEKINILV 125
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
650-749 |
2.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 650 EQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASI----------R 719
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakeI 158
|
90 100 110
....*....|....*....|....*....|.
gi 358248335 720 LMEQdtcnLEEE-ERKASTKIKEInVQKAKL 749
Cdd:PRK12704 159 LLEK----VEEEaRHEAAVLIKEI-EEEAKE 184
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-453 |
2.20e-03 |
|
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: 42.41 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 163 EQVAALNIQVGNLCQFLpqDKVGEFAKLSKIELlEATEKSVGPPEmhryhcelKNFREKEKQLETSCKEKTeyleKMVQR 242
Cdd:pfam15921 461 EKVSSLTAQLESTKEML--RKVVEELTAKKMTL-ESSERTVSDLT--------ASLQEKERAIEATNAEIT----KLRSR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 243 NERYKQDVERFYERKRHLdliemleakrpwveyENVRQEYEGVKLI---RDRVKEEVRKLKEGqipMTRRIEEIDRQRHT 319
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHL---------------RNVQTECEALKLQmaeKDKVIEILRQQIEN---MTQLVGQHGRTAGA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 320 LEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELktaencENLQPQ 399
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER------DQLLNE 661
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 358248335 400 IDTVTNDLRRVQEEKALCEGEIIDKQREKEM----LEKQRRSVSDHITRFDNLMNQKE 453
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKSME 719
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
53-117 |
3.15e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 3.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358248335 53 IVRIAMENFLTYDICEV--SPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRG 117
Cdd:COG3950 3 IKSLTIENFRGFEDLEIdfDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNG 69
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
214-468 |
3.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 214 ELKNFREKEKQLETSCKEKTEYLEKmVQRNERYKQDVERFYERKRHLDLIEMLEAKRpwveYENVRQEYEGVKLIR--DR 291
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEEEKKMKaeEA 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 292 VKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKelQQALTVKQNEELDRQK 371
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 372 RISNTRKmiedlQSELKTAENCENLQPQIDTVTNDLRRVQEEKALcEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQ 451
Cdd:PTZ00121 1691 AEALKKE-----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKI-KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
250
....*....|....*..
gi 358248335 452 KEDKLRQRYRDTYDAVL 468
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVI 1781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
214-372 |
3.80e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 214 ELKNFREKEKQLETSCKEKTEYLEKMV---QRNERYK--------QDVERFYERKRHLDLIemleakrpwveYENVRQEY 282
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralYRLGRQPplalllspEDFLDAVRRLQYLKYL-----------APARREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 283 EGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVK 362
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
170
....*....|
gi 358248335 363 QNEELDRQKR 372
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
219-409 |
3.94e-03 |
|
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: 41.17 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 219 REKEKQLETSCKEKTEYLEKMVQRNERYKQDVERfyeRKRHLDLIEmlEAKrpwveyENVRQEYEGVKLIRDRVKEEVRK 298
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELEELKEQNEELEKQYKV---KKKTLDLLP--DAE------ENIAKLQALVDASAQRLVELAGQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 299 LKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTvKQNEELDRQ---KRI-- 373
Cdd:pfam05667 424 WEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE-RLPKDVSRSaytRRIle 502
|
170 180 190
....*....|....*....|....*....|....*...
gi 358248335 374 --SNTRKMIEDLQselKTAENCENLQPQIDTVTNDLRR 409
Cdd:pfam05667 503 ivKNIKKQKEEIT---KILSDTKSLQKEINSLTGKLDR 537
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
329-412 |
3.94e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 329 TDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKTAEncENLQPQIDTVTNDLR 408
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE--AEIEERREELGERAR 93
|
....
gi 358248335 409 RVQE 412
Cdd:COG3883 94 ALYR 97
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
952-1074 |
5.49e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.77 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 952 CAGEVDLHTENEEDYDKYGIRIRVKFRSstQLheltphhqSGGERSVSTMLYLMALQelnrCPFRVVDEINQGMDPINER 1031
Cdd:cd00267 52 TSGEILIDGKDIAKLPLEELRRRIGYVP--QL--------SGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRE 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 358248335 1032 RVFEMVVNTACKENTsqYFFITPKLLQNLPYSEKmtVLFVYNG 1074
Cdd:cd00267 118 RLLELLRELAEEGRT--VIIVTHDPELAELAADR--VIVLKDG 156
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-385 |
5.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 209 HRYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNE-RYKQDVERFYERKRHLDLIEM-LEAKRpwVEYENVRQEYEGVK 286
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAeLEELR--AELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 287 LIRDRVKEEVRKLKE-----GqipmTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCK------------------QRQD 343
Cdd:COG4913 316 ARLDALREELDELEAqirgnG----GDRLEQLEREIERLERELEERERRRARLEALLAalglplpasaeefaalraEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 358248335 344 LIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQS 385
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-455 |
8.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 171 QVGNLCQFLPQDKVGEFAKLSKIELLEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDV 250
Cdd:PTZ00121 1065 HVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 251 ERFYERKRHLDLIEMLEAKRPWVEY---ENVRQEYEGVKLIRDRVKEEVRKLKEgqipmTRRIEEIDR---QRHTLEVRI 324
Cdd:PTZ00121 1145 ARKAEDAKRVEIARKAEDARKAEEArkaEDAKKAEAARKAEEVRKAEELRKAED-----ARKAEAARKaeeERKAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 325 KEKSTDIKEASQkckqrqdlIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKTAENCENLQPQIDTVT 404
Cdd:PTZ00121 1220 AEDAKKAEAVKK--------AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 358248335 405 NDLRRVQEEKALCEgEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDK 455
Cdd:PTZ00121 1292 ADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
52-127 |
8.55e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 39.76 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 52 SIVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAI-CLGLAG-----KPAFMGRADKVGFFVKRGCSKGLVEI 125
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIyLLAPGRshrtaRDKELIRFGAEAAVIHGRVEKGGREL 81
|
..
gi 358248335 126 EL 127
Cdd:PRK00064 82 PL 83
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
207-476 |
9.24e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 207 EMHRYHCELKNFREKEKQLETSC-------KEKTEYLEKMVQRNERYKQDVERFYERK-RHLDLIEMLEAKRPWV--EYE 276
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCdklllenKELTQEASDMTLELKKHQEDIINCKKQEeRMLKQIENLEEKEMNLrdELE 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 277 NVRQEYegvKLIRDRVKEEVRKLKEgqipmtrrieeidrQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQ 356
Cdd:pfam05483 552 SVREEF---IQKGDEVKCKLDKSEE--------------NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 357 QALTVKQNEELDRQKRISNTRKMIEDLQSELKTAEncENLQPQIDTVTNDL--RRVQEEKALCEGE----IIDK--QREK 428
Cdd:pfam05483 615 QENKALKKKGSAENKQLNAYEIKVNKLELELASAK--QKFEEIIDNYQKEIedKKISEEKLLEEVEkakaIADEavKLQK 692
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 358248335 429 EMLEKQRRSVSDHITRFDNLMNQKEDKLRQRyrdtyDAVLWLRNNRDR 476
Cdd:pfam05483 693 EIDKRCQHKIAEMVALMEKHKHQYDKIIEER-----DSELGLYKNKEQ 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
650-834 |
9.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 650 EQRRHLEEQLKEMNRQLEAVDsglAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDT---- 725
Cdd:COG4942 48 KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358248335 726 ----CNLEEEERKA---STKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVT 798
Cdd:COG4942 125 llspEDFLDAVRRLqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
170 180 190
....*....|....*....|....*....|....*.
gi 358248335 799 EQQFIELDDNRQRLLQKCKELMKKARQVCNLSADQA 834
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| |
