|
Name |
Accession |
Description |
Interval |
E-value |
| SCAPER_N |
pfam16501 |
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly ... |
73-170 |
3.18e-56 |
|
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly conserved region close to the N-terminus. SCAPER is localized to the endoplasmic reticulum and is a substrate for cyclin A/Cdk2. It associates with cyclin A and localizes to the ER. One theory suggests that SCAPER functions to create a local high concentration of cyclin A2 in the cytoplasm. Alternatively, SCAPER might be acting to sequester a portion of cellular cyclin A2 that could then be readily available for nuclear translocation, which may be needed for exit from G0 phase.
Pssm-ID: 406813 Cd Length: 98 Bit Score: 189.54 E-value: 3.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 73 KTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTS 152
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 2462544429 153 LAWEVKKMSPGRHVIPSP 170
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
527-761 |
2.60e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQLREKLREEkTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 606
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 607 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLMKR 685
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544429 686 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAEL 761
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
379-760 |
1.22e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 379 EEKFPAEKARIE-NEMDPSDISNVSAANLSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTRE--IEAEENNDINIE 455
Cdd:PTZ00121 1415 AAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEE 1494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 456 TDNDSDfsasmgsgsvsfcgmsmdwndvladyEARESWRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRtiAESKK 535
Cdd:PTZ00121 1495 AKKKAD--------------------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 536 KHEEKQmKAQQLReKLREEKTLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKV 613
Cdd:PTZ00121 1547 KADELK-KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKA 1622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 614 NEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLMKRKEQ 688
Cdd:PTZ00121 1623 EEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAE 1699
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544429 689 EARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 760
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-760 |
2.46e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 539 EKQMKAQQLREKLRE-EKTLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEia 617
Cdd:COG1196 210 EKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 618 fintleAQNKRHDVLSKLKEYEQRLNELQeerQRRQEEKQARDEAVQERKRALE--AERQARVEELLMKRKEQEARIEQQ 695
Cdd:COG1196 286 ------AQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462544429 696 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 760
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-701 |
6.48e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 329 QFTVSTLDD--VKNSGSIRDNYVRTSEISAVHIDTECVSVMLQAGTPPLQVNEEKFPAEKARIENEMDPSDISnVSAANL 406
Cdd:TIGR02169 638 KYRMVTLEGelFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE-LSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 407 SMAEVLAKKEELADRLEKANEEaiasaIAEEEQLTREIEAEENNDINIETDNDSDFSAsmgsgsvsfcgMSMDWNDV--- 483
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARIEE-----------LEEDLHKLeea 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 484 LADYEARES---WRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEK----T 556
Cdd:TIGR02169 781 LNDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlN 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 557 LKLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKRHDVLSKLK 636
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELS 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 637 EYEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLMK-------RKEQEARIEQQRQ 697
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAILERIEEYEK 1014
|
....
gi 2462544429 698 EKEK 701
Cdd:TIGR02169 1015 KKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-757 |
9.54e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 385 EKARIENEMDPSDISNVSAANLSMAEVLAKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDND 459
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 460 SDFSASMGSgsvsfcgmsmDWNDVLADYEARESWRQNTSwGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEE 539
Cdd:PRK02224 411 EDFLEELRE----------ERDELREREAELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 540 KQMKAQQLREKL--------REEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQA 601
Cdd:PRK02224 480 LEAELEDLEEEVeeveerleRAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREA 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 602 IVKKAQEEEAKVNEIAFIN--------TLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRAL 670
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNsklaelkeRIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKREL 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 671 EAERQ-ARVEELLMKRKEQEARIEQQRQEkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESI 744
Cdd:PRK02224 640 EAEFDeARIEEAREDKERAEEYLEQVEEK-------------------LDELR----EERDDLQAEIgavenELEELEEL 696
|
410
....*....|...
gi 2462544429 745 RRHMEQIEQRKEK 757
Cdd:PRK02224 697 RERREALENRVEA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
527-919 |
1.49e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEEL---------LDQRRRMMEEKLLHAEFKREV 597
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAK-KADEAKKKAEEAK--KADEAKKKAEEAKKKADEAkkaaeakkkADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 598 QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQAR 677
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 678 VEELlmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEK 757
Cdd:PTZ00121 1609 AEEA---KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKK 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 758 AAELSSGRHANTDYAPKLTPYERKKQcslcnvlISSEVYLFSHVKGRKHQQAVR--ENTSIQGRELSDEEVEhlslkkyi 835
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------- 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 836 idivvESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSGSWA 915
Cdd:PTZ00121 1742 -----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
....
gi 2462544429 916 NNKV 919
Cdd:PTZ00121 1817 GNLV 1820
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
526-760 |
2.14e-10 |
|
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: 63.78 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 526 RKRTIAESKKKHEEKQMKAQQLREKLREEKtLKLQKLLEREKDvrkwkEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 605
Cdd:pfam13868 71 RKRYRQELEEQIEEREQKRQEEYEEKLQER-EQMDEIVERIQE-----EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 606 AQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-KRALEAERQARVE 679
Cdd:pfam13868 145 LEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQEEQERKERQKER 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 680 ELLMKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHDESIRRHMEQIEQ 753
Cdd:pfam13868 225 EEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHRRELEKQIEEREE 304
|
....*..
gi 2462544429 754 RKEKAAE 760
Cdd:pfam13868 305 QRAAERE 311
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
520-700 |
5.89e-10 |
|
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: 63.99 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 520 KLSSPSRKRTIAESKKKHEEKQMKAQQLRE----KLREEKTLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 591
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 592 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 671
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 2462544429 672 AERQARVEELLMKRKEQEARIEQQRQEKE 700
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
379-854 |
1.04e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 379 EEKFPAEKARIENEMDPSDISNVSAANLSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDN 458
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 459 dsdfsasmgsgsvsfcgmsmdwndvlADYEARESWRQNTSWGDIVEE--EPARPPGHGIHMHEKLSSPSRKRTIAESKKK 536
Cdd:PTZ00121 1320 --------------------------AKKKAEEAKKKADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 537 HEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEELldqrRRMMEEKLLHAEFKR---EVQLQAIVKKAQEEEAKV 613
Cdd:PTZ00121 1374 EEAKK-KADAAKKKAEEKK--KADEAKKKAEEDKKKADEL----KKAAAAKKKADEAKKkaeEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 614 NEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEEllmKRKEQEARIE 693
Cdd:PTZ00121 1447 DEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA--EA---KKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 694 QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAP 773
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 774 KLTPYERKKQCSlcnvlissevylfshvKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKyiidivVESTAPAEALKDGE 853
Cdd:PTZ00121 1599 KLYEEEKKMKAE----------------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE------AEEKKKAEELKKAE 1656
|
.
gi 2462544429 854 E 854
Cdd:PTZ00121 1657 E 1657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
530-762 |
2.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 530 IAESKKKHEEKQMKAQQLREKLRE------EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIV 603
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 604 KKAQEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARvEELL 682
Cdd:COG1196 349 AEEELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 683 MKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELS 762
Cdd:COG1196 428 EALAELEEEEEEEEEALEE---------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
525-754 |
2.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 602
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 603 VKKAQEEEAKVNEIAfiNTLEAQNKRHDVLSKLKEYEQRLNELqeeRQRRQEEKQARDEAVQERKRALEAERQARVEELL 682
Cdd:COG1196 375 AEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544429 683 MKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 754
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
526-760 |
1.10e-08 |
|
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: 58.78 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 526 RKRTIAESKK----KHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQL 599
Cdd:pfam13868 24 RDAQIAEKKRikaeEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 600 QAIVKKAQEEEAKVNEIAFI---NTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 675
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 676 ARVEELLmkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRH 747
Cdd:pfam13868 184 REIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQ 244
|
250
....*....|...
gi 2462544429 748 MEQIEQRKEKAAE 760
Cdd:pfam13868 245 IELKERRLAEEAE 257
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
519-761 |
1.32e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.11 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 519 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLqkllEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 598
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 599 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 676
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 677 RVEELLMKRKEQEAR-IEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKkiQLKHDESIRRHMEQIEQRK 755
Cdd:pfam02029 249 KLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAER--KLREEEEKRRMKEEIERRR 326
|
....*.
gi 2462544429 756 EKAAEL 761
Cdd:pfam02029 327 AEAAEK 332
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
527-760 |
1.54e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQLREKLRE---EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 602
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkekELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 603 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 675
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 676 ArVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 755
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 2462544429 756 EKAAE 760
Cdd:PRK03918 401 EEIEE 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
532-760 |
3.10e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 532 ESKKKHEEKQM-KAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQE 608
Cdd:TIGR02168 199 ERQLKSLERQAeKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 609 EEAKVNEI--------AFINTLEAQ-----NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERq 675
Cdd:TIGR02168 279 LEEEIEELqkelyalaNEISRLEQQkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 676 ARVEELLMKRKEQEARIEQQRQEKEKaredaarerardreerLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRK 755
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET----------------LRSKVAQLELQIASLNNEIE-----RLEARLERLEDRR 416
|
....*
gi 2462544429 756 EKAAE 760
Cdd:TIGR02168 417 ERLQQ 421
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
532-760 |
3.80e-08 |
|
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: 58.06 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 532 ESKKKHEEKQMKAQQLREKLREEKTLKlqKLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ-------- 598
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQEL--KLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQellrdeqe 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 599 ----LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 672
Cdd:pfam02463 252 eiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 673 ERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-DESIRRHME 749
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeEEKEAQLLL 411
|
250
....*....|.
gi 2462544429 750 QIEQRKEKAAE 760
Cdd:pfam02463 412 ELARQLEDLLK 422
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
532-760 |
8.16e-08 |
|
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: 57.06 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 532 ESKKKHEEKQMKAQQL--REKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEeKLLHAEFKREVQlqaivKKAQEE 609
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKAR-QAEMDRQAAIYAEQERMAMERERELE-RIRQEERKRELE-----RIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 610 EA----KVNEIAFINtLEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ--- 675
Cdd:pfam17380 370 IAmeisRMRELERLQ-MERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERArem 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 676 ARVEELLMKRKEQEARIEQQRQE-------KEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 748
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEErkrkkleLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250
....*....|..
gi 2462544429 749 EQIEQRKEKAAE 760
Cdd:pfam17380 529 IYEEERRREAEE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-760 |
1.12e-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: 56.60 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLREektlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 598
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 599 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 676
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 677 RVEELLMKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 754
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 2462544429 755 KEKAAE 760
Cdd:TIGR02168 896 LEELSE 901
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
527-770 |
2.39e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREK-DVRKWKEELLDQRRRMMEekllhaefkrevqlqaI 602
Cdd:TIGR02169 307 ERSIAEKErelEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERkRRDKLTEEYAELKEELED----------------L 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 603 VKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeqRLNELQEERQRRQEEKQARDEAVQERKRALE------AERQA 676
Cdd:TIGR02169 370 RAELEEVDKEFAE-----TRDELKDYREKLEKLKR---EINELKRELDRLQEELQRLSEELADLNAAIAgieakiNELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 677 RVEELLMKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKiqlkhdesiRRHMEQIEQRKE 756
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSK------------YEQELYDLKEEYDRVEKELSKL---------QRELAEAEAQAR 500
|
250
....*....|....
gi 2462544429 757 KAAELSSGRHANTD 770
Cdd:TIGR02169 501 ASEERVRGGRAVEE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
529-907 |
2.77e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 529 TIAESKKKHEEKQMKaqqlrEKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKREVQLQAIVKKAqe 608
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKT-----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAEDAKRVEIARKA-- 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 609 EEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL----MK 684
Cdd:PTZ00121 1161 EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKkaeeAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 685 RKEQEA-RIEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME--QIEQRKEKAAEL 761
Cdd:PTZ00121 1237 KDAEEAkKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 762 SSGRHA--NTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKGRKHQQAVREntsiqgRELSDEEVEHLSLKKYiidiv 839
Cdd:PTZ00121 1315 KKADEAkkKAEEAKKKADAAKKK---------AEEAKKAAEAAKAEAEAAADE------AEAAEEKAEAAEKKKE----- 1374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544429 840 vESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQ 907
Cdd:PTZ00121 1375 -EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
499-754 |
3.76e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 499 WGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREK--LREEKTLKLQKLLErEKDVRKWKEEL 576
Cdd:TIGR02794 20 LGSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKklEQQAEEAEKQRAAE-QARQKELEQRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 577 LDQRRRMMEEKllHAEFKREVQLQAIVKKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEE 655
Cdd:TIGR02794 99 AAEKAAKQAEQ--AAKQAEEKQKQAEEAKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 656 KQARDEAV----QERKRALEAERQARVEELLMKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEA 728
Cdd:TIGR02794 165 KKKAEEAKkkaeAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGS 244
|
250 260
....*....|....*....|....*..
gi 2462544429 729 MEELQKKIQLKHDES-IRRHMEQIEQR 754
Cdd:TIGR02794 245 NAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
528-760 |
4.62e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 528 RTIAESKKKHEEKQMKaQQLREKLREEKTLKLQKLLErekdvrkWKEELLDQRRrmmeekllhaEFKREVqlqaivkKAQ 607
Cdd:PRK12704 26 KKIAEAKIKEAEEEAK-RILEEAKKEAEAIKKEALLE-------AKEEIHKLRN----------EFEKEL-------RER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 608 EEEakvneiafintLEAQNKRhdvlskLKEYEQRLNElqeerqrrqeekqaRDEAVQERKRALEAERQ---ARVEELLMK 684
Cdd:PRK12704 81 RNE-----------LQKLEKR------LLQKEENLDR--------------KLELLEKREEELEKKEKeleQKQQELEKK 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544429 685 RKEQEARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 760
Cdd:PRK12704 130 EEELEELIEEQLQELER----------------ISGLTAeeAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
518-779 |
4.75e-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: 54.36 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 518 HEKLSSpSRKRT---IAESKKKHEEKQMKAQQLR---EKLREEKTLKLqkllEREKDVRKWKEELLDQRRrmmeEKLLHA 591
Cdd:pfam17380 339 QERMAM-ERERElerIRQEERKRELERIRQEEIAmeiSRMRELERLQM----ERQQKNERVRQELEAARK----VKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 592 EFKREVQLQAIVK---KAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYE--QRLNELQEERQRRQEEKQARDEavQER 666
Cdd:pfam17380 410 ERQRKIQQQKVEMeqiRAEQEEARQREV---RRLEEERAREMERVRLEEQErqQQVERLRQQEEERKRKKLELEK--EKR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 667 KRALEAERQARVEELLMKRKEQeARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQEAMEElQKKIQ------- 737
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ-AMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQeqmrkat 562
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462544429 738 -----LKHDESIRRHMEQIEQRKEKAAELSSGRHANT---DYAPKLTPYE 779
Cdd:pfam17380 563 eersrLEAMEREREMMRQIVESEKARAEYEATTPITTikpIYRPRISEYQ 612
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
531-702 |
6.92e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 531 AESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 610
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 611 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEA 690
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 2462544429 691 RIEQQRQEKEKA 702
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
541-767 |
9.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 541 QMKAQQLRE-----------KLREEKTLKlqKL------LEREKDVRkwkEELLDQRRR--------------MMEEKLL 589
Cdd:COG1196 151 EAKPEERRAiieeaagiskyKERKEEAER--KLeateenLERLEDIL---GELERQLEPlerqaekaeryrelKEELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 590 HAEFK----REVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekQARDEAVQ 664
Cdd:COG1196 226 EAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEA-----------QAEEYELL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 665 ERKRALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREDAarerardrEERLAALTAAQQEAMEELQKKiQLKHDESI 744
Cdd:COG1196 295 AELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEEL--------EEELEELEEELEEAEEELEEA-EAELAEAE 364
|
250 260
....*....|....*....|...
gi 2462544429 745 RRHMEQIEQRKEKAAELSSGRHA 767
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEE 387
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
527-699 |
1.04e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.03 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQlrEKLREEKtlKLQKLLEREKdvRKWKEELLDQRRRMMEEKLLHAEFKREVQLQaivKKA 606
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQ--EQLERAE--KMREELELEQ--QRRFEEIRLRKQRLEEERQRQEEEERKQRLQ---LQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 607 QEEEAKVNEIAFINTLE--AQNKRHDVLSKLKEYEQRLNELQEERQRRQEE--KQARDEAVQERKRALEAERQARVEELL 682
Cdd:pfam15709 417 AQERARQQQEEFRRKLQelQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQEAEEKARLEAEE 496
|
170 180
....*....|....*....|...
gi 2462544429 683 MKRKEQEA------RIEQQRQEK 699
Cdd:pfam15709 497 RRQKEEEAarlaleEAMKQAQEQ 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-760 |
1.55e-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: 53.14 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 516 HMHEKLSSPSRKRT--IAESKKKHEEKQMKAQQLREKLREekTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF 593
Cdd:TIGR02168 253 EELEELTAELQELEekLEELRLEVSELEEEIEELQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 594 KREvQLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALEA 672
Cdd:TIGR02168 331 KLD-ELAEELAELEEKLEELKEE-----LESLEAELEELeAELEELESRLEEL-------------EEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 673 ERQarvEELLMKR-KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQI 751
Cdd:TIGR02168 392 ELQ---IASLNNEiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEEL 466
|
....*....
gi 2462544429 752 EQRKEKAAE 760
Cdd:TIGR02168 467 REELEEAEQ 475
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
527-755 |
1.61e-06 |
|
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: 51.84 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQLREKLREEKTLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 596
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 597 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 675
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 676 -ARVEELLMKRKEQEA-RIEQQRQEKEKAREDAARERARDREERLAAL-TAAQQEAMEELQKKIQLkhDESIRRHMEQIE 752
Cdd:pfam13868 258 rEEEEFERMLRKQAEDeEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 2462544429 753 QRK 755
Cdd:pfam13868 336 QKK 338
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
525-735 |
1.84e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.26 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAEskkKHEEKQMKAQQLREKLREEKTLKlQKLLEREKdvrKWKEEL-LDQRRRMMEEKLlhaefkREVQLQAIV 603
Cdd:pfam15709 334 SRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRRFEEIRL------RKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 604 KKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEAVQERKRALEaERQARVEELLM 683
Cdd:pfam15709 401 QRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEAEKQRQKELE-MQLAEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462544429 684 KRKEQEaRIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 735
Cdd:pfam15709 470 EMAEEE-RLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
379-700 |
1.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 379 EEKFPAEKARIENEMDPSDISNVSAANLSMAEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIET 456
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 457 DNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNtswgDIVEEEPARPPGHGIHMHEKLsspsrKRTIAESKKK 536
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEE-----KKKVEQLKKK 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 537 HEEKQMKAQQLReKLREEKTLKLQKLLEREKDVRKWKEELL---DQRRRMMEEKLLHAEFKREVQlQAIVKKAQE----E 609
Cdd:PTZ00121 1642 EAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEkkkaE 1719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 610 EAKVNEiafintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQE 689
Cdd:PTZ00121 1720 ELKKAE-------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL-DEEDEK 1791
|
330
....*....|.
gi 2462544429 690 ARIEQQRQEKE 700
Cdd:PTZ00121 1792 RRMEVDKKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-761 |
2.20e-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: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 603
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 604 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 682
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462544429 683 MKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 761
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-775 |
2.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 563 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 633
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 634 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEEL--LMKRKEQE-ARIEQQRQEKEKAREDA 706
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLerEIERLERElEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462544429 707 ARERARDREERLAALTAAQQ--EAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 775
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
527-764 |
2.99e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRM----MEEKLLHAEFKREVQLQAI 602
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELaeleKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 603 VKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELL 682
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAERA-ELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 683 MKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRKEKAAELS 762
Cdd:COG4942 181 AELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERT 243
|
..
gi 2462544429 763 SG 764
Cdd:COG4942 244 PA 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-942 |
3.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 427 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNTSWGdivEEE 506
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 507 PARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQmKAQQLR--EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMM 584
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 585 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 656
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 657 QARDEAVQERKRALEAERQARVEELLM---KRKEQEARieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQ 733
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 734 KKIQ--LKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKgRKHQQAVR 811
Cdd:PTZ00121 1336 KKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 812 ENTSIQGRELSDEEVEHLSLKkyiidiVVESTAPAEALKDGEERQknkkkakkikarmnfRAKEYESLMETKNSGSDSPY 891
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK------AEEKKKADEAKKKAEEAK---------------KADEAKKKAEEAKKAEEAKK 1464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2462544429 892 KAKLQRLAKDLLKQVQVQDSGSWANNKVSALDRTLGEITRILEKENVADQI 942
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
512-761 |
4.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 512 GHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEeLLDQRRRMMEEKLLHA 591
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE-LLREAEELEEELQLEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 592 EFKREVQLQAIVKKAQEEEakvneiaFINTLEAQNKRHDVLSKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALE 671
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEE-------LRAALEQAEEYQELKEELEELEEQLEEL-------------LGELEELLEALDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 672 AERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKH--DESIRRHME 749
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKlaLELLEEARE 507
|
250
....*....|....*..
gi 2462544429 750 QIEQRK-----EKAAEL 761
Cdd:COG4717 508 EYREERlppvlERASEY 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
534-737 |
7.31e-06 |
|
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: 49.92 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 534 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDqrRRMMEEkllHAEFKREVQLQAIVKKAQEEEakv 613
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA--KLYQEE---QERKERQKEREEAEKKARQRQ--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 614 nEIAFINTLEAQNKRHdVLSKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQArveellMKRKEQEARIE 693
Cdd:pfam13868 236 -ELQQAREEQIELKER-RLAEEAEREEEEFE-----------RMLRKQAEDEEIEQEEAEKRR------MKRLEHRRELE 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462544429 694 QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ 737
Cdd:pfam13868 297 KQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
527-701 |
7.80e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQLREKLrEEKTLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 604
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 605 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKR-------------ALE 671
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkylslgqkgevlSIP 658
|
170 180 190
....*....|....*....|....*....|
gi 2462544429 672 AERQARVEELLMKRKEQEARIEQQRQEKEK 701
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSDLEKIQKPKKK 688
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
525-701 |
1.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 585
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 586 EKLLHaefKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvLSKLKEYEQRLNELQEERQRRQEEKQAR-DEAVQ 664
Cdd:PRK03918 313 EKRLS---RLEEEINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKKRLtGLTPE 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462544429 665 ERKRALEAERQAR--VEELLMKRKEQEARIEQQRQEKEK 701
Cdd:PRK03918 388 KLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKK 426
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
484-775 |
1.92e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.49 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 484 LADYEARESWRQNTSWGDIVEEEPARPpghgihmHEKLSspsRKRTIAESKKKHEEKQMKAQQ-LREKLREEKTLKLQKL 562
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 563 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 635
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 636 keyEQRLNELQEerqrrqeekQARDEAVQERK---RALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREdaarerar 712
Cdd:pfam15558 218 ---EERHRELRE---------KAQKEEEQFQRakwRAEEKEEE-RQEHKEALAELADRKIQQARQVAHKTVQ-------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544429 713 DREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 775
Cdd:pfam15558 277 DKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKT 339
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
550-939 |
2.45e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 550 KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKllhAEFKREVQLQAIVKKAQEEEAKVNEIAF--------INT 621
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLneeridllQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 622 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-----RQARVEELLMKRKEQEARIEQQR 696
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElkselLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 697 QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhdESIRRHMEQIEQRKEKAAELSSGRhantDYAPKLT 776
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAK----LKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 777 PYERKKQCSLCNVLISSEvyLFSHVKGRKHQQAV------RENTSIQGRELSDEEVEHLSLKKYIIDIVVESTAPAEALK 850
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQ--LEDLLKEEKKEELEileeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 851 D---GEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSGSWANNKVSALDRTLG 927
Cdd:pfam02463 477 TqlvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
410
....*....|..
gi 2462544429 928 EITRILEKENVA 939
Cdd:pfam02463 557 ADEVEERQKLVR 568
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
524-760 |
2.67e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.11 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 524 PSRKRTIAE---SKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 600
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 601 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 680
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 681 LLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 754
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 2462544429 755 KEKAAE 760
Cdd:pfam15558 225 REKAQK 230
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
582-760 |
3.87e-05 |
|
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: 47.61 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 582 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 661
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 662 AVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 740
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 2462544429 741 DESIRRHMEQIEQRKEKAAE 760
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
510-616 |
4.16e-05 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 44.65 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 510 PPGHGIHMHEKLSSPSRKRTIAESKkkheEKQMKAQQLREKLREEKTLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKL 588
Cdd:pfam00836 23 PPSVNAAPPKLSLSPKKKDSSLEEI----QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKL 98
|
90 100 110
....*....|....*....|....*....|..
gi 2462544429 589 LHA----EFKREVQLQAIVKKAQEEEAKVNEI 616
Cdd:pfam00836 99 KQKmeayKENREAQIAALKEKLKEKEKHVEEV 130
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
519-760 |
4.50e-05 |
|
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: 48.04 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 519 EKLSSPSRKRTIAESKKKHEEKQMKAQQlREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ 598
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEK-ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 599 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARV 678
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 679 EELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIrrhmeQIEQRKEKA 758
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII-----SAHGRLGDL 534
|
..
gi 2462544429 759 AE 760
Cdd:pfam02463 535 GV 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
519-701 |
4.76e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 519 EKLSSPS-RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMmeekllhaefKREV 597
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 598 QLQAIVKKAQEEEAKVNEIAfintleaqnkrhDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 677
Cdd:COG4717 126 QLLPLYQELEALEAELAELP------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180
....*....|....*....|....
gi 2462544429 678 VEELLMKRKEQEARIEQQRQEKEK 701
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEE 217
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
780-812 |
6.43e-05 |
|
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.
Pssm-ID: 197732 [Multi-domain] Cd Length: 35 Bit Score: 41.47 E-value: 6.43e-05
10 20 30
....*....|....*....|....*....|...
gi 2462544429 780 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 812
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
479-703 |
1.00e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 479 DWNDVLADYEARESWRQNTSW--GDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKT 556
Cdd:pfam02029 95 DEKESVAERKENNEEEENSSWekEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 557 LKLQKLLEREKDVRKWKEE---LLDQRRRMMEEKLLHAEF---------KREVQLQAIVKKAQEEEAKVNEIAfiNTLEA 624
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEevtklkvttKRRQGGLSQSQEREEEAEVFLEAE--QKLEE 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462544429 625 QNKRHDVLSKlKEYEQRLNELQEERQRRQEEKQARdeavQERKRALEAERQARVEEllmkRKEQEARIEQqrqEKEKAR 703
Cdd:pfam02029 253 LRRRRQEKES-EEFEKLRQKQQEAELELEELKKKR----EERRKLLEEEEQRRKQE----EAERKLREEE---EKRRMK 319
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
534-762 |
1.17e-04 |
|
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: 46.89 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 534 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 613
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 614 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNElqeerqrRQEEKQARDEAVQERKRALEAERQARvEELLMKRKEQEARI 692
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544429 693 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 762
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
546-761 |
2.19e-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: 45.29 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 546 QLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRR--RMMEEKLLHAEFKREvqlqaivkkaQEEEAKVNE-IAFINTL 622
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIK-AEEKEEERRldEMMEEERERALEEEE----------EKEEERKEErKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 623 EAQNKRHDVLsKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKa 702
Cdd:pfam13868 79 EEQIEEREQK-RQEEYEEKLQE-----------REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544429 703 redaarerardreerlaaltaaQQEAMEELQKKIQ----LKHDESIRRHMEQIEQRKEKAAEL 761
Cdd:pfam13868 146 ----------------------EKEEEREEDERILeylkEKAEREEEREAEREEIEEEKEREI 186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
526-782 |
2.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 526 RKRTIAESKKKHEEKQMKAQQLRE---------KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRM-----MEEKL--- 588
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeleeKEERLeel 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 589 --LHAEFKREV-QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE 665
Cdd:PRK03918 344 kkKLKELEKRLeELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 666 RKRALEAERQAR-------------------------VEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAa 720
Cdd:PRK03918 424 LKKAIEELKKAKgkcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA- 502
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544429 721 ltaaqqEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKK 782
Cdd:PRK03918 503 ------EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
544-770 |
2.26e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 544 AQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 623
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 624 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQRQEKEKAR 703
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK-RKAEEEAKRKAEEERKAAEA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462544429 704 EDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTD 770
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
543-763 |
2.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 543 KAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 617
Cdd:PRK02224 409 NAEDFLEELREER----DELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 618 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLM 683
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 684 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 762
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 2462544429 763 S 763
Cdd:PRK02224 641 A 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
521-754 |
2.40e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 521 LSSPSRKRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEeLLDQRRRMmEEKLlhaefkREV 597
Cdd:PRK03918 445 LTEEHRKELLEEYTaelKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKE-LAEQLKEL-EEKL------KKY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 598 QLQAIVKKAQEEEaKVNEIAfiNTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA----- 672
Cdd:PRK03918 516 NLEELEKKAEEYE-KLKEKL--IKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfes 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 673 --ERQARVEEL--------LMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTaaqqEAMEELQKKIQLKHDE 742
Cdd:PRK03918 587 veELEERLKELepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR----KELEELEKKYSEEEYE 662
|
250
....*....|..
gi 2462544429 743 SIRRHMEQIEQR 754
Cdd:PRK03918 663 ELREEYLELSRE 674
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
488-761 |
2.53e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 488 EARESWRQntswgdivEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLReKLREEKTLKLQKLLEREK 567
Cdd:pfam02029 17 EERRRQKE--------EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 568 D----VRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaivkkAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLN 643
Cdd:pfam02029 88 EfdptIADEKESVAERKENNEEEENSSWEKEEKRD-------SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 644 ELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA 723
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462544429 724 AQQEAMEELQKKIQLKHDESIRRHMEQIEQRK-EKAAEL 761
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQqEAELEL 279
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
522-761 |
3.23e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 522 SSPSRKRTIAESKKKHEEKQmkaqqlreklREEKTLKLQKLLEREKDVR-KWKEELLDQRRRMMEEKLLHAEFKREVQlq 600
Cdd:pfam15709 297 SSPTQTFVVTGNMESEEERS----------EEDPSKALLEKREQEKASRdRLRAERAEMRRLEVERKRREQEEQRRLQ-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 601 aivKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeQRLNElqeerqrrQEEKQARDEAVQERKRALEAERqARVEE 680
Cdd:pfam15709 365 ---QEQLERAEKMRE-----ELELEQQRRFEEIRLRK--QRLEE--------ERQRQEEEERKQRLQLQAAQER-ARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 681 LLMKRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRK 755
Cdd:pfam15709 426 EEFRRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKE 501
|
....*.
gi 2462544429 756 EKAAEL 761
Cdd:pfam15709 502 EEAARL 507
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
519-976 |
3.24e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 519 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREK----LREEKTLKLQKLLEREKDVRKWKEElLDQRRRMMEEKLLHAEFK 594
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKakeeAEEERLAELEAKRQAEEEAREAKAE-AEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 595 REVQLQAIVKKAQEEEAKVNEiafintlEAQnkrhdvlsklkeyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 674
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAK-------EAE-------------AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 675 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 754
Cdd:COG3064 142 KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 755 KEKAAELSSGRHANTDYAPKLTPYERKKQcslcnvliSSEVYLFSHVKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKY 834
Cdd:COG3064 222 AARAAAASREAALAAVEATEEAALGGAEE--------AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 835 IIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSG 912
Cdd:COG3064 294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAasLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544429 913 SWANNKVSALDRTLGEITRILEKENVADQIAFQAAGGLTALEHILQAVVPATNVNTVLRIPPKS 976
Cdd:COG3064 374 ALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALL 437
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
530-758 |
3.48e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 530 IAESKKKHEEKQMKAQQLREK-----LREEKTLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 604
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 605 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMK 684
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544429 685 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 758
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
656-783 |
3.58e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 656 KQARDEAVQERKRALEAE-RQARVEEllmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 734
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462544429 735 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 783
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
530-728 |
4.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 530 IAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 603
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 604 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 674
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462544429 675 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 728
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
656-739 |
4.90e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 44.10 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 656 KQARDEAVQERKRALEAERQarvEELLMKRKEQEarieqqRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 735
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAK------KKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 2462544429 736 IQLK 739
Cdd:pfam07946 319 KEQR 322
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
525-699 |
4.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMME------EKLLHAEFKRE-- 596
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEyl 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 597 VQLQAIVKKAQEEEAKVNEI-AFINTLEAQNKRHDVLSK-LKEYEQRLNELQEERQRRQEEKQARDEAVQERKR--ALEA 672
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIeERIKELEEKEERLEELKKkLKELEKRLEELEERHELYEEAKAKKEELERLKKRltGLTP 386
|
170 180
....*....|....*....|....*...
gi 2462544429 673 ERQARVEELLMKRKEQ-EARIEQQRQEK 699
Cdd:PRK03918 387 EKLEKELEELEKAKEEiEEEISKITARI 414
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
784-806 |
5.05e-04 |
|
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.
Pssm-ID: 463736 [Multi-domain] Cd Length: 25 Bit Score: 38.63 E-value: 5.05e-04
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
528-935 |
5.58e-04 |
|
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: 44.57 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 528 RTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQ 607
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 608 EEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEE 680
Cdd:TIGR00618 542 TSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 681 LLMKRKEQEARIE----QQRQEKEkaredaarerardreerlaaLTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKE 756
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALK--------------------LTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 757 KAAELSSGRHANTDYAPKLTPYERKKQCSLCNVLISS----EVYLFSHVKGRK-HQQAVRENTSIQG-RELSDEEVEHLS 830
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefnEIENASSSLGSDlAAREDALNQSLKElMHQARTVLKART 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 831 LkkyiIDIVVESTAPAEALKDGEERQKNKKKAkkikarmNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQD 910
Cdd:TIGR00618 761 E----AHFNNNEEVTAALQTGAELSHLAAEIQ-------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
410 420
....*....|....*....|....*
gi 2462544429 911 SGSwANNKVSALDRTLGEITRILEK 935
Cdd:TIGR00618 830 EEQ-FLSRLEEKSATLGEITHQLLK 853
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
539-767 |
5.63e-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: 43.75 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 539 EKQMKAQQLREKLREEKTLKLQKLLEREkDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIvKKAQEEEAKVNEIAF 618
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEEQIEEREQ-KRQEEYEEKLQEREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 619 INTLEAQNKRHDvlskLKEYEQRLNElqeerqrrQEE-KQARDEAVQERKRALEAERQA------RVEELLMKRKEQEAR 691
Cdd:pfam13868 103 MDEIVERIQEED----QAEAEEKLEK--------QRQlREEIDEFNEEQAEWKELEKEEereedeRILEYLKEKAEREEE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544429 692 IEQQRQEKEKaredaARERARDREERLAALTAAQQEAMEEL-QKKIQLKHDESIR-RHMEQIEQRKEKAAELSSGRHA 767
Cdd:pfam13868 171 REAEREEIEE-----EKEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKERqKEREEAEKKARQRQELQQAREE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
526-645 |
7.36e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 526 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 604
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462544429 605 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNEL 645
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
537-701 |
7.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 537 HEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKwKEELLDQRRRMMEEKLLHAEFKREVQLQAivkkaqeeeakvnEI 616
Cdd:COG4913 283 LWFAQRRLELLEAELEELRA-ELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLER-------------EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 617 AfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqARVEELLMKRKEQEARIEQQR 696
Cdd:COG4913 348 E-----RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRREL 421
|
....*
gi 2462544429 697 QEKEK 701
Cdd:COG4913 422 RELEA 426
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
538-701 |
8.22e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 538 EEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWK-EELLDQRRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEI 616
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQ--KQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 617 AFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQR 696
Cdd:PRK09510 145 AKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
....*
gi 2462544429 697 QEKEK 701
Cdd:PRK09510 214 EAKKK 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
558-763 |
1.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 558 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 632
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 633 SKLKEYEQRLNE----------LQEERQRRQEEKQARDEAVQERKRA---LEAERQARVEELLMKRKEQEArIEQQRQEK 699
Cdd:PRK02224 241 EVLEEHEERREEletleaeiedLRETIAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEA-VEARREEL 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544429 700 EKAREDAARErardreerLAALTAAQQEAMEELQKkiqlkHDESIRRHMEQIEQRKEKAAELSS 763
Cdd:PRK02224 320 EDRDEELRDR--------LEECRVAAQAHNEEAES-----LREDADDLEERAEELREEAAELES 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
546-694 |
1.67e-03 |
|
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: 42.57 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 546 QLREKLREEKTL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 620
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462544429 621 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLMKRKEQEARIEQ 694
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
519-917 |
2.25e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 519 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 596
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 597 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 665
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 666 RKRAL----EAERQARVEELLMKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 740
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 741 DESIRRHMEQIEQRKEKAAELSSGRhANTDYAPKLTpYERKKQCSLCNVLISSEVYLFS--HVKGRKHQQAVRENTSIQG 818
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRR-ENSLLDDKQL-YQLESTENLLKTINVKDLEVTNrnLVKPANVLQFIVAQMIKLN 1126
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 819 reLSDEEVEHLSLKKYIIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDS------- 889
Cdd:COG5022 1127 --LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 2462544429 890 PYKAKLQRLAKDLLKQVQVQDSGSWANN 917
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
527-645 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 527 KRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 606
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462544429 607 QEEEAKVNEiafinTLEAQNKRHDvlSKLKEYEQRLNEL 645
Cdd:COG1579 130 EAELAELEA-----ELEEKKAELD--EELAELEAELEEL 161
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
529-701 |
3.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 529 TIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMME-EKLLHAEFKREVQLQAIVKKAQ 607
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEElNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 608 EEEAKVNEIafINTLEAQNKrhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-RQARVEELLMKRK 686
Cdd:COG4372 108 EEAEELQEE--LEELQKERQ------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQALSEA 179
|
170
....*....|....*
gi 2462544429 687 EQEARIEQQRQEKEK 701
Cdd:COG4372 180 EAEQALDELLKEANR 194
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
526-616 |
3.64e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 526 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 605
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEG 281
|
90
....*....|..
gi 2462544429 606 AQEE-EAKVNEI 616
Cdd:pfam02841 282 FKTEaESLQKEI 293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
635-761 |
3.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 635 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDR 714
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462544429 715 EERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 761
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAEL 175
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
660-764 |
4.82e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 660 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 737
Cdd:cd16269 190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247
|
90 100
....*....|....*....|....*...
gi 2462544429 738 LKHDESIRRHMEQIEQR-KEKAAELSSG 764
Cdd:cd16269 248 EERENLLKEQERALESKlKEQEALLEEG 275
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
549-761 |
5.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 549 EKLREEktlkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 628
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 629 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAA 707
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544429 708 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 761
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
574-737 |
6.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 574 EELLDQRRRMMEEKLL--HAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLnelqeerqr 651
Cdd:COG1196 624 GRTLVAARLEAALRRAvtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE--------- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 652 rqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE 731
Cdd:COG1196 695 ---LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*.
gi 2462544429 732 LQKKIQ 737
Cdd:COG1196 772 LEREIE 777
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
530-742 |
6.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 530 IAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAE----FKREVQLQAIVKK 605
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 606 AQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEA--ERQARVEEL 681
Cdd:COG1340 152 AKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQELHEEMIEL---YKEADELRKEADELHKEivEAQEKADEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462544429 682 lmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 742
Cdd:COG1340 229 ---HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEE 286
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
531-615 |
6.56e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.88 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 531 AESKKKHEEKQMKAQQLRE--------KLREEKTLKLQKLLEREKDVRKWKEEllDQRRRMMEEKLLHAEFKREVQLQAI 602
Cdd:pfam15346 43 VEEARKIMEKQVLEELEREreaeleeeRRKEEEERKKREELERILEENNRKIE--EAQRKEAEERLAMLEEQRRMKEERQ 120
|
90
....*....|...
gi 2462544429 603 VKKAQEEEAKVNE 615
Cdd:pfam15346 121 RREKEEEEREKRE 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
525-701 |
7.22e-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: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTL--KLQKLLEREKDVRKWKEEL--LDQRRRMMEE---KLLHAEfKREV 597
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIaeLEAELERLDAssdDLAALE-EQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 598 QLQAIVKKAQEEEAKVNEIAFintlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeekqARDEAVQERKRALEAERQAR 677
Cdd:COG4913 696 ELEAELEELEEELDELKGEIG----RLEKELEQAEEELDELQDRLEA-------------AEDLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....
gi 2462544429 678 VEELLMKRKEQEARIEQQRQEKEK 701
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARL 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-760 |
7.41e-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: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 565 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 638
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 639 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLMKRKEQEARIEQQRQEKEKAREDAA 707
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462544429 708 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 760
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
525-701 |
7.55e-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: 39.52 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 525 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRRRMMEekllhaefKREVQLQAiVK 604
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEARIK--------KYEEQLGN-VR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 605 KAQEEEAKVNEIafintlEAQNKRHDVLSK-LKEYEQRLNELqeerqrrqeekqardEAVQERKRALEAERQARVEELLM 683
Cdd:COG1579 87 NNKEYEALQKEI------ESLKRRISDLEDeILELMERIEEL---------------EEELAELEAELAELEAELEEKKA 145
|
170
....*....|....*...
gi 2462544429 684 KRKEQEARIEQQRQEKEK 701
Cdd:COG1579 146 ELDEELAELEAELEELEA 163
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
522-759 |
7.81e-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: 40.72 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 522 SSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLlerekdvrKWKEELLDQRRRMME---EKLLHAEFKREVQ 598
Cdd:TIGR00618 216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL--------KKQQLLKQLRARIEElraQEAVLEETQERIN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 599 LQAIVKKAQEEEAKVNEIAF----INTL--EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQ----ARDEAVQERKR 668
Cdd:TIGR00618 288 RARKAAPLAAHIKAVTQIEQqaqrIHTElqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 669 ALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 748
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250
....*....|....
gi 2462544429 749 E---QIEQRKEKAA 759
Cdd:TIGR00618 448 TctaQCEKLEKIHL 461
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
657-760 |
7.99e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 657 QARDEAVQERKRALEAERQARVEEllMKRKEQEARI--EQQRQEKEKAREDAARERARDREERLAALTAAQQeAMEELQK 734
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQ--KKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKK 169
|
90 100
....*....|....*....|....*.
gi 2462544429 735 KiqlkhdesirrhmEQIEQRKEKAAE 760
Cdd:PRK09510 170 K-------------AEAEAAKKAAAE 182
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
530-762 |
9.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 530 IAESKKKHEEKQMKAQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEE-----KLLHAEFKREVQLQAIVK 604
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKR-DELNEKVKELKEERDELNEKLNELREEldelrKELAELNKAGGSIDKLRK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 605 KAQEEEAKvneiaFIN---TLEAQNKrhdVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQarVEEL 681
Cdd:COG1340 117 EIERLEWR-----QQTevlSPEEEKE---LVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKK--IKEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544429 682 LMKRKEQEARIEQQRQEKEKAREDAARERardreerlAALTAAQQEAMEELQKKIQLKhdESIRRHMEQIEQRKEKAAEL 761
Cdd:COG1340 187 AEEAQELHEEMIELYKEADELRKEADELH--------KEIVEAQEKADELHEEIIELQ--KELRELRKELKKLRKKQRAL 256
|
.
gi 2462544429 762 S 762
Cdd:COG1340 257 K 257
|
|
| |
