|
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 |
3.56e-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: 3.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 73 KTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTS 152
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 2217301410 153 LAWEVKKMSPGRHVIPSP 170
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
521-755 |
2.52e-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: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQLREKLREEkTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 600
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 601 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLMKR 679
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301410 680 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAEL 755
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
376-754 |
3.95e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 376 QVNEEKFPAEKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREiEAEENNDinietdndsd 455
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKAD---------- 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 456 fsasmgsgsvsfcgmsmdwndvladyEARESWRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQ 535
Cdd:PTZ00121 1501 --------------------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 536 mKAQQLReKLREEKTLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEIafi 613
Cdd:PTZ00121 1553 -KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEEL--- 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 614 NTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLMKRKEQEARIEQ 688
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301410 689 QRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 754
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
533-754 |
2.42e-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: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 533 EKQMKAQQLREKLRE-EKTLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEia 611
Cdd:COG1196 210 EKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 612 fintleAQNKRHDVLSKLKEYEQRLNELQeerQRRQEEKQARDEAVQERKRALE--AERQARVEELLMKRKEQEARIEQQ 689
Cdd:COG1196 286 ------AQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217301410 690 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 754
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-695 |
5.77e-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: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 329 QFTVSTLDD--VKNSGSIRDNYVRTSEISAVHIDTECVSVMLQAGTPPLQVNEEKFPAEKARIENEMDP-----SDISNS 401
Cdd:TIGR02169 638 KYRMVTLEGelFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDElsqelSDASRK 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 402 MAEVLAKKEELADRLEKANEEaiasaIAEEEQLTREIEAEENNDINIETDNDSDFSAsmgsgsvsfcgMSMDWNDV---L 478
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARIEE-----------LEEDLHKLeeaL 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 479 ADYEARES---WRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEK----TL 551
Cdd:TIGR02169 782 NDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNG 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 552 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKRHDVLSKLKE 631
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELSE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 632 YEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLMK-------RKEQEARIEQQRQE 692
Cdd:TIGR02169 936 IEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAILERIEEYEKK 1015
|
...
gi 2217301410 693 KEK 695
Cdd:TIGR02169 1016 KRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
407-751 |
1.26e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 407 AKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDNDSDFSASMGSgsvsfcgmsmDWNDVLADY 481
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEELRE----------ERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 482 EARESWRQNTSwGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKL--------REEKTLKL 553
Cdd:PRK02224 429 AELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerleRAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 554 QKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQAIVKKAQEEEAKVNEIAFIN--------T 615
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNsklaelkeR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 616 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLMKRKEQEARIEQQRQ 691
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQVEE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217301410 692 EkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 751
Cdd:PRK02224 668 K-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-913 |
1.42e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEEL---------LDQRRRMMEEKLLHAEFKREV 591
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAK-KADEAKKKAEEAK--KADEAKKKAEEAKKKADEAkkaaeakkkADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 592 QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQAR 671
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 672 VEELlmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEK 751
Cdd:PTZ00121 1609 AEEA---KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKK 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 752 AAELSSGRHANTDYAPKLTPYERKKQcslcnvlISSEVYLFSHVKGRKHQQAVR--ENTSIQGRELSDEEVEhlslkkyi 829
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------- 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 830 idivvESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSGSWA 909
Cdd:PTZ00121 1742 -----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
....
gi 2217301410 910 NNKV 913
Cdd:PTZ00121 1817 GNLV 1820
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
520-754 |
2.42e-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: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 520 RKRTIAESKKKHEEKQMKAQQLREKLREEKtLKLQKLLEREKDvrkwkEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 599
Cdd:pfam13868 71 RKRYRQELEEQIEEREQKRQEEYEEKLQER-EQMDEIVERIQE-----EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 600 AQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-KRALEAERQARVE 673
Cdd:pfam13868 145 LEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQEEQERKERQKER 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 674 ELLMKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHDESIRRHMEQIEQ 747
Cdd:pfam13868 225 EEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHRRELEKQIEEREE 304
|
....*..
gi 2217301410 748 RKEKAAE 754
Cdd:pfam13868 305 QRAAERE 311
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
514-694 |
5.90e-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: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 514 KLSSPSRKRTIAESKKKHEEKQMKAQQLRE----KLREEKTLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 585
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 586 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 665
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 2217301410 666 AERQARVEELLMKRKEQEARIEQQRQEKE 694
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
519-848 |
1.02e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEELldqrRRMMEEKLLHAEFKR---EVQLQA 595
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKK-KADAAKKKAEEKK--KADEAKKKAEEDKKKADEL----KKAAAAKKKADEAKKkaeEKKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 596 IVKKAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEEl 675
Cdd:PTZ00121 1435 EAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA--EA- 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 676 lmKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAEL 755
Cdd:PTZ00121 1509 --KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 756 SSGRHANTDYAPKLTPYERKKQCSlcnvlissevylfshvKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKyiidivVE 835
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAE----------------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE------AE 1644
|
330
....*....|...
gi 2217301410 836 STAPAEALKDGEE 848
Cdd:PTZ00121 1645 EKKKAEELKKAEE 1657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
524-756 |
1.97e-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: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 524 IAESKKKHEEKQMKAQQLREKLRE------EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIV 597
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 598 KKAQEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARvEELL 676
Cdd:COG1196 349 AEEELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 677 MKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELS 756
Cdd:COG1196 428 EALAELEEEEEEEEEALEE---------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
519-748 |
2.28e-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: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 596
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 597 VKKAQEEEAKVNEIAfiNTLEAQNKRHDVLSKLKEYEQRLNELqeeRQRRQEEKQARDEAVQERKRALEAERQARVEELL 676
Cdd:COG1196 375 AEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217301410 677 MKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 748
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
520-754 |
1.30e-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: 58.39 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 520 RKRTIAESKK----KHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQL 593
Cdd:pfam13868 24 RDAQIAEKKRikaeEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 594 QAIVKKAQEEEAKVNEIAFI---NTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 669
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 670 ARVEELLmkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRH 741
Cdd:pfam13868 184 REIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQ 244
|
250
....*....|...
gi 2217301410 742 MEQIEQRKEKAAE 754
Cdd:pfam13868 245 IELKERRLAEEAE 257
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
513-755 |
1.46e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.11 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 513 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLqkllEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 592
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 593 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 670
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 671 RVEELLMKRKEQEAR-IEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKkiQLKHDESIRRHMEQIEQRK 749
Cdd:pfam02029 249 KLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAER--KLREEEEKRRMKEEIERRR 326
|
....*.
gi 2217301410 750 EKAAEL 755
Cdd:pfam02029 327 AEAAEK 332
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
521-754 |
1.71e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQLREKLRE---EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 596
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkekELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 597 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 669
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 670 ArVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 749
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 2217301410 750 EKAAE 754
Cdd:PRK03918 401 EEIEE 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
526-754 |
3.03e-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: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 526 ESKKKHEEKQM-KAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQE 602
Cdd:TIGR02168 199 ERQLKSLERQAeKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 603 EEAKVNEI--------AFINTLEAQ-----NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERq 669
Cdd:TIGR02168 279 LEEEIEELqkelyalaNEISRLEQQkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 670 ARVEELLMKRKEQEARIEQQRQEKEKaredaarerardreerLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRK 749
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET----------------LRSKVAQLELQIASLNNEIE-----RLEARLERLEDRR 416
|
....*
gi 2217301410 750 EKAAE 754
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 ... |
526-754 |
4.14e-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: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 526 ESKKKHEEKQMKAQQLREKLREEKTLKlqKLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ-------- 592
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQEL--KLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQellrdeqe 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 593 ----LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 666
Cdd:pfam02463 252 eiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 667 ERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-DESIRRHME 743
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeEEKEAQLLL 411
|
250
....*....|.
gi 2217301410 744 QIEQRKEKAAE 754
Cdd:pfam02463 412 ELARQLEDLLK 422
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
526-754 |
8.40e-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: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 526 ESKKKHEEKQMKAQQL--REKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEeKLLHAEFKREVQlqaivKKAQEE 603
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKAR-QAEMDRQAAIYAEQERMAMERERELE-RIRQEERKRELE-----RIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 604 EA----KVNEIAFINtLEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ--- 669
Cdd:pfam17380 370 IAmeisRMRELERLQ-MERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERArem 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 670 ARVEELLMKRKEQEARIEQQRQE-------KEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 742
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEErkrkkleLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250
....*....|..
gi 2217301410 743 EQIEQRKEKAAE 754
Cdd:pfam17380 529 IYEEERRREAEE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-754 |
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 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLREektlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 592
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 593 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 670
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 671 RVEELLMKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 748
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 2217301410 749 KEKAAE 754
Cdd:TIGR02168 896 LEELSE 901
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
521-764 |
2.44e-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: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREK-DVRKWKEELLDQRRRMMEekllhaefkrevqlqaI 596
Cdd:TIGR02169 307 ERSIAEKErelEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERkRRDKLTEEYAELKEELED----------------L 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 597 VKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeqRLNELQEERQRRQEEKQARDEAVQERKRALE------AERQA 670
Cdd:TIGR02169 370 RAELEEVDKEFAE-----TRDELKDYREKLEKLKR---EINELKRELDRLQEELQRLSEELADLNAAIAgieakiNELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 671 RVEELLMKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKiqlkhdesiRRHMEQIEQRKE 750
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSK------------YEQELYDLKEEYDRVEKELSKL---------QRELAEAEAQAR 500
|
250
....*....|....
gi 2217301410 751 KAAELSSGRHANTD 764
Cdd:TIGR02169 501 ASEERVRGGRAVEE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
523-901 |
2.64e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 523 TIAESKKKHEEKQMKaqqlrEKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKREVQLQAIVKKAqe 602
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKT-----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAEDAKRVEIARKA-- 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 603 EEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL----MK 678
Cdd:PTZ00121 1161 EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKkaeeAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 679 RKEQEA-RIEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME--QIEQRKEKAAEL 755
Cdd:PTZ00121 1237 KDAEEAkKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 756 SSGRHA--NTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKGRKHQQAVREntsiqgRELSDEEVEHLSLKKYiidiv 833
Cdd:PTZ00121 1315 KKADEAkkKAEEAKKKADAAKKK---------AEEAKKAAEAAKAEAEAAADE------AEAAEEKAEAAEKKKE----- 1374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301410 834 vESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQ 901
Cdd:PTZ00121 1375 -EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
493-748 |
3.67e-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: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 493 WGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREK--LREEKTLKLQKLLErEKDVRKWKEEL 570
Cdd:TIGR02794 20 LGSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKklEQQAEEAEKQRAAE-QARQKELEQRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 571 LDQRRRMMEEKllHAEFKREVQLQAIVKKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEE 649
Cdd:TIGR02794 99 AAEKAAKQAEQ--AAKQAEEKQKQAEEAKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 650 KQARDEAV----QERKRALEAERQARVEELLMKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEA 722
Cdd:TIGR02794 165 KKKAEEAKkkaeAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGS 244
|
250 260
....*....|....*....|....*..
gi 2217301410 723 MEELQKKIQLKHDES-IRRHMEQIEQR 748
Cdd:TIGR02794 245 NAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
522-754 |
4.64e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 522 RTIAESKKKHEEKQMKaQQLREKLREEKTLKLQKLLErekdvrkWKEELLDQRRrmmeekllhaEFKREVqlqaivkKAQ 601
Cdd:PRK12704 26 KKIAEAKIKEAEEEAK-RILEEAKKEAEAIKKEALLE-------AKEEIHKLRN----------EFEKEL-------RER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 602 EEEakvneiafintLEAQNKRhdvlskLKEYEQRLNElqeerqrrqeekqaRDEAVQERKRALEAERQ---ARVEELLMK 678
Cdd:PRK12704 81 RNE-----------LQKLEKR------LLQKEENLDR--------------KLELLEKREEELEKKEKeleQKQQELEKK 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301410 679 RKEQEARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 754
Cdd:PRK12704 130 EEELEELIEEQLQELER----------------ISGLTAeeAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
512-773 |
4.89e-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: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 512 HEKLSSpSRKRT---IAESKKKHEEKQMKAQQLR---EKLREEKTLKLqkllEREKDVRKWKEELLDQRRrmmeEKLLHA 585
Cdd:pfam17380 339 QERMAM-ERERElerIRQEERKRELERIRQEEIAmeiSRMRELERLQM----ERQQKNERVRQELEAARK----VKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 586 EFKREVQLQAIVK---KAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYE--QRLNELQEERQRRQEEKQARDEavQER 660
Cdd:pfam17380 410 ERQRKIQQQKVEMeqiRAEQEEARQREV---RRLEEERAREMERVRLEEQErqQQVERLRQQEEERKRKKLELEK--EKR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 661 KRALEAERQARVEELLMKRKEQeARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQEAMEElQKKIQ------- 731
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ-AMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQeqmrkat 562
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217301410 732 -----LKHDESIRRHMEQIEQRKEKAAELSSGRHANT---DYAPKLTPYE 773
Cdd:pfam17380 563 eersrLEAMEREREMMRQIVESEKARAEYEATTPITTikpIYRPRISEYQ 612
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
525-696 |
6.54e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 525 AESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 604
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 605 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEA 684
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 2217301410 685 RIEQQRQEKEKA 696
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
535-761 |
9.51e-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: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 535 QMKAQQLRE-----------KLREEKTLKlqKL------LEREKDVRkwkEELLDQRRR--------------MMEEKLL 583
Cdd:COG1196 151 EAKPEERRAiieeaagiskyKERKEEAER--KLeateenLERLEDIL---GELERQLEPlerqaekaeryrelKEELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 584 HAEFK----REVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekQARDEAVQ 658
Cdd:COG1196 226 EAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEA-----------QAEEYELL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 659 ERKRALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREDAarerardrEERLAALTAAQQEAMEELQKKiQLKHDESI 738
Cdd:COG1196 295 AELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEEL--------EEELEELEEELEEAEEELEEA-EAELAEAE 364
|
250 260
....*....|....*....|...
gi 2217301410 739 RRHMEQIEQRKEKAAELSSGRHA 761
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEE 387
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
521-693 |
1.11e-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: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQlrEKLREEKtlKLQKLLEREKdvRKWKEELLDQRRRMMEEKLLHAEFKREVQLQaivKKA 600
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQ--EQLERAE--KMREELELEQ--QRRFEEIRLRKQRLEEERQRQEEEERKQRLQ---LQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 601 QEEEAKVNEIAFINTLE--AQNKRHDVLSKLKEYEQRLNELQEERQRRQEE--KQARDEAVQERKRALEAERQARVEELL 676
Cdd:pfam15709 417 AQERARQQQEEFRRKLQelQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQEAEEKARLEAEE 496
|
170 180
....*....|....*....|...
gi 2217301410 677 MKRKEQEA------RIEQQRQEK 693
Cdd:pfam15709 497 RRQKEEEAarlaleEAMKQAQEQ 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
379-694 |
1.38e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 379 EEKFPAEKARIENEmdpsdisNSMAEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIETDNDSDF 456
Cdd:PTZ00121 1507 EAKKKADEAKKAEE-------AKKADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAKKAEEDK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 457 SASMGSGSVSFCGMSMDWNDVLADYEARESWRQNtswgDIVEEEPARPPGHGIHMHEKLsspsrKRTIAESKKKHEEKQM 536
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEE-----KKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 537 KAQQLReKLREEKTLKLQKLLEREKDVRKWKEELL---DQRRRMMEEKLLHAEFKREVQlQAIVKKAQE----EEAKVNE 609
Cdd:PTZ00121 1648 KAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEkkkaEELKKAE 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 610 iafintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQ 689
Cdd:PTZ00121 1726 -------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL-DEEDEKRRMEVD 1797
|
....*
gi 2217301410 690 RQEKE 694
Cdd:PTZ00121 1798 KKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
510-754 |
1.52e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 510 HMHEKLSSPSRKRT--IAESKKKHEEKQMKAQQLREKLREekTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF 587
Cdd:TIGR02168 253 EELEELTAELQELEekLEELRLEVSELEEEIEELQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 588 KREvQLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALEA 666
Cdd:TIGR02168 331 KLD-ELAEELAELEEKLEELKEE-----LESLEAELEELeAELEELESRLEEL-------------EEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 667 ERQarvEELLMKR-KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQI 745
Cdd:TIGR02168 392 ELQ---IASLNNEiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEEL 466
|
....*....
gi 2217301410 746 EQRKEKAAE 754
Cdd:TIGR02168 467 REELEEAEQ 475
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
519-729 |
1.85e-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: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAEskkKHEEKQMKAQQLREKLREEKTLKlQKLLEREKdvrKWKEEL-LDQRRRMMEEKLlhaefkREVQLQAIV 597
Cdd:pfam15709 334 SRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRRFEEIRL------RKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 598 KKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEAVQERKRALEaERQARVEELLM 677
Cdd:pfam15709 401 QRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEAEKQRQKELE-MQLAEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217301410 678 KRKEQEaRIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 729
Cdd:pfam15709 470 EMAEEE-RLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
521-749 |
1.93e-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: 51.46 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQLREKLREEKTLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 590
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 591 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 669
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 670 -ARVEELLMKRKEQEA-RIEQQRQEKEKAREDAARERARDREERLAAL-TAAQQEAMEELQKKIQLkhDESIRRHMEQIE 746
Cdd:pfam13868 258 rEEEEFERMLRKQAEDeEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 2217301410 747 QRK 749
Cdd:pfam13868 336 QKK 338
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-755 |
2.15e-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: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 597
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 598 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 676
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217301410 677 MKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 755
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
557-769 |
2.49e-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: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 557 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 627
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 628 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEEL--LMKRKEQE-ARIEQQRQEKEKAREDA 700
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLerEIERLERElEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217301410 701 ARERARDREERLAALTAAQQ--EAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 769
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
386-755 |
2.50e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 386 KARIENEMDPSDIS--NSMAEVLAKKEELADRLEKAnEEAIASAIAEEEQLTREIEAEENNDINIETDN---DSDFSASM 460
Cdd:COG4717 176 QEELEELLEQLSLAteEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAALEErlkEARLLLLI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 461 GSGSVSFCGMSMDWNDVLAdyeareswrqnTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQ 540
Cdd:COG4717 255 AAALLALLGLGGSLLSLIL-----------TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 541 LREKLREEKTLKLQKLLEREKDVRKWKEeLLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEakvneiaFINTLEAQN 620
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEEE-------LRAALEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 621 KRHDVLSKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDA 700
Cdd:COG4717 396 EYQELKEELEELEEQLEEL-------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217301410 701 ARERARDREERLAALTAAQQEAMEELQKKIQLKH--DESIRRHMEQIEQRK-----EKAAEL 755
Cdd:COG4717 463 EQLEEDGELAELLQELEELKAELRELAEEWAALKlaLELLEEAREEYREERlppvlERASEY 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
521-758 |
2.90e-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: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRM----MEEKLLHAEFKREVQLQAI 596
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELaeleKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 597 VKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELL 676
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAERA-ELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 677 MKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRKEKAAELS 756
Cdd:COG4942 181 AELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERT 243
|
..
gi 2217301410 757 SG 758
Cdd:COG4942 244 PA 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
421-936 |
2.96e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 421 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNTSWGdivEEE 500
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 501 PARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQmKAQQLR--EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMM 578
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 579 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 650
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 651 QARDEAVQERKRALEAERQARVEELLM---KRKEQEARieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQ 727
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 728 KKIQ--LKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKgRKHQQAVR 805
Cdd:PTZ00121 1336 KKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 806 ENTSIQGRELSDEEVEHLSLKkyiidiVVESTAPAEALKDGEERQknkkkakkikarmnfRAKEYESLMETKNSGSDSPY 885
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK------AEEKKKADEAKKKAEEAK---------------KADEAKKKAEEAKKAEEAKK 1464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2217301410 886 KAKLQRLAKDLLKQVQVQDSGSWANNKVSALDRTLGEITRILEKENVADQI 936
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
521-695 |
7.83e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQLREKLrEEKTLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 598
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 599 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKR-------------ALE 665
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkylslgqkgevlSIP 658
|
170 180 190
....*....|....*....|....*....|
gi 2217301410 666 AERQARVEELLMKRKEQEARIEQQRQEKEK 695
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSDLEKIQKPKKK 688
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
528-731 |
8.98e-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: 49.53 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 528 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDqrRRMMEEkllHAEFKREVQLQAIVKKAQEEEakv 607
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA--KLYQEE---QERKERQKEREEAEKKARQRQ--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 608 nEIAFINTLEAQNKRHdVLSKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQArveellMKRKEQEARIE 687
Cdd:pfam13868 236 -ELQQAREEQIELKER-RLAEEAEREEEEFE-----------RMLRKQAEDEEIEQEEAEKRR------MKRLEHRRELE 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217301410 688 QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ 731
Cdd:pfam13868 297 KQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
519-695 |
1.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 579
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 580 EKLLHaefKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvLSKLKEYEQRLNELQEERQRRQEEKQAR-DEAVQ 658
Cdd:PRK03918 313 EKRLS---RLEEEINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKKRLtGLTPE 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217301410 659 ERKRALEAERQAR--VEELLMKRKEQEARIEQQRQEKEK 695
Cdd:PRK03918 388 KLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKK 426
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
478-769 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 478 LADYEARESWRQNTSWGDIVEEEPARPpghgihmHEKLSspsRKRTIAESKKKHEEKQMKAQQ-LREKLREEKTLKLQKL 556
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 557 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 629
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 630 keyEQRLNELQEerqrrqeekQARDEAVQERK---RALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREdaarerar 706
Cdd:pfam15558 218 ---EERHRELRE---------KAQKEEEQFQRakwRAEEKEEE-RQEHKEALAELADRKIQQARQVAHKTVQ-------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301410 707 DREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 769
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 ... |
544-759 |
2.65e-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: 48.81 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 544 KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKllhAEFKREVQLQAIVKKAQEEEAKVNEIAF--------INT 615
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLneeridllQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 616 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-----RQARVEELLMKRKEQEARIEQQR 690
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElkselLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217301410 691 QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhdESIRRHMEQIEQRKEKAAELSSGR 759
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAK 391
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
518-754 |
2.97e-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: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 518 PSRKRTIAE---SKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 594
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 595 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 674
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 675 LLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 748
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 2217301410 749 KEKAAE 754
Cdd:pfam15558 225 REKAQK 230
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
504-610 |
4.26e-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: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 504 PPGHGIHMHEKLSSPSRKRTIAESKkkheEKQMKAQQLREKLREEKTLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKL 582
Cdd:pfam00836 23 PPSVNAAPPKLSLSPKKKDSSLEEI----QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKL 98
|
90 100 110
....*....|....*....|....*....|..
gi 2217301410 583 LHA----EFKREVQLQAIVKKAQEEEAKVNEI 610
Cdd:pfam00836 99 KQKmeayKENREAQIAALKEKLKEKEKHVEEV 130
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
576-754 |
4.43e-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: 47.22 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 576 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 655
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 656 AVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 734
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 2217301410 735 DESIRRHMEQIEQRKEKAAE 754
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
513-754 |
4.83e-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: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 513 EKLSSPSRKRTIAESKKKHEEKQMKAQQlREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ 592
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEK-ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 593 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARV 672
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 673 EELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIrrhmeQIEQRKEKA 752
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII-----SAHGRLGDL 534
|
..
gi 2217301410 753 AE 754
Cdd:pfam02463 535 GV 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
513-695 |
4.90e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 513 EKLSSPS-RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMmeekllhaefKREV 591
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 592 QLQAIVKKAQEEEAKVNEIAfintleaqnkrhDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 671
Cdd:COG4717 126 QLLPLYQELEALEAELAELP------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180
....*....|....*....|....
gi 2217301410 672 VEELLMKRKEQEARIEQQRQEKEK 695
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEE 217
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
385-697 |
6.50e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 385 EKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEeaiaSAIAEEEQ--LTREIEAEENNDINIETDNDsdfsasmgs 462
Cdd:pfam02029 18 ERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG----QGGLDEEEafLDRTAKREERRQKRLQEALE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 463 GSVSFCGMSMDWNDVLADYEARESWRQNTSW--GDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQ 540
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWekEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 541 LREKLREEKTLKLQKLLEREKDVRKWKEE---LLDQRRRMMEEKLLHAEF---------KREVQLQAIVKKAQEEEAKVN 608
Cdd:pfam02029 165 EAEEVPTENFAKEEVKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEevtklkvttKRRQGGLSQSQEREEEAEVFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 609 EIAfiNTLEAQNKRHDVLSKlKEYEQRLNELQEERQRRQEEKQARdeavQERKRALEAERQARVEEllmkRKEQEARIEQ 688
Cdd:pfam02029 245 EAE--QKLEELRRRRQEKES-EEFEKLRQKQQEAELELEELKKKR----EERRKLLEEEEQRRKQE----EAERKLREEE 313
|
....*....
gi 2217301410 689 qrqEKEKAR 697
Cdd:pfam02029 314 ---EKRRMK 319
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
774-806 |
6.53e-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: 41.08 E-value: 6.53e-05
10 20 30
....*....|....*....|....*....|...
gi 2217301410 774 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 806
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
528-756 |
1.28e-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: 46.50 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 528 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 607
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 608 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNElqeerqrRQEEKQARDEAVQERKRALEAERQARvEELLMKRKEQEARI 686
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301410 687 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 756
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
538-764 |
1.99e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 538 AQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 617
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 618 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQRQEKEKAR 697
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK-RKAEEEAKRKAEEERKAAEA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217301410 698 EDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTD 764
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
537-757 |
2.35e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 537 KAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 611
Cdd:PRK02224 409 NAEDFLEELREER----DELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 612 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLM 677
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 678 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 756
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 2217301410 757 S 757
Cdd:PRK02224 641 A 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
520-776 |
2.49e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 520 RKRTIAESKKKHEEKQMKAQQLRE---------KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRM-----MEEKL--- 582
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeleeKEERLeel 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 583 --LHAEFKREV-QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE 659
Cdd:PRK03918 344 kkKLKELEKRLeELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 660 RKRALEAERQAR-------------------------VEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAa 714
Cdd:PRK03918 424 LKKAIEELKKAKgkcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA- 502
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217301410 715 ltaaqqEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKK 776
Cdd:PRK03918 503 ------EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
515-748 |
2.58e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 515 LSSPSRKRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEeLLDQRRRMmEEKLlhaefkREV 591
Cdd:PRK03918 445 LTEEHRKELLEEYTaelKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKE-LAEQLKEL-EEKL------KKY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 592 QLQAIVKKAQEEEaKVNEIAfiNTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 671
Cdd:PRK03918 516 NLEELEKKAEEYE-KLKEKL--IKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 672 VEELLMKRKE---------------QEARIEQQRQEKEKAREDAARERARDREERLAALTaaqqEAMEELQKKIQLKHDE 736
Cdd:PRK03918 587 VEELEERLKElepfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELR----KELEELEKKYSEEEYE 662
|
250
....*....|..
gi 2217301410 737 SIRRHMEQIEQR 748
Cdd:PRK03918 663 ELREEYLELSRE 674
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
540-755 |
2.67e-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: 44.91 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 540 QLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRR--RMMEEKLLHAEFKREvqlqaivkkaQEEEAKVNE-IAFINTL 616
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIK-AEEKEEERRldEMMEEERERALEEEE----------EKEEERKEErKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 617 EAQNKRHDVLsKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKa 696
Cdd:pfam13868 79 EEQIEEREQK-RQEEYEEKLQE-----------REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301410 697 redaarerardreerlaaltaaQQEAMEELQKKIQ----LKHDESIRRHMEQIEQRKEKAAEL 755
Cdd:pfam13868 146 ----------------------EKEEEREEDERILeylkEKAEREEEREAEREEIEEEKEREI 186
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
482-755 |
2.70e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 482 EARESWRQntswgdivEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLReKLREEKTLKLQKLLEREK 561
Cdd:pfam02029 17 EERRRQKE--------EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 562 D----VRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaivkkAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLN 637
Cdd:pfam02029 88 EfdptIADEKESVAERKENNEEEENSSWEKEEKRD-------SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 638 ELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA 717
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 2217301410 718 AQQEAMEELQKKIQLKHDESIRRHMEQIEQRK-EKAAEL 755
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQqEAELEL 279
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
513-970 |
2.88e-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: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 513 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREK----LREEKTLKLQKLLEREKDVRKWKEElLDQRRRMMEEKLLHAEFK 588
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKakeeAEEERLAELEAKRQAEEEAREAKAE-AEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 589 REVQLQAIVKKAQEEEAKVNEiafintlEAQnkrhdvlsklkeyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 668
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAK-------EAE-------------AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 669 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 748
Cdd:COG3064 142 KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 749 KEKAAELSSGRHANTDYAPKLTPYERKKQcslcnvliSSEVYLFSHVKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKY 828
Cdd:COG3064 222 AARAAAASREAALAAVEATEEAALGGAEE--------AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 829 IIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSG 906
Cdd:COG3064 294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAasLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217301410 907 SWANNKVSALDRTLGEITRILEKENVADQIAFQAAGGLTALEHILQAVVPATNVNTVLRIPPKS 970
Cdd:COG3064 374 ALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALL 437
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
524-752 |
3.29e-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: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 524 IAESKKKHEEKQMKAQQLREK-----LREEKTLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 598
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 599 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMK 678
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217301410 679 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 752
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
516-755 |
3.36e-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: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 516 SSPSRKRTIAESKKKHEEKQmkaqqlreklREEKTLKLQKLLEREKDVR-KWKEELLDQRRRMMEEKLLHAEFKREVQlq 594
Cdd:pfam15709 297 SSPTQTFVVTGNMESEEERS----------EEDPSKALLEKREQEKASRdRLRAERAEMRRLEVERKRREQEEQRRLQ-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 595 aivKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeQRLNElqeerqrrQEEKQARDEAVQERKRALEAERqARVEE 674
Cdd:pfam15709 365 ---QEQLERAEKMRE-----ELELEQQRRFEEIRLRK--QRLEE--------ERQRQEEEERKQRLQLQAAQER-ARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 675 LLMKRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRK 749
Cdd:pfam15709 426 EEFRRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKE 501
|
....*.
gi 2217301410 750 EKAAEL 755
Cdd:pfam15709 502 EEAARL 507
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
650-777 |
3.85e-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: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 650 KQARDEAVQERKRALEAE-RQARVEEllmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 728
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217301410 729 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 777
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
524-722 |
4.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 524 IAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 597
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 598 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 668
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217301410 669 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 722
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
650-733 |
4.92e-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: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 650 KQARDEAVQERKRALEAERQarvEELLMKRKEQEarieqqRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 729
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAK------KKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 2217301410 730 IQLK 733
Cdd:pfam07946 319 KEQR 322
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
778-800 |
5.13e-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: 5.13e-04
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
519-693 |
5.62e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMME------EKLLHAEFKRE-- 590
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEyl 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 591 VQLQAIVKKAQEEEAKVNEI-AFINTLEAQNKRHDVLSK-LKEYEQRLNELQEERQRRQEEKQARDEAVQERKR--ALEA 666
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIeERIKELEEKEERLEELKKkLKELEKRLEELEERHELYEEAKAKKEELERLKKRltGLTP 386
|
170 180
....*....|....*....|....*...
gi 2217301410 667 ERQARVEELLMKRKEQ-EARIEQQRQEK 693
Cdd:PRK03918 387 EKLEKELEELEKAKEEiEEEISKITARI 414
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
522-929 |
6.14e-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: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 522 RTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQ 601
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 602 EEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEE 674
Cdd:TIGR00618 542 TSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 675 LLMKRKEQEARIE----QQRQEKEkaredaarerardreerlaaLTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKE 750
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALK--------------------LTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 751 KAAELSSGRHANTDYAPKLTPYERKKQCSLCNVLISS----EVYLFSHVKGRK-HQQAVRENTSIQG-RELSDEEVEHLS 824
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefnEIENASSSLGSDlAAREDALNQSLKElMHQARTVLKART 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 825 LkkyiIDIVVESTAPAEALKDGEERQKNKKKAkkikarmNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQD 904
Cdd:TIGR00618 761 E----AHFNNNEEVTAALQTGAELSHLAAEIQ-------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
410 420
....*....|....*....|....*
gi 2217301410 905 SGSwANNKVSALDRTLGEITRILEK 929
Cdd:TIGR00618 830 EEQ-FLSRLEEKSATLGEITHQLLK 853
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
533-761 |
6.55e-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: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 533 EKQMKAQQLREKLREEKTLKLQKLLEREkDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIvKKAQEEEAKVNEIAF 612
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEEQIEEREQ-KRQEEYEEKLQEREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 613 INTLEAQNKRHDvlskLKEYEQRLNElqeerqrrQEE-KQARDEAVQERKRALEAERQA------RVEELLMKRKEQEAR 685
Cdd:pfam13868 103 MDEIVERIQEED----QAEAEEKLEK--------QRQlREEIDEFNEEQAEWKELEKEEereedeRILEYLKEKAEREEE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301410 686 IEQQRQEKEKaredaARERARDREERLAALTAAQQEAMEEL-QKKIQLKHDESIR-RHMEQIEQRKEKAAELSSGRHA 761
Cdd:pfam13868 171 REAEREEIEE-----EKEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKERqKEREEAEKKARQRQELQQAREE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
520-639 |
7.20e-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: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 520 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 598
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2217301410 599 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNEL 639
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
532-695 |
7.57e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 532 EEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWK-EELLDQRRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEI 610
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQ--KQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 611 AFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQR 690
Cdd:PRK09510 145 AKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
....*
gi 2217301410 691 QEKEK 695
Cdd:PRK09510 214 EAKKK 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
531-695 |
7.71e-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: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 531 HEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKwKEELLDQRRRMMEEKLLHAEFKREVQLQAivkkaqeeeakvnEI 610
Cdd:COG4913 283 LWFAQRRLELLEAELEELRA-ELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLER-------------EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 611 AfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqARVEELLMKRKEQEARIEQQR 690
Cdd:COG4913 348 E-----RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRREL 421
|
....*
gi 2217301410 691 QEKEK 695
Cdd:COG4913 422 RELEA 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
552-757 |
1.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 552 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 626
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 627 SKLKEYEQRLNE----------LQEERQRRQEEKQARDEAVQERKRA---LEAERQARVEELLMKRKEQEArIEQQRQEK 693
Cdd:PRK02224 241 EVLEEHEERREEletleaeiedLRETIAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEA-VEARREEL 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217301410 694 EKAREDAARErardreerLAALTAAQQEAMEELQKkiqlkHDESIRRHMEQIEQRKEKAAELSS 757
Cdd:PRK02224 320 EDRDEELRDR--------LEECRVAAQAHNEEAES-----LREDADDLEERAEELREEAAELES 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
540-688 |
1.76e-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: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 540 QLREKLREEKTL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 614
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217301410 615 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLMKRKEQEARIEQ 688
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
513-911 |
2.29e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 513 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 590
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 591 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 659
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 660 RKRAL----EAERQARVEELLMKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 734
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 735 DESIRRHMEQIEQRKEKAAELSSGRhANTDYAPKLTpYERKKQCSLCNVLISSEVYLFS--HVKGRKHQQAVRENTSIQG 812
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRR-ENSLLDDKQL-YQLESTENLLKTINVKDLEVTNrnLVKPANVLQFIVAQMIKLN 1126
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 813 reLSDEEVEHLSLKKYIIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDS------- 883
Cdd:COG5022 1127 --LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 2217301410 884 PYKAKLQRLAKDLLKQVQVQDSGSWANN 911
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
521-639 |
2.33e-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: 41.06 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 521 KRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 600
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110
....*....|....*....|....*....|....*....
gi 2217301410 601 QEEEAKVNEiafinTLEAQNKRHDvlSKLKEYEQRLNEL 639
Cdd:COG1579 130 EAELAELEA-----ELEEKKAELD--EELAELEAELEEL 161
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
523-695 |
3.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 523 TIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMME-EKLLHAEFKREVQLQAIVKKAQ 601
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEElNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 602 EEEAKVNEIafINTLEAQNKrhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-RQARVEELLMKRK 680
Cdd:COG4372 108 EEAEELQEE--LEELQKERQ------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQALSEA 179
|
170
....*....|....*
gi 2217301410 681 EQEARIEQQRQEKEK 695
Cdd:COG4372 180 EAEQALDELLKEANR 194
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
520-610 |
3.65e-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: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 520 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 599
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEG 281
|
90
....*....|..
gi 2217301410 600 AQEE-EAKVNEI 610
Cdd:pfam02841 282 FKTEaESLQKEI 293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
629-755 |
3.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 629 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDR 708
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217301410 709 EERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 755
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAEL 175
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
654-758 |
4.93e-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: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 654 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 731
Cdd:cd16269 190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247
|
90 100
....*....|....*....|....*...
gi 2217301410 732 LKHDESIRRHMEQIEQR-KEKAAELSSG 758
Cdd:cd16269 248 EERENLLKEQERALESKlKEQEALLEEG 275
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
543-755 |
5.34e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 543 EKLREEktlkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 622
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 623 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAA 701
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301410 702 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 755
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-731 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 384 AEKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSg 463
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 464 svsfcgmSMDWNDVLADYEARESWRQNTSWG----------DIVEEEPARPPGHGIHMHEKLSSPSR--KRTIAESKKKH 531
Cdd:COG1196 498 -------EAEADYEGFLEGVKAALLLAGLRGlagavavligVEAAYEAALEAALAAALQNIVVEDDEvaAAAIEYLKAAK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 532 EEKQMKAQQLREKLREEKTLKLQKLL----------EREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQ 601
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 602 EEEAKVNEIAFIntLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKE 681
Cdd:COG1196 651 LEGEGGSAGGSL--TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2217301410 682 QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEaMEELQKKIQ 731
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE-LERLEREIE 777
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
525-609 |
7.18e-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: 38.49 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 525 AESKKKHEEKQMKAQQLRE--------KLREEKTLKLQKLLEREKDVRKWKEEllDQRRRMMEEKLLHAEFKREVQLQAI 596
Cdd:pfam15346 43 VEEARKIMEKQVLEELEREreaeleeeRRKEEEERKKREELERILEENNRKIE--EAQRKEAEERLAMLEEQRRMKEERQ 120
|
90
....*....|...
gi 2217301410 597 VKKAQEEEAKVNE 609
Cdd:pfam15346 121 RREKEEEEREKRE 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-695 |
7.19e-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: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTL--KLQKLLEREKDVRKWKEEL--LDQRRRMMEE---KLLHAEfKREV 591
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIaeLEAELERLDAssdDLAALE-EQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 592 QLQAIVKKAQEEEAKVNEIAFintlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeekqARDEAVQERKRALEAERQAR 671
Cdd:COG4913 696 ELEAELEELEEELDELKGEIG----RLEKELEQAEEELDELQDRLEA-------------AEDLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....
gi 2217301410 672 VEELLMKRKEQEARIEQQRQEKEK 695
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARL 782
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
524-736 |
7.22e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 524 IAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAE----FKREVQLQAIVKK 599
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 600 AQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEA--ERQARVEEL 675
Cdd:COG1340 152 AKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQELHEEMIEL---YKEADELRKEADELHKEivEAQEKADEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217301410 676 lmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 736
Cdd:COG1340 229 ---HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEE 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
559-754 |
7.37e-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: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 559 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 632
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 633 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLMKRKEQEARIEQQRQEKEKAREDAA 701
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217301410 702 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 754
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
519-695 |
7.65e-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: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 519 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRRRMMEekllhaefKREVQLQAiVK 598
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEARIK--------KYEEQLGN-VR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 599 KAQEEEAKVNEIafintlEAQNKRHDVLSK-LKEYEQRLNELqeerqrrqeekqardEAVQERKRALEAERQARVEELLM 677
Cdd:COG1579 87 NNKEYEALQKEI------ESLKRRISDLEDeILELMERIEEL---------------EEELAELEAELAELEAELEEKKA 145
|
170
....*....|....*...
gi 2217301410 678 KRKEQEARIEQQRQEKEK 695
Cdd:COG1579 146 ELDEELAELEAELEELEA 163
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
651-754 |
7.81e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 651 QARDEAVQERKRALEAERQARVEEllMKRKEQEARI--EQQRQEKEKAREDAARERARDREERLAALTAAQQeAMEELQK 728
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQ--KKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKK 169
|
90 100
....*....|....*....|....*.
gi 2217301410 729 KiqlkhdesirrhmEQIEQRKEKAAE 754
Cdd:PRK09510 170 K-------------AEAEAAKKAAAE 182
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
516-753 |
7.97e-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: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 516 SSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLlerekdvrKWKEELLDQRRRMME---EKLLHAEFKREVQ 592
Cdd:TIGR00618 216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL--------KKQQLLKQLRARIEElraQEAVLEETQERIN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 593 LQAIVKKAQEEEAKVNEIAF----INTL--EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQ----ARDEAVQERKR 662
Cdd:TIGR00618 288 RARKAAPLAAHIKAVTQIEQqaqrIHTElqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301410 663 ALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 742
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250
....*....|....
gi 2217301410 743 E---QIEQRKEKAA 753
Cdd:TIGR00618 448 TctaQCEKLEKIHL 461
|
|
| |
