|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
2620-2820 |
2.60e-109 |
|
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: 346.66 E-value: 2.60e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2620 FQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA 2699
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2700 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2779
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1676318895 2780 EQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2820
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2618-2824 |
9.49e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2618 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKT---IAQM-IEDEQREKSVshQTVQQLV 2693
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2694 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2768
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676318895 2769 ------------EIAQVRGKAQQEQAAHQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2824
Cdd:PRK03918 341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2625-2814 |
1.46e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2625 LDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKT---IAQMIEDEQREKsvshqtvQQLVLEKEQALA 2701
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQK-------QILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2702 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVH---AEEKLDRANAEIAQVRGKAQ 2778
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIA 396
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1676318895 2779 qeqaahqaSLRKEQLRVDA----LERTLEQKNKEIEELTK 2814
Cdd:TIGR02168 397 --------SLNNEIERLEArlerLEDRRERLQQEIEELLK 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2461-2818 |
2.35e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2461 NETKFSSPTEE-LDYRNSYEIEYMEKIGSSLPQDDDAPKKQALYLMFDTSQESPVKS-SPVRMSESPTPcSGSSFEETEA 2538
Cdd:PTZ00121 1006 NHFSFTALTANtIDFNQNFNIEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAkAHVGQDEGLKP-SYKDFDFDAK 1084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2539 LVNTAAKNQHPVPRGLAPNQESHLQVPEKSSQKElEAMGLGTPSEAIE-------------IREAAHPTDVSISKTALYS 2605
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAE-EAKKKAEDARKAEearkaedarkaeeARKAEDAKRVEIARKAEDA 1163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2606 RigTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREV--SEWKDKYEESRR-----------------EVMEMRKIVAE 2666
Cdd:PTZ00121 1164 R--KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDArkAEAARKAEEERKaeearkaedakkaeavkKAEEAKKDAEE 1241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2667 YEKTIAQMIEDEQR---EKSVSHQTVQQLVLEKEQAL-AD--LNSVEKSLADLFRRYEKMKEVLEGFRKNEEvlKRCAQE 2740
Cdd:PTZ00121 1242 AKKAEEERNNEEIRkfeEARMAHFARRQAAIKAEEARkADelKKAEEKKKADEAKKAEEKKKADEAKKKAEE--AKKADE 1319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676318895 2741 YLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQeqaahqasLRKEQLRVDALERTLEQKNKEIEELTKICDE 2818
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2625-2823 |
4.01e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2625 LDSALQIARAEIITKE-REVSEWKDKYEESRREVMEMRKIVAEYEKTIAQmiedeqreksvshqtvqqlVLEKEQALADL 2703
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEE-------------------LEELEEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2704 NSVEKSLADLFRRYEKMKEVLEGFRKNEEvLKRCAQEYLSRVKKEEQRYQALKvHAEEKLDRANAEIAQVRGKAQQEQAA 2783
Cdd:COG4717 108 EAELEELREELEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1676318895 2784 HQASLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAKM 2823
Cdd:COG4717 186 LSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
15-468 |
4.47e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 15 SAQTPRSA-QPPGNSQNIKRKQQDTPGSPdhrdASSIGSVGLGGFCTASESSASLDPCLVSPEVTEPRKDPQGARGPEGS 93
Cdd:PHA03247 2567 SVPPPRPApRPSEPAVTSRARRPDAPPQS----ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP 2642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 94 LLPSPPPSQEREHPSssmpfaecPPEGCLASPAAAPEDGPQTQSPRREPAPnapgdiaaafPAERDSSTPYQEIAAVPSA 173
Cdd:PHA03247 2643 PPTVPPPERPRDDPA--------PGRVSRPRRARRLGRAAQASSPPQRPRR----------RAARPTVGSLTSLADPPPP 2704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 174 GRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLREPMKAPLCGEGDQPGGFESQEKEA--------------AGGFPPAES 239
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPttagppapappaapAAGPPRRLT 2784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 240 RQGVASVQVT------PEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLTD-------DLEF 306
Cdd:PHA03247 2785 RPAVASLSESreslpsPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggDVRR 2864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 307 LRACHLPRSNSGAAPEAEVNAASQESCQQPVGAYLPHAELPWGLPSPALVPEAGGSGKEALDTIDVQGHPQTGMRGTKPN 386
Cdd:PHA03247 2865 RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 387 QVVCVAAGGQPEGGLPvSPEPSLLTPTEEAHPaSSLASFPAAQIPIAVEEPGSSSRESVSKAGMPVSADAAKEVVDAGLV 466
Cdd:PHA03247 2945 PTTDPAGAGEPSGAVP-QPWLGALVPGRVAVP-RFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPV 3022
|
..
gi 1676318895 467 GL 468
Cdd:PHA03247 3023 SL 3024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2624-2821 |
1.09e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2624 DLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADL 2703
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2704 NSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2783
Cdd:COG1196 326 AELEEELEEL---EEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190
....*....|....*....|....*....|....*...
gi 1676318895 2784 HQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2821
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2610-2814 |
1.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2610 AEVEKPAGLLFQQPDLDSALQIARAEIITKEREV--SEWKDKYEESR----REVMEMRKIVAEYEKTIAQMIEDEQREKS 2683
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKkkAEEAKKAEEDKnmalRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2684 VSHQTVQQLVLEKEQaLADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLK-RCAQEylsRVKKEEQRYQALKVHAEEK 2762
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEE-LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEE---AKKAEEDKKKAEEAKKAEE 1685
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1676318895 2763 LDRANAE-----------IAQVRgKAQQEQAAHQASLRKEQ----LRVDALERTLEQKNKEIEELTK 2814
Cdd:PTZ00121 1686 DEKKAAEalkkeaeeakkAEELK-KKEAEEKKKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2624-2822 |
2.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2624 DLDSALQIARAEIITKEREV--SEWKDKYEESRREvmEMRKIVAEYEKTIAQMIEdEQREKSVSHQTVQQLVLEKEQALA 2701
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2702 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 2781
Cdd:PTZ00121 1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1676318895 2782 AAHQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2822
Cdd:PTZ00121 1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2633-2812 |
2.59e-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: 53.52 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2633 RAEIITKEREVseWKDKYEESRREVMEMRKIVAEYEktiaQMIEDEQREKSVSHQTVQQLVL---EKEQALADLNSVEKS 2709
Cdd:TIGR02168 219 KAELRELELAL--LVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLevsELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2710 LADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaahqasLR 2789
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LE 361
|
170 180
....*....|....*....|...
gi 1676318895 2790 KEQLRVDALERTLEQKNKEIEEL 2812
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETL 384
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2633-2822 |
3.35e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2633 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMiEDEQreksvshQTvQQLVLEKEQALadlnsVEKsLAD 2712
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK-IKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2713 LFRRYEKMKEVLEGFRKNEEVLKRCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVRGKAQqeqaahqaSLRKE- 2791
Cdd:COG1340 145 LEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAD--------ELRKEa 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1676318895 2792 ----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2822
Cdd:COG1340 212 delhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2602-2805 |
4.52e-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: 52.75 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2602 ALYSRIGTAEV------EKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMi 2675
Cdd:TIGR02168 292 ALANEISRLEQqkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2676 EDEQREKSVSHQTVQQLVLEKEQALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKRCAQEYLSRVKKEEQ 2750
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1676318895 2751 RYQALKVHAEEKLDRANAEIAQVRgkaqQEQAAHQASLRKEQLRVDALERTLEQK 2805
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAE----QALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2633-2814 |
5.57e-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: 52.37 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2633 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKS 2709
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2710 LADLfrrYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLR 2789
Cdd:TIGR02168 756 LTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180
....*....|....*....|....*...
gi 1676318895 2790 K---EQLRVDALERTLEQKNKEIEELTK 2814
Cdd:TIGR02168 832 RiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2632-2821 |
7.16e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2632 ARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIED-----EQREKSVSHQTVQQ---------LVLEKE 2697
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2698 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRGK 2776
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLERS 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1676318895 2777 AQQEQAAHQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2821
Cdd:TIGR02169 310 IAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2618-2820 |
9.70e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2618 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQ-------REKSVSHQTVQ 2690
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekiGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2691 QLVLEKEQALADLnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEi 2770
Cdd:TIGR02169 308 RSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE- 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2771 aqvrgkaqqeqaahqasLRKEQlrvDALERTLEQKNKEIEELTKICDELI 2820
Cdd:TIGR02169 383 -----------------TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2621-2822 |
1.09e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2621 QQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIaqmiedEQREKSVSHQTVQQLVLEKEQAL 2700
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL------EAQKEELAELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2701 ADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2780
Cdd:COG4942 123 ALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1676318895 2781 qaahqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2822
Cdd:COG4942 201 -------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2611-2819 |
1.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2611 EVEKPAGLLFQQPdldSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQ 2690
Cdd:PRK03918 311 EIEKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2691 QLVLE-------KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRK------------NEEVLKRCAQEYLSRVKKEEQR 2751
Cdd:PRK03918 388 KLEKEleelekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1676318895 2752 YQALKvHAEEKLDRANAEIAQVRGKAQQ--EQAAHQASLR--KEQLRVDALERtLEQKNKEIEELTKICDEL 2819
Cdd:PRK03918 468 LKEIE-EKERKLRKELRELEKVLKKESEliKLKELAEQLKelEEKLKKYNLEE-LEKKAEEYEKLKEKLIKL 537
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2586-2814 |
1.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2586 EIREAAHPTDVSISKTALYSRIGTAEVEKPAGLlFQQPDLDSALQIARAEiitKEREVSEWKDKYEESRREVMEMRKIVA 2665
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL-YEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2666 EYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA--LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYls 2743
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-- 1721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2744 RVKKEEQRYQALKVHAEEKLDRANAEIAQVR-------GKAQQEQAAHQASLRKEQLRV--DALERTLEQKNKEIEELTK 2814
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkiAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
87-668 |
2.30e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 87 ARGPEGSLLPSPPPSQerehPSSSMPFAEC---PPEGCLASPAAAPEDGPQTQSPRrepapnAPGDIAAAFPAerdsstP 163
Cdd:PHA03247 2548 AGDPPPPLPPAAPPAA----PDRSVPPPRPaprPSEPAVTSRARRPDAPPQSARPR------APVDDRGDPRG------P 2611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 164 YQEIAAVPSAGRERQPKEEGQKSSFSFSSGidqSPGMSPVPLRePMKAPLCGEGDQPGGFESQEKEAAGGFPPAESRQGV 243
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPH---PPPTVPPPER-PRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA 2687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 244 ASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAP-RASDRERGQGEAPPqyltddleflrachlPRSNSGAAPE 322
Cdd:PHA03247 2688 ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAaRQASPALPAAPAPP---------------AVPAGPATPG 2752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 323 AEVNAASQESCQQPVGAYLPHAelPWGLPSPALVPEAGGSGKEALDTIDVQGHPqtgmrgTKPNQVVCVAAGGQPEGGLP 402
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAA--PAAGPPRRLTRPAVASLSESRESLPSPWDP------ADPPAAVLAPAAALPPAASP 2824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 403 VSPEPSLLTPTEEAHPASSLASFPAAQIPIAVEEPGSSSRESVSKAGMPVSADAAKEVVDaglvglerqvsdlgskgehp 482
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVR-------------------- 2884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 483 egdpgEVPAPSPQERGEHLNTEQSHEVQPGVPPPPLPKEQSHEVQPGAPPPPLPKAPSESARGPPGPTDGAKVHEDSTSP 562
Cdd:PHA03247 2885 -----RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 563 AVAKEGSRSPGD---------SPGGKEEAPEPP-----DGGDPGNLQGEDSQAFSSKRDP-EVGKDELSKPSSDAESRDH 627
Cdd:PHA03247 2960 PQPWLGALVPGRvavprfrvpQPAPSREAPASStppltGHSLSRVSSWASSLALHEETDPpPVSLKQTLWPPDDTEDSDA 3039
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1676318895 628 PSSHSAQPPRKGGAG---HTDGPHSQTAEADASGLPHKLGEEDP 668
Cdd:PHA03247 3040 DSLFDSDSERSDLEAldpLPPEPHDPFAHEPDPATPEAGARESP 3083
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2633-2821 |
2.52e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2633 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAE------YEKTIAQMIEDEQREKSVSHQTV----------------- 2689
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELekkaeeyeklkeklikl 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2690 --QQLVLEKEqaLADLNSVEKSLADLFRRYEKMKEVL---------EGFRKNEEV------LKRCAQEYL------SRVK 2746
Cdd:PRK03918 538 kgEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELaellkeleeLGFESVEELeerlkeLEPFYNEYLelkdaeKELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2747 KEEQRYQALK---VHAEEKLDRANAEIAQVRGK----AQQEQAAHQASLRKEQLRvdaLERTLEQKNKEIEELTKICDEL 2819
Cdd:PRK03918 616 REEKELKKLEeelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEI 692
|
..
gi 1676318895 2820 IA 2821
Cdd:PRK03918 693 KK 694
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2629-2770 |
3.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2629 LQIARAEIITKEREVSEWKDKYEESRREVMEMRKI--VAEYEKtiaqmIEDEQREKSVSHQTVQQlvlEKEQALADLNSV 2706
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676318895 2707 EKSLADLFRRYEKMKEVlegfRKNEEVLKRcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2770
Cdd:PRK03918 693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2651-2814 |
4.21e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2651 EESRREVMEMRKIVAEYEKTIAQmIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 2730
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2731 EEVLkrcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaahqaslRKEQLRvdALERTLEQKNKEIE 2810
Cdd:COG4372 110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEELK--ELEEQLESLQEELA 167
|
....
gi 1676318895 2811 ELTK 2814
Cdd:COG4372 168 ALEQ 171
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2633-2825 |
4.85e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2633 RAEIITkerEVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIE------DEQREKSVSHQTVQQLVLEKEQALADLNSV 2706
Cdd:COG1340 31 RDELNE---ELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2707 EKSLADLFRRYEKMK-----EVLeGFRKNEEVLKRCAQ--EYLSRVKKEEQ----------RYQALKVHAE--------- 2760
Cdd:COG1340 108 GGSIDKLRKEIERLEwrqqtEVL-SPEEEKELVEKIKEleKELEKAKKALEkneklkelraELKELRKEAEeihkkikel 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676318895 2761 -EKLDRANAEIAQVRGKaqqeqaahQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2825
Cdd:COG1340 187 aEEAQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2628-2822 |
7.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2628 ALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVE 2707
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2708 KSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAHQ 2785
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEAL 444
|
170 180 190
....*....|....*....|....*....|....*..
gi 1676318895 2786 ASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2822
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2628-2812 |
8.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2628 ALQIARAEIITKEREVSEWKDKYEESRREVMEMRKI----------------VAEYEKTIAQmIEDEQREKSVSHQTVQQ 2691
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2692 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 2771
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1676318895 2772 QvrgkaqqeqaahqaSLRKeqlRVDALERTLEQKNKEIEEL 2812
Cdd:COG4913 769 E--------------NLEE---RIDALRARLNRAEEELERA 792
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2619-2811 |
9.28e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2619 LFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM----------IEDEQREKSVSHQT 2688
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAqaelaqaqeeLESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2689 VQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLkrcaQEYLSRVKKEEQRYqaLKVHAEEKLDRANA 2768
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL----QEELAALEQELQAL--SEAEAEQALDELLK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1676318895 2769 EIAqvRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEE 2811
Cdd:COG4372 191 EAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2571-2774 |
1.13e-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: 48.14 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2571 KELEAMGLGtpsEAIEIREAAHPTDVSISKT----ALY----------SRIGTAEVEKpagLLFQQPDLDSALQIARAEI 2636
Cdd:TIGR02169 279 KKIKDLGEE---EQLRVKEKIGELEAEIASLersiAEKereledaeerLAKLEAEIDK---LLAEIEELEREIEEERKRR 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2637 ITKEREVSEWKDKYEESRREVMEM-------RKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQALADLNSV 2706
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKLkreINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676318895 2707 EKSLADLfrrYEKMKEVLEGFRKNEEVLKRCAQEylsrVKKEEQRYQALKvhaeEKLDRANAEIAQVR 2774
Cdd:TIGR02169 433 EAKINEL---EEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLK----EEYDRVEKELSKLQ 489
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
73-475 |
1.55e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.29 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 73 VSPEVTEPRKDPQGARGPEGSLLPSP----PPSQEREHPSSSMPFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPG 148
Cdd:PRK07764 387 VAGGAGAPAAAAPSAAAAAPAAAPAPaaaaPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 149 DIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQS--PGMSPVPLREPMKAPLCGEGDQPGGFESQ 226
Cdd:PRK07764 467 APAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERwpEILAAVPKRSRKTWAILLPEATVLGVRGD 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 227 E---KEAAGGFPPAESRQGVASV-----------QVTPEA-----PAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASD 287
Cdd:PRK07764 547 TlvlGFSTGGLARRFASPGNAEVlvtalaeelggDWQVEAvvgpaPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAA 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 288 RERGQGEAPPQYLTDDleflRACHLPRSNSGAAPEAEVNAASQESCQQPVGAYLPHAELPWGLPSPALVPEAGGSGKEAL 367
Cdd:PRK07764 627 PAPAGAAAAPAEASAA----PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 368 DTIDVQGHPQTGMRGTKPNQVVCVAAGGQPEGGLPVSPEPSllTPTEEAHPASSLASFPAAQIPIAVEEPGSSSRESVSK 447
Cdd:PRK07764 703 PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPP--EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
|
410 420
....*....|....*....|....*...
gi 1676318895 448 AGMPVSADAAKEVVDAGLVGLERQVSDL 475
Cdd:PRK07764 781 EEEEMAEDDAPSMDDEDRRDAEEVAMEL 808
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2630-2804 |
1.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2630 QIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQ-TVQQLVLEKEQALADLNSVEK 2708
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2709 SLADLFRRYEKMKEVLEGFRKNEEVLKRCAQE--------------YLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVR 2774
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEEleelleqlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190
....*....|....*....|....*....|
gi 1676318895 2775 GKAQQEqaahqaslrKEQLRVDALERTLEQ 2804
Cdd:COG4717 227 EELEQL---------ENELEAAALEERLKE 247
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2630-2822 |
3.37e-04 |
|
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: 45.68 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2630 QIARAEIITKEREvsewkdkyEESRREVMEMRKivaEYEKTIAQMIEDEQREKSVSHQTVQQLV-----------LEKEQ 2698
Cdd:pfam13868 27 QIAEKKRIKAEEK--------EEERRLDEMMEE---ERERALEEEEEKEEERKEERKRYRQELEeqieereqkrqEEYEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2699 ALADLNSV--------EKSLADLFRRYEKMKEVLEGFRK-NEEVLKRCAQEYLsRVKKEEQRYQAlkvHAEEKLDRANAE 2769
Cdd:pfam13868 96 KLQEREQMdeiveriqEEDQAEAEEKLEKQRQLREEIDEfNEEQAEWKELEKE-EEREEDERILE---YLKEKAEREEER 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1676318895 2770 IAQVRGKAqqeqaahqaslRKEQLRVDALERTLEQKNKEIEELtkicDELIAK 2822
Cdd:pfam13868 172 EAEREEIE-----------EEKEREIARLRAQQEKAQDEKAER----DELRAK 209
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
238-602 |
3.93e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 238 ESRQGVASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLTDDLEFLRACHLPRSNS 317
Cdd:PRK07764 382 ERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 318 GAAPEAEVNAASQESCQQPVGAYLPHAElPWGLPSPALVPEAGGSGKEAlDTID-------------------------- 371
Cdd:PRK07764 462 PSAQPAPAPAAAPEPTAAPAPAPPAAPA-PAAAPAAPAAPAAPAGADDA-ATLRerwpeilaavpkrsrktwaillpeat 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 372 ---------VQGHPQTGMRG--TKPN-----------------QVVCVAAGGQPEGGLPVSPEP-SLLTPTEEAHPASSL 422
Cdd:PRK07764 540 vlgvrgdtlVLGFSTGGLARrfASPGnaevlvtalaeelggdwQVEAVVGPAPGAAGGEGPPAPaSSGPPEEAARPAAPA 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 423 ASF--PAAQIPIAVEEPGSSSRESVSKAGMPVSADAAKEVVDAGLVGLERQVSDLGSKGEHPEGDPGEVPAPSPQERGeh 500
Cdd:PRK07764 620 APAapAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA-- 697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 501 lnteQSHEVQPGVPPPPLPKEQSHEVQPGAPPPPLPKAPSESARG---------PPGPTDGAKVHEDSTSPAVAKEGSRS 571
Cdd:PRK07764 698 ----PAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvplppepddPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
410 420 430
....*....|....*....|....*....|.
gi 1676318895 572 PGDSPGGKEEAPEPPDGGDPGNLQGEDSQAF 602
Cdd:PRK07764 774 PPPSPPSEEEEMAEDDAPSMDDEDRRDAEEV 804
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2566-2822 |
4.39e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2566 EKSSQKELEAmglgtpSEAIEIREAAHPTDVSISKTALYSRIGT---AEVEKPAGLLFQQPDLDSALQIARAEIITKERE 2642
Cdd:PTZ00121 1233 EEAKKDAEEA------KKAEEERNNEEIRKFEEARMAHFARRQAaikAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2643 V---SEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALAD--LNSVEKSLADLFRRY 2717
Cdd:PTZ00121 1307 AkkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAekKKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2718 EKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVR----GKAQQEQAAHQASLRK- 2790
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKkadeAKKKAEEAKKAEEAKKk 1465
|
250 260 270
....*....|....*....|....*....|....
gi 1676318895 2791 --EQLRVDALERTLEQKNKEiEELTKICDELIAK 2822
Cdd:PTZ00121 1466 aeEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKK 1498
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2609-2814 |
6.92e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2609 TAEVEKPAGLLFQQPDLDSALQIARAEII---------TKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIED-- 2677
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIEnivgevelsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtl 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2678 -EQREKSVSHQT-VQQLVLEKEQALADLNSVEKSLADLFRR---------YEKMKEVLEGFRKNEEVLKRcaqeylsRVK 2746
Cdd:COG5185 416 kAADRQIEELQRqIEQATSSNEEVSKLLNELISELNKVMREadeesqsrlEEAYDEINRSVRSKKEDLNE-------ELT 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676318895 2747 KEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTK 2814
Cdd:COG5185 489 QIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNA 556
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2570-2818 |
8.17e-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: 44.96 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2570 QKELEAMGLGTPSEAIEIREAAhptdvSISKtalYSRIGTAEVEKpaglLFQqpdldsaLQIARAEIITKEREVsewkdk 2649
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEEEA-----AGSR---LKRKKKEALKK----LIE-------ETENLAELIIDLEEL------ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2650 yEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTV--QQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGF 2727
Cdd:pfam02463 196 -KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2728 RKNEEVLK-----------RCAQEYLSRVKKEEQRYQALK--VHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQL- 2793
Cdd:pfam02463 275 KEEEKEKKlqeeelkllakEEEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAe 354
|
250 260
....*....|....*....|....*...
gi 1676318895 2794 ---RVDALERTLEQKNKEIEELTKICDE 2818
Cdd:pfam02463 355 eeeEEELEKLQEKLEQLEEELLAKKKLE 382
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
221-695 |
8.47e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 221 GGFESQEKEAAGGFPPAESRQGVASVQVTPEAPAAAqqgtesSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEAPP--- 297
Cdd:PHA03307 17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAA------VTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTptw 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 298 QYLTDDLEFLRACHLPRSNSGAAPEAEVNAASQESCQQPVGAYLPHAELPWGLPSPALVPEAGGSGkealdtidvqghpq 377
Cdd:PHA03307 91 SLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAG-------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 378 tgmrgtkpnqvvcvAAGGQPEGGLPVSPEPSLLTPTEEAH---PASSLASFPAAQIPIAVEEPGSS-SRESVSKAGMPVS 453
Cdd:PHA03307 157 --------------ASPAAVASDAASSRQAALPLSSPEETaraPSSPPAEPPPSTPPAAASPRPPRrSSPISASASSPAP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 454 ADAAKEVVDAG-----LVGLERQVSDLGSKGEHPEGDPGEVPAPSPQERGEHLNTEQShevqpgvpppplpkEQSHEVQP 528
Cdd:PHA03307 223 APGRSAADDAGasssdSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSS--------------RPGPASSS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 529 GAPPPPLPKAPSESARGPPGPTDGAKVHEDSTSPAVAKEGSRSPGDSPGGKEEAPEPPDGGDPGNLQGEDSQAFSSKRDP 608
Cdd:PHA03307 289 SSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 609 EvgkdelskPSSDAESRDHPSSHSAQPPRKGGAGHTDGPHSQTAEADASGLPHKLGEEDPVLPPVPDGAGEPTVPEGAIW 688
Cdd:PHA03307 369 P--------RPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPW 440
|
....*..
gi 1676318895 689 EGSGLQP 695
Cdd:PHA03307 441 PGSPPPP 447
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2632-2765 |
8.68e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2632 ARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTI----AQMIE-----DEQREKSVS-HQTVQqlvlEKEQALA 2701
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAqelhEEMIElykeaDELRKEADElHKEIV----EAQEKAD 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1676318895 2702 DLNsveKSLADLFRRYEKMKEVLEGFRKNEEVLKRcaqeylsrvKKEEQRYQALKVHAEEKLDR 2765
Cdd:COG1340 227 ELH---EEIIELQKELRELRKELKKLRKKQRALKR---------EKEKEELEEKAEEIFEKLKK 278
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2632-2811 |
1.77e-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: 43.37 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2632 ARAEIITKEREVSEWKDKYEEsrREVMEMRKIvAEYEKTIAQ---MIEDEQREKSVSHQTVQQLVL-----------EKE 2697
Cdd:pfam13868 128 LREEIDEFNEEQAEWKELEKE--EEREEDERI-LEYLKEKAEreeEREAEREEIEEEKEREIARLRaqqekaqdekaERD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2698 QALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYlsRVKKEEQRYQALKVHAE-EKLDRANAE 2769
Cdd:pfam13868 205 ELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQEEAE 282
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1676318895 2770 iaQVRGKAQQEQAAHQASLR-KEQLRVDALERTLEQKNKEIEE 2811
Cdd:pfam13868 283 --KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2683-2825 |
1.81e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2683 SVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEgfRKNEEVLKrcAQEYLSRVKKEEQRYQALKVHAEEK 2762
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--QARSELEQ--LEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676318895 2763 LDRANAEIAQVRGKAQQEQAAHQA-SLRKEQL--RVDALERTLEQKNKEIEELTKICDELIAKMGK 2825
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDlEQQRKQLeaQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2639-2822 |
1.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2639 KEREVSEWKDKYEESRReVMEMRKIVAEYEKtiAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 2718
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKK-ADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2719 KMKEVLEgFRKNEEVLKRCAQEYLSRVKK-EEQRYQALKVHAEEKLDRA--NAEIA----QVRGKAQQEQAAHQASLRKE 2791
Cdd:PTZ00121 1532 EAKKADE-AKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMAlrKAEEAkkaeEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190
....*....|....*....|....*....|.
gi 1676318895 2792 QLRVDALERTLEQKNKEIEELTKICDELIAK 2822
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
69-299 |
2.02e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 69 DPCLVSPEVTEPRKDPQGARGPEGSLLPSPPPSQEREHPSSSMPFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPG 148
Cdd:PHA03307 131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 149 DIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLREPMKAPLCGEGDQPGGFESQEK 228
Cdd:PHA03307 211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 229 EAAGGFPPAESRQGV--------ASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPI--------PQDPAPRASDRERGQ 292
Cdd:PHA03307 291 PRERSPSPSPSSPGSgpapssprASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPsrspspsrPPPPADPSSPRKRPR 370
|
....*..
gi 1676318895 293 GEAPPQY 299
Cdd:PHA03307 371 PSRAPSS 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2627-2814 |
2.30e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2627 SALQIARAEIITKE--REVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM-------------IEDEQREKsvsHQTVQQ 2691
Cdd:TIGR04523 298 SDLNNQKEQDWNKElkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnsesenseKQRELEEK---QNEIEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2692 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKrcaQEYLSrVKKEEQRYQALKVHAEEKLDRANAEIA 2771
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ---QEKEL-LEKEIERLKETIIKNNSEIKDLTNQDS 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1676318895 2772 ----------QVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTK 2814
Cdd:TIGR04523 451 vkeliiknldNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
16-347 |
2.59e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 16 AQTPRSAQPPGNSQNIKRKQQDTPGSPDHRDASSIGSVGLGGFCTASESSASLDPCLVS---PEVTEPRKDPQGARGPEG 92
Cdd:PHA03307 118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLsspEETARAPSSPPAEPPPST 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 93 SLLPSPPPSQEREHPSSSmpFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPGDIAAAFPAERDSSTPYQEIAAVPS 172
Cdd:PHA03307 198 PPAAASPRPPRRSSPISA--SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 173 AGRERQPKEEGQKSSFSFSSGiDQSPGMSPVPLREPMKAPLCGEGDQP-----GGFESQEKEAAGGFPPAESRQGVASVQ 247
Cdd:PHA03307 276 NGPSSRPGPASSSSSPRERSP-SPSPSSPGSGPAPSSPRASSSSSSSRessssSTSSSSESSRGAAVSPGPSPSRSPSPS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 248 VTPEAPAAAQQGtessavleKSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLTDDLEFLRACHLPRSNSGAAPEAEVNA 327
Cdd:PHA03307 355 RPPPPADPSSPR--------KRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAF 426
|
330 340
....*....|....*....|
gi 1676318895 328 ASQESCQQPVGAYLPHAELP 347
Cdd:PHA03307 427 YARYPLLTPSGEPWPGSPPP 446
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
69-286 |
3.28e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 69 DPCLVSPEVTEPRKDPQGARGPEGSLLPSPPPSQEREHPSSSMPFAECPPEGCLASPAAA-PEDGPQTQSPRREPAPNAP 147
Cdd:PHA03307 52 AVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPsSPDPPPPTPPPASPPPSPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 148 GDIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLRE--PMKAPLCGEGDQPGGFES 225
Cdd:PHA03307 132 PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAepPPSTPPAAASPRPPRRSS 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676318895 226 QEKEAAGGFPPAESRQGVASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRAS 286
Cdd:PHA03307 212 PISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA 272
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2605-2776 |
4.11e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2605 SRIGTAEVEKpagllfqqpdlDSALQIARAEiitKEREVSEwkdkyEESRREVMEMRkiVAEYEKTIAQMIEDEQREKsv 2684
Cdd:COG2268 201 ARIAEAEAER-----------ETEIAIAQAN---REAEEAE-----LEQEREIETAR--IAEAEAELAKKKAEERREA-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2685 shqtvqqlvlEKEQALADLnSVEKsladlfRRYEKMKEV---LEGFRKNEEVLkrcAQEylSRVKKEEQRYQA---LKVH 2758
Cdd:COG2268 258 ----------ETARAEAEA-AYEI------AEANAEREVqrqLEIAEREREIE---LQE--KEAEREEAELEAdvrKPAE 315
|
170 180
....*....|....*....|..
gi 1676318895 2759 AE----EKLDRANAEIAQVRGK 2776
Cdd:COG2268 316 AEkqaaEAEAEAEAEAIRAKGL 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2689-2813 |
4.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2689 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVLKRC---AQEYLS-RVKKEEQRYQALKVH---AEE 2761
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLEPIrelAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1676318895 2762 KLDRANAEIAQVRgkaqqeqaahqASLRKEQLRVDALERTLEQKNKEIEELT 2813
Cdd:COG4913 289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2624-2823 |
4.56e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2624 DLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEyektiaqmIEDEQREKSVSHQTVQQLVLEKEQALA-- 2701
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------LEKEIKRLELEIEEVEARIKKYEEQLGnv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2702 ----DLNSVEKSLADLfrryEKMKEVLEgfrknEEVLkrcaqeylsrvkkeeqryqalkvHAEEKLDRANAEIAQVRGKA 2777
Cdd:COG1579 86 rnnkEYEALQKEIESL----KRRISDLE-----DEIL-----------------------ELMERIEELEEELAELEAEL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1676318895 2778 QQeqaahqaslRKEQLR--VDALERTLEQKNKEIEELTKICDELIAKM 2823
Cdd:COG1579 134 AE---------LEAELEekKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2625-2819 |
4.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2625 LDSALQIARAEIitkeREVSEW-KDKYEESRREVMEMRKIVAEYEKtiAQMIEDEQREKSVSHQTVQQLVLEKEQALADL 2703
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2704 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkrcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 2780
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1676318895 2781 QAAHQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 2819
Cdd:COG3206 311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2611-2820 |
7.14e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2611 EVEKpagllfQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQR--EKSVSHQT 2688
Cdd:PRK04778 307 YVEK------NSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERiaEQEIAYSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2689 VQqlvlekeqalADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLS-------RVKKEE-----QRYQALK 2756
Cdd:PRK04778 381 LQ----------EELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklheikrYLEKSNlpglpEDYLEMF 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1676318895 2757 VHAEEKLDRANAEIAQVRgkaqqeqaahqaslrkeqLRVDALERTLEQKNKEIEELTKICDELI 2820
Cdd:PRK04778 451 FEVSDEIEALAEELEEKP------------------INMEAVNRLLEEATEDVETLEEETEELV 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2621-2824 |
7.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2621 QQPDLDSalQIARAEIITK-EREVSEWKDKYEESRREVMEMRKIVAEYEKTI------AQMIEDEQREKSVSHQTVQQLV 2693
Cdd:PRK02224 490 EVEEVEE--RLERAEDLVEaEDRIERLEERREDLEELIAERRETIEEKRERAeelrerAAELEAEAEEKREAAAEAEEEA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2694 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKvhaeEKLDRanaeIAQV 2773
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA----EKRER----KREL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1676318895 2774 RGKAQQEqaahqaslRKEQLRVDA--LERTLEQKNKEIEELTKICDELIAKMG 2824
Cdd:PRK02224 640 EAEFDEA--------RIEEAREDKerAEEYLEQVEEKLDELREERDDLQAEIG 684
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2637-2825 |
7.76e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2637 ITKEREVSEWKDKYE----ESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQT-VQQLVLEKEQALADLNSVEKSLA 2711
Cdd:TIGR00618 245 LTQKREAQEEQLKKQqllkQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKaVTQIEQQAQRIHTELQSKMRSRA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2712 DLFRRY----------EKMKEVLEGFRKNEEVLKRCAQ------EYLSRVKKEEQRYQAL---KVHAEEKLDRANAEIAQ 2772
Cdd:TIGR00618 325 KLLMKRaahvkqqssiEEQRRLLQTLHSQEIHIRDAHEvatsirEISCQQHTLTQHIHTLqqqKTTLTQKLQSLCKELDI 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1676318895 2773 VRgKAQQEQAAHQASLRKEQLRVDALERT--LEQKNKEIEELTKICDELIAKMGK 2825
Cdd:TIGR00618 405 LQ-REQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAITCTAQCEKLEK 458
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
142-370 |
8.91e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 142 PAPNAPGDIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLREPMKAPLCGEGDQPG 221
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 222 GFESQEKEAAGGFPPAESRQGVASVQVTPEAPAAAQQGTESSAvlekSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLT 301
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG----QADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 302 DDLEFLRACHL-PRSNSGAAPEAEVNAASQESCQQPVGAYLPHAELPWGLPSPAlvpEAGGSGKEALDTI 370
Cdd:PRK07764 746 DDPPDPAGAPAqPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRR---DAEEVAMELLEEE 812
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
84-295 |
9.41e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 84 PQGARGPEGSLLPSPPPSQEREHPSSSMPFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPGdiAAAFPAERDSST- 162
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA--PEALAAARQASAr 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 163 -------PYQEIAAVPSAGRERQPKEEGQKSsfsfssgidqSPGMSPVPLREPMKAPLCGEGDQPGGFESQEKEAAGGFP 235
Cdd:PRK12323 443 gpggapaPAPAPAAAPAAAARPAAAGPRPVA----------AAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPA 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 236 PAESRQGVASVQVTPEaPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEA 295
Cdd:PRK12323 513 QPDAAPAGWVAESIPD-PATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASAS 571
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2633-2770 |
9.74e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318895 2633 RAEIITKER-EVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLA 2711
Cdd:PRK01156 347 RYDDLNNQIlELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1676318895 2712 DLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEI 2770
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKI 485
|
|
| |
