|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
842-1921 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1413.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 842 RHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLE 921
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 922 ARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRV 1001
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1002 AEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK 1081
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1082 EEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL 1161
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1162 RSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKG 1241
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1242 DSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEEN 1321
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1322 RQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRL 1401
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1402 EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSL 1481
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1482 ARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 1561
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1562 LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLR 1641
Cdd:pfam01576 722 MQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLK 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1642 KLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALAL 1721
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1722 EEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAV 1801
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1802 KSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEE 1881
Cdd:pfam01576 962 KSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 74180985 1882 AEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:pfam01576 1042 AEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1360.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKD---QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 74180985 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
95-764 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1343.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKD----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYR-FLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 330 GIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 410 ADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 490 EEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK-FQKPKQLKDKADF 568
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsETALPGAFKTRKGMFRTVGQ 648
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 74180985 729 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1335.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPED 334
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 335 EQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 495 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 574
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 575 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 654
Cdd:cd14919 481 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 655 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 734
Cdd:cd14919 561 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 74180985 735 DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14919 641 DGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1306.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtALPGAFKTRKGMFRTVG 647
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 74180985 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1251.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtaLPGAFKTRKGMFRTVG 647
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 74180985 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1200.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 74180985 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1147.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASShKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 241
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 242 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 321
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 322 TMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 482 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKpKQ 561
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 562 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKG 641
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 74180985 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1128.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 331
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 74180985 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-764 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1119.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 83 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 163 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 243 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQE 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 322 TMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:pfam00063 320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 482 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 561
Cdd:pfam00063 400 HHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 562 lKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVagmsETALPGAFKTRKG 641
Cdd:pfam00063 477 -QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 74180985 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-776 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1026.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 76 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 156 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKkdqGELERQLLQANPILEAFGNAKTVKNDNSSRF 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 236 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQ 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVDGID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 315 DKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNT-AAQKVSHLLGINVTDFTRGILTPR 393
Cdd:smart00242 238 DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTH 553
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 554 PKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalp 633
Cdd:smart00242 474 PHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 634 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:smart00242 535 VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 714 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERD 776
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1151 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 908.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 32 VWVPSSKNGFEPASLKEEVGEEAIVEL---VENGKKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 106
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 107 SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 186
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 187 VIQYLAHVASSHKSkkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIR 266
Cdd:COG5022 172 IMQYLASVTSSSTV--EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 267 QAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISG 345
Cdd:COG5022 250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 346 VLQLGNIAFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERM 425
Cdd:COG5022 330 ILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 426 FRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFg 505
Cdd:COG5022 409 FDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 506 LDLQPCIDLIEKpAGPPGILALLDEECWFPKATDKSFVEKVVQ--EQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADE 583
Cdd:COG5022 487 FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDVEG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 584 WLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIigldqvagmsetalpgafkTRKGMFRTVGQLYKEQLAKLMATLRN 663
Cdd:COG5022 564 FLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------------------ESKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 664 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS----IPKGFMDGKQA 739
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 740 CVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAY 819
Cdd:COG5022 705 VKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 820 LRLRNWQWWRLFTKVKPLLNSIRHEDELLAKEAELTKVrekhlaaenrltemetmqsQLMAEK-LQLQEQLQAETELCAE 898
Cdd:COG5022 785 RLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL-------------------QKTIKReKKLRETEEVEFSLKAE 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 899 AEELRARLTAKKQELEEICHDLEARVeeeeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEE 978
Cdd:COG5022 846 VLIQKFGRSLKAKKRFSLLKKETIYL-------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELK-KSLSS 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 979 DQII-MEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKS--------KSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG5022 918 DLIEnLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPElnklheveSKLKETSEEYEDLLKKSTILVREGNKANSELKNF 997
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1050 RRKLegdsTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAA---QKNMALKKIRELETQISELQEDLeseras 1126
Cdd:COG5022 998 KKEL----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTelsILKPLQKLKGLLLLENNQLQARY------ 1066
|
1130 1140
....*....|....*....|....*
gi 74180985 1127 rnKAEKQKRDLGEELEALKTELEDT 1151
Cdd:COG5022 1067 --KALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-764 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 881.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASSHKSKKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL-----SNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 327 RIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNT--DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQ-GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 484 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 563
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 564 DKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriigldqvagmsetalpgafktrkgmf 643
Cdd:cd00124 478 KLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 644 rtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd00124 519 ------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 74180985 724 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 787.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVAS---------SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 245
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 246 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETM 323
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 324 EAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 403
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 404 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 484 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 559
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 560 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTR 639
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--------VGSDSTEDPKSGVKEK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 640 K---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14927 548 RkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 74180985 717 FRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14927 628 FKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 762.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 329 MGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKA 566
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 567 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVAKKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 757.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKD-QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKeYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 333 EDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 493 QREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK---ADF 568
Cdd:cd14934 400 KREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdriIGLDQVAGMSETALPGAFKTRKGM-FRTVG 647
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMTVS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14934 543 NFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPN 622
|
650 660 670
....*....|....*....|....*....|....*..
gi 74180985 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14934 623 VIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 753.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMG 330
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 331 IPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 411 DFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 491 EYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLK---DKA 566
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiGLDQVAGMSETAlpGAFKTRKGMFRTV 646
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAK--GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 74180985 727 NSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 731.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDILGFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 333 EDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14929 239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14929 319 AVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 493 QREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK--ADFC 569
Cdd:cd14929 398 RKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGmseTALPGAFKTRK--GMFRTVG 647
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD---SAIQFGEKKRKkgASFQTVA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14929 545 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 74180985 728 SIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14929 625 TFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-764 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 717.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSG-LIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKKdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFA 413
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 414 IEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 493 QREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK--FQKPKQLKDKadFCI 570
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvdriigldqvagmsetalpgafKTRKgmfRTVGQLY 650
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW 596
|
650 660 670
....*....|....*....|....*....|....
gi 74180985 731 KGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01380 597 LR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 712.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 329 MGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK- 565
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 566 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 695.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 565
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 566 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 643
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 692.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASSHKSKKD------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYR--FLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDK 565
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 566 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigLDQVAGMSETALPGAfKTRKGMF 643
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY-----AGAEAGDSGGSKKGG-KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-764 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 690.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 177 GAGKTENTKKVIQYLAHVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 330 GIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 409 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 489 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 568 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAfKTRKGMFRT 645
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSGAKKGA-KKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 74180985 726 PNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 327 RIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 564
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGM 642
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG-----KKKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 74180985 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14912 631 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 327 RIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 565 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqvAGMSETALPGAFK--TRK 640
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG----------AAAAEAEEGGGKKggKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 641 G-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14910 546 GsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 74180985 720 RYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14910 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-764 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 676.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASSHKskkdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--HLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 333 EDEQMGLLRVISGVLQLGNIAFKK-ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14883 316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 492 YQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAGMSETALPGAfKTRKGMfRTVGQLYK 651
Cdd:cd14883 472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSR-GTSKGK-PTVGDTFK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14883 549 HQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA 628
|
650 660 670
....*....|....*....|....*....|...
gi 74180985 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14883 629 DHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 675.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 327 RIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 74180985 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-764 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 655.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVasshkSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG---RDYVQKAQTKE 408
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFVEKVVQEQGTHPKFQKPKQLKD--K 565
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 566 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalpgafKTRKGMFRT 645
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 74180985 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-764 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 651.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASshkskkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPED 334
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 335 EQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd01383 314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 495 EGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkqlKDKAdFCIIHYA 574
Cdd:cd01383 394 DGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIRHYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 575 GKVDYKADEWLMKNMDPLNDNIATLL----HQSSDKFVSELWKDVDRIigldqvagmsetALPGAFKTRKGMFRTVGQLY 650
Cdd:cd01383 467 GEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKA------------LPLTKASGSDSQKQSVATKF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIp 730
Cdd:cd01383 535 KGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV- 613
|
650 660 670
....*....|....*....|....*....|....
gi 74180985 731 KGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01383 614 SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-764 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 635.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGIS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 333 EDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPD---NTAAQKVSHLLGINVTDFTRGiLTPRIKVGRD-YVQKAQTKE 408
Cdd:cd01384 239 EEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 409 QADFAIEALAKATYERMFRWLVLRINKAL--DKTKRqgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd01384 318 AATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKqlKDKA 566
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalPGAFKTRKgmFRTV 646
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR---------------EGTSSSSK--FSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 74180985 727 NsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01384 613 E-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-764 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 616.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGAS--FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01381 315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 490 EEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAdF 568
Cdd:cd01381 395 EEYDKEGINWQHIEF-VDNQDVLDLIaLKPM---NIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS-F 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdVDRIIGLDQVAGMSetalpgafkTRKGMfRTVGQ 648
Cdd:cd01381 470 GINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSE---------TRKKS-PTLSS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd01381 533 QFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 74180985 729 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-764 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 597.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---------------KDPLLDDVGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKKERNT-------DQASMPDNTAAqkvSHLLGINVTDF-----TRGILTPRIKVGRDYV 401
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRGGAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 482 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKP-- 559
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrk 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 560 ------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagMSETALP 633
Cdd:cd01382 453 sklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN---------NNKDSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 634 gafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:cd01382 524 ---KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 74180985 714 FQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01382 601 FHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-764 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 569.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASShkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAgeHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKKERNTDQAS---MPDNTAAQKVSHLLGINVTDFTRGILTPRIKV-GRDYVQKAQTKEQ 409
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 490 EEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFC 569
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalpGAFKTRKGmfrTVGQL 649
Cdd:cd14872 470 VKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-----------------GDQKTSKV---TLGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPNSI 729
Cdd:cd14872 530 FRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTI 608
|
650 660 670
....*....|....*....|....*....|....*.
gi 74180985 730 PKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14872 609 AKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-764 |
8.80e-180 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 560.14 E-value: 8.80e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01387 155 SQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKKERNTDQ---ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd01387 235 EEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd01387 315 LDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 491 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADFCI 570
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPEFTI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldQVAGMSETALP----GAFKTRKGMFRTV 646
Cdd:cd01387 469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPrlgkGRFVTMKPRTPTV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01387 540 AARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVA 619
|
650 660 670
....*....|....*....|....*....|....*....
gi 74180985 727 NSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 764
Cdd:cd01387 620 LKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-764 |
2.26e-178 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 556.70 E-value: 2.26e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 170 ILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 237 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 317 DMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASmpDNTAAQKVSH---LLGINVTDFTRGILTPR 393
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-KPAGPPGILALLDeECWFPKAT--DKSFVEKVVQEQ 550
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 551 GT-------------HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdr 617
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 618 iigldqvagmsetalpgafKTRKGMfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 697
Cdd:cd14890 542 -------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 698 LEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-762 |
1.01e-173 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 544.00 E-value: 1.01e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 167 --DQSILCTGESGAGKTENTKKVIQYLAHVASshKSKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 239
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 240 RINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKD 317
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 318 MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAF-KKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKV 396
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 397 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS-FIGILDIAGFEIFDLNSFEQLCINYTNEK 475
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 476 LQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQG 551
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 552 THPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmseta 631
Cdd:cd14901 472 KHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 632 lpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 711
Cdd:cd14901 531 -------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 712 VVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSKVF 762
Cdd:cd14901 598 FPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-764 |
1.43e-173 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 544.66 E-value: 1.43e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVasshkSKKDQGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCY-TLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAFKKER-NTDQASMPDNTAAQK-VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 410 ADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 486 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkQLKDK 565
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 566 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVAGMSETALPGAFKT-----RK 640
Cdd:cd01385 470 A-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAVFRWAVLRAFFRAmaafrEA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 641 GMFR-----------------------------TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 691
Cdd:cd01385 542 GRRRaqrtaghsltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQ 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 692 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01385 622 LRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-764 |
2.06e-172 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 540.52 E-value: 2.06e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVAsshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLsgAGEHLKTDLLLEPYNKYRFL-SNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 329 MGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASM--PDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14903 230 IGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14903 310 KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVVqeqGTHPKFQK----PKql 562
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdrIIGLDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14903 460 TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 74180985 723 ILTPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 764
Cdd:cd14903 617 LFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-764 |
9.32e-169 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 529.54 E-value: 9.32e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVasshkSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSNGHVTIPG----QQDKDMFQETMEAMRIMG 330
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 331 IPEDEQMGLLRVISGVLQLGNIAFK---KERNTDQASM-PDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQ 405
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 406 TKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 484 MFILEQEEYQREGIEWNFIDFGlDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPkFQKPKql 562
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd01379 469 SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 frTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 723 ILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-764 |
1.99e-168 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 528.88 E-value: 1.99e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLahvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHL-----MKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-------KDMFQETMEAM 326
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLTNIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 327 RIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 407 KEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKql 562
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASP-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd14897 471 GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 frtvgQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14897 522 -----SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYK 596
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 723 ILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14897 597 EICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-726 |
3.73e-168 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 529.26 E-value: 3.73e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD--------- 244
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN------------------- 305
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAdakpisidmssfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 306 -----GHVTIPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQ---KVSHL 377
Cdd:cd14888 238 yltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 378 LGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFE 457
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKA 537
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVPGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 538 TDKSFVEKVVQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-VD 616
Cdd:cd14888 475 KDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAyLR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 617 RIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14888 553 RGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 74180985 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-764 |
1.26e-167 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 527.06 E-value: 1.26e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASSH---KSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 330 GIPEDEQMGLLRVISGVLQLGNIAFKkerNTDQASMPDNTAAQKVSHLLGINVTDFTRgILTPRIKVGR-DYVQKAQTKE 408
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTD-ALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 409 QADFAIEALAKATYERMFRWLVLRINKALdkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDkaDF 568
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdvdriiglDQVAGMSETALPGAFKTRKGmfRTVGQ 648
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR--PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 74180985 729 IPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-764 |
1.37e-165 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 522.01 E-value: 1.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 168 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMF 319
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 320 QETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFkkERNTDQ----ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 395
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 396 VGRDYV-QKAQTKEQADFAIEALAKATYERMFRWLVLRINKAldkTKRQG------------ASFIGILDIAGFEIFDLN 462
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 463 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKS 541
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 542 FVEKVVQEQ-GTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriig 620
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 621 ldqvagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 700
Cdd:cd14892 536 ----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEV 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 701 IRICRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----LDSNLYRIGQSKVFFR 764
Cdd:cd14892 587 VRIRREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-764 |
9.98e-153 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 486.72 E-value: 9.98e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 173 TGESGAGKTENTKKVIQYLAHVAsshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGA 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHvtipGQQD-----KDMFQETMEAMR 327
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKRevqywKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKkerntdqasmPDNTAAQKVSH-------------------LLG--INVTDFT 386
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENdsngwlkaaagqfgvseedLLKtlTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 387 RGiltprikvgrDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG--ASFIGILDIAGFEIFDLNSF 464
Cdd:cd14889 302 RG----------EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14889 372 EQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 545 KVVQEQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLDQ 623
Cdd:cd14889 449 KLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMP 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 624 VAGMSETALPGAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14889 527 RAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRI 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 704 CRQGFPNRVVFQEFRQRYEIL--TPNsIPKgfmdGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14889 604 RREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-727 |
4.51e-149 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 477.22 E-value: 4.51e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 166 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSK--------------KDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 232 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLS---NG 306
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 307 HVTIPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQA--SMPDNTAAQKVSHLLGINVTD 384
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 385 FTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------DKTKRQGASFIGILDIAGFE 457
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP 535
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 536 KATDKSFVEKVVQEQGTHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDV 615
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 616 DRiigldqvagmSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCN 695
Cdd:cd14907 557 DG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 74180985 696 GVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-730 |
4.01e-146 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 467.48 E-value: 4.01e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 164 ----DREDQSILCTGESGAGKTENTKKVIQYLAHV-----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 235 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlktdlllepynkyrflsnghvtipGQQ 314
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 315 DKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTD-QASMPDNTAAQKV------SHLLGINVTDFTR 387
Cdd:cd14900 217 KRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 388 GILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGAS-FIGILDIAGFEIFDLNS 463
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 464 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFV 543
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 544 EKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatLLHQSSdkfvselwkdVDriigldq 623
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 624 vagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14900 509 ------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|....*..
gi 74180985 704 CRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-764 |
2.27e-144 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 462.98 E-value: 2.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERyySGLI----YTYSGLFCVVINPYKNLPiysEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 167
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 168 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKSKKDQG-----------ELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEqsskkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 235 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPG 312
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 313 QQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKK----ERNTDQASMPDNTAAQKVSHLLGINVTDFTRG 388
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 389 ILTPRIkVGRDYVQKAQ-TKEQADFAIEALAKATYERMFRWLVLRINKALDKtKRQGASFIGILDIAGFEIFDL-NSFEQ 466
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 467 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKV 546
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 547 VQEQGTHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHqSSDKFVselwkdvdriigldqva 625
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFS----------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 626 gmsetalpgafktrkgmfrtvgqlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 705
Cdd:cd14891 532 --------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 706 QGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSKVFFR 764
Cdd:cd14891 586 VGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-764 |
1.58e-142 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 458.25 E-value: 1.58e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASSHKSKKDQgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAFkKERNTDQASMPDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQTKEQA 410
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRI-EEALCNRSVVTRnESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 491 EYQREGIEWNFIDFGlDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKPKQlkDKAD 567
Cdd:cd14904 394 EYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvaGMSETALPGAFKTRKGMfRTVG 647
Cdd:cd14904 468 FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 74180985 728 SIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFFR 764
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-764 |
2.64e-140 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 451.93 E-value: 2.64e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLahvaSSHKSKKDQGELeRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKKERNTDQ--ASMPDNTAAQKVSHLLGINvTDFTRGILTPRIKV-GRDYVQKAQTKEQA 410
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPVEGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14896 314 IDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 490 EEYQREGIEWNFIDfGLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADFC 569
Cdd:cd14896 394 EECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmsetalpgafktrkgmfrTVGQL 649
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI 729
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*
gi 74180985 730 PkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14896 611 E-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-747 |
2.43e-139 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 451.65 E-value: 2.43e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 165 REDQSILCTGESGAGKTENTKKVIQYLAHV----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT---IPGQQDKD 317
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 318 --MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKE-RNTDQASMPDNTAAQ--KVSHLLGINVTDFTRGILTP 392
Cdd:cd14902 241 aqLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 393 RIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD--------KTKRQGASFIGILDIAGFEIFDLNSF 464
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK--SNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 545 KVVQEQGThpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSelwkdvdrIIGLDQV 624
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV--------AIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 625 AGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 702
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 74180985 703 ICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 747
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-764 |
7.62e-135 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 438.19 E-value: 7.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 165 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHK-SKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKF 238
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 239 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--------HLKTDLLLEPYNKYRFLSNGHVTI 310
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 311 PGQ-QDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNtDQASMPDNTAAQK----VSHLLGINVTDF 385
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 386 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSF 464
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFV 543
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 544 EKVV--------QEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdniatllhqssdkfvselwkd 614
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 615 vdriigldqvagmsetalpgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALELDSNLYR--------------- 755
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipedt 671
|
730
....*....|.
gi 74180985 756 --IGQSKVFFR 764
Cdd:cd14908 672 mqLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
93-821 |
3.68e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 437.92 E-value: 3.68e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 93 NEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 172 CTGESGAGKTENTKKVIQYLAhvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA----SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:PTZ00014 264 GSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 332 PEDEQMGLLRVISGVLQLGNIAF--KKERNTDQASM--PDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:PTZ00014 344 SESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:PTZ00014 424 KDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDK 565
Cdd:PTZ00014 503 RESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 566 aDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGMFrt 645
Cdd:PTZ00014 579 -NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL-- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:PTZ00014 640 IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKR 802
Cdd:PTZ00014 720 LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN 799
|
730
....*....|....*....
gi 74180985 803 qqqltaMKVLQRNCaAYLR 821
Cdd:PTZ00014 800 ------IKSLVRIQ-AHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-764 |
2.79e-130 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 425.91 E-value: 2.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPiyseeivEMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 163
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 164 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 237
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 238 FIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNG--HV 308
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGqcYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 309 TIPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTD---------------QASMPDNTAAQK 373
Cdd:cd14895 235 RNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 374 ---VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTK--------- 441
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 442 -RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEkpAG 520
Cdd:cd14895 395 nKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE--QR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 521 PPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIAT 598
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 599 LLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalpgafKTRKGMFRTV--GQLYKEQLAKLMATLRNTNPNFVRCIIPNH 676
Cdd:cd14895 550 VLGKTSDAHLRELFEFFKASESAELSLGQPKL------RRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 677 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELdsnlyri 756
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 74180985 757 GQSKVFFR 764
Cdd:cd14895 697 GKTRVFLR 704
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-764 |
3.93e-126 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 413.63 E-value: 3.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKyrflSNGHVTIPGQQDKDM------FQETMEAMR 327
Cdd:cd01386 156 IQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAAMK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGI------------LTPRIK 395
Cdd:cd01386 232 TLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 396 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEifdlN----------SFE 465
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 466 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAG------------PPGILALLDEECW 533
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 534 FPKATDKSFVEKVVQEQG--THPKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSDKF 607
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 608 vselwkdvdriigldqvagmsetalpgAFKTRKGMFRTVgqlyKEQLAKLMATLRNTNPNFVRCIIPNHE------KKAG 681
Cdd:cd01386 547 ---------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 682 KLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF-----MDGKQACVLMIKALELD 750
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 74180985 751 SNLYRIGQSKVFFR 764
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-762 |
3.68e-124 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 406.68 E-value: 3.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAhvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLsNGHVT-IPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL-NPKCLdVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 333 EDEQMGLLRVISGVLQLGNIAFKKErntDQASMPDntAA----------QKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 402
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 483 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFqKPKQL 562
Cdd:cd14876 390 IVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGM 642
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 FrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14876 530 L--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 74180985 723 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 762
Cdd:cd14876 608 FLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-762 |
1.63e-123 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 405.00 E-value: 1.63e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 171 LCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERieqRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIpgqqDKDMFQETMEAMR 327
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVS---HLLGINVTDFTRGILTPRIKVGRDYV--Q 402
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQL 562
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgafktrkgm 642
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPV---------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14880 544 -LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 74180985 723 ILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 762
Cdd:cd14880 623 LLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-760 |
3.55e-121 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 400.51 E-value: 3.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 173 TGESGAGKTENTKKVIQYLAHVASSHKSKK-----DQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 247 GYIVGANIETYLLEKSR-AIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP-YNKYRFL--------------SNGHVTI 310
Cdd:cd14906 161 GKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 311 PGQQDKD-MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQAS--MPDNTAA-QKVSHLLGINVTDFT 386
Cdd:cd14906 241 NNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 387 RGILTPRIKV-GRDYVQ-KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDK----------TKRQGASFIGILDIA 454
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 455 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWF 534
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 535 PKATDKSFVEKVVQEQGTHPKFQkpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKd 614
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYY--QRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 615 vdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14906 555 ------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-764 |
2.44e-113 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 376.46 E-value: 2.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYS-GLIYTYSGLFCVVINPYKNLPIYSEEIVEMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 171
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 172 CTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQ----LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKidenLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLSNGHVTI----PGQ--QDKDMF 319
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVrrgvDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 320 QETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILtprIKVGRD 399
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 400 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQ 478
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 479 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQ 557
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 558 KPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigLDQVAGMSEtalpgafk 637
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLAR-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 638 tRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 717
Cdd:cd14875 536 -RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 74180985 718 RQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVFFR 764
Cdd:cd14875 612 CRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-764 |
2.45e-110 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 367.29 E-value: 2.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 169 SILCTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMR 327
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 328 IMgIPEDEQMGLLRVISGVLQLGNIAFKKERN--TDQASMPDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 484
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 485 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgpPGILALLDEECWFPKATDKSFVE---KVVQEQGTHPKfqKPKQ 561
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSsckSKIKNNSFIPG--KGSQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 562 LKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLdqvagmsetalpgafktRKG 641
Cdd:cd14886 469 CN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-----------------MKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 642 MFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14886 528 KF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRN 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 74180985 722 EILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14886 606 KILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-721 |
9.43e-107 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 359.02 E-value: 9.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 164 DREDQSILCTGESGAGKTENTKKVIQYLA------------HVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 232 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-----AGEHLKTDLLLEPYNKYRFLSN 305
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 306 GHVTI--PGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAF-----KKERNT--DQASMPDNTAA----- 371
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 372 QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------------- 437
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 438 DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEK 517
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 518 PagPPGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 594
Cdd:cd14899 480 R--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 595 NIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMFRT----VGQLYKEQLAKLMATLRNTNPNFVR 670
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSND----EDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVR 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 74180985 671 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14899 634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-764 |
2.04e-100 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 340.86 E-value: 2.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYS--------GLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 167 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvtiPGQQDKDMF--QETME 324
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTdlRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 325 AMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTA--------AQKVSHLL-------GINVTDFTRGI 389
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 390 LT--------PRIKVGRDYV------------QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR------- 442
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 443 ------QGASFIGILDIAGFEIF---DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQPC 511
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 512 IDLIEKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEKVVQEQGTHPKFQK--PKQL 562
Cdd:cd14887 463 STLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLhQSSDKFVSElwkdvdriIGLDQVAGMSetalpgAFKTRKgm 642
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNSGVR------AISSRR-- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14887 606 -STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 74180985 723 ILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14887 685 TKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-763 |
3.65e-97 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 328.74 E-value: 3.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 92 LNEASVLHNLKERYYSGLIYTY---SGLfcVVINPYKNLPIYSEEIVEMYK-------GKKRHEMPPHIYAITDTAYRSM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 162 MQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 241
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSHSKKGTK--LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 242 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVT--IPGQQDKD 317
Cdd:cd14879 156 QFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLplGPGSDDAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 318 MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAF--KKERNTDQASMpDNTAA-QKVSHLLGINVTDFtRGILTPRI 394
Cdd:cd14879 236 GFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSLTYKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 395 K-VGRD----YVQKAQTKEQADfaieALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFD---LNSFEQ 466
Cdd:cd14879 314 KlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRSstgGNSLDQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 467 LCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIEKPAGppGILALLDEEC-WFPKATDK 540
Cdd:cd14879 390 FCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLLGILDDQTrRMPKKTDE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 541 SFVEKVVQEQGTHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllhqSSDkFVSelwkdvdr 617
Cdd:cd14879 462 QMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 618 iigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 697
Cdd:cd14879 523 ------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGL 577
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 698 LEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYRIGQSKVFF 763
Cdd:cd14879 578 PELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-764 |
5.34e-97 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 328.13 E-value: 5.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEivemYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQ-YLAHVasshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV-------KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIpE 333
Cdd:cd14937 150 IEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM-H 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFK---KERNTDQASMPDNT--AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14937 229 DMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14937 309 ESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 489 QEEYQREGIEWNFIDFGLDlQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKaDF 568
Cdd:cd14937 388 TELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagMSETAlpgafkTRKGMfrtVGQ 648
Cdd:cd14937 463 VIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL------GRKNL---ITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd14937 524 KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYST 602
|
650 660 670
....*....|....*....|....*....|....*.
gi 74180985 729 IPKGFMDGKQACVLMIKAlELDSNLYRIGQSKVFFR 764
Cdd:cd14937 603 SKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-726 |
6.77e-97 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 325.70 E-value: 6.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNlpIYSEEIVEMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGYIVGANIE 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlllepYNKYRF-LSNGHVTIPGQQDKDMFQETMEAMRIMGIPED 334
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIANFKSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 335 EQMGLlrvisGVLQLGNIAFKKERNTDQASmpdNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14898 225 EDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 415 EALAKATYERMFRWLVLRINKALDKTkrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 495 EGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVvqeqgthpKFQKPKQLKDKADFCII--H 572
Cdd:cd14898 374 EGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI--------KKYLNGFINTKARDKIKvsH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 573 YAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwKDVDRIIGLDQVAgmsetalpgafktRKGMFRTVGQLYKE 652
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN-------------DEGSKEDLVKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74180985 653 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-764 |
4.30e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 317.14 E-value: 4.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 172 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH----VTIPGQQDKDMFQETMEAM 326
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 327 RIMGIPEDEQMGLLRVISGVLQLGNIAFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 407 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 484 MFILEQEEYQREGIEWNFIDFGLDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKP 559
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 560 KQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigldqvagmsetal 632
Cdd:cd14878 473 KDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL--------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 633 pgaFKTRkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14878 532 ---FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 74180985 713 VFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14878 606 SFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
96-750 |
3.35e-82 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 284.70 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYknlpiyseeiveMYKGKKRH-------EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 169 SILCTGESGAGKTENTKKVIQYLAHVASshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 244
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQET 322
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 323 MEAMRIMGIPedeQMGLLRVISGVLQLGNIAFKkERNTDQASMPDNTAAQKVSHLLGINVTDFTRGiLTPRIK-VGRDYV 401
Cdd:cd14881 221 KACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKaldkTKRQGAS--------FIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 474 EKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIEkpAGPPGILALLDEECwFPKATDKSFVEKVVQEQGT 552
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 553 HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmsetal 632
Cdd:cd14881 448 NPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 633 pgAFKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14881 502 --GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 74180985 713 VFQEFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 750
Cdd:cd14881 573 RFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-716 |
9.15e-82 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 284.88 E-value: 9.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 167 DQSILCTGESGAGKTENTKKVIQYLAHVasshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 245 -------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSN----------G 306
Cdd:cd14884 157 entqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrsvkG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 307 HVTIPG----------QQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAFKkerntdqasmpdntaaqKVSH 376
Cdd:cd14884 237 TLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------AAAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 377 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA----------- 445
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysine 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 446 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKpagppgIL 525
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------IF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 526 ALLDE-----ECWFPKATDKSFV-----EKVVQEQGTH------PKFQK---PKQLKDKADFCIIHYAGKVDYKADEWLM 586
Cdd:cd14884 453 RRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 587 KNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNP 666
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDM 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 74180985 667 NFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14884 590 YYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-729 |
4.30e-70 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 249.02 E-value: 4.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 174 GESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNgYIVGAN 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 254 IE-TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14874 143 LKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 333 EDEQMGLLRVISGVLQLGNIAFKKERNTD---QASMPDNTAAQK-VSHLLGINVTDFTRgILTPRIKVGrdyvqKAQTKE 408
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLVN-FLLPKSEDG-----TTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 489 QEEYQREGIEWNF-IDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlKDKAD 567
Cdd:cd14874 375 LVDYAKDGISVDYkVPNSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KERLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalpgAFKTRKgMFRTVG 647
Cdd:cd14874 452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-------------------SSNTSD-MIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14874 512 QFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG 591
|
..
gi 74180985 728 SI 729
Cdd:cd14874 592 DI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-717 |
1.35e-68 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 245.77 E-value: 1.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASShKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 334 DEQMGLLRVISGVLQLGNIAFKKERNtdQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAqtkeqadfa 413
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 414 iEALAKATYERMFRWLVLRINKALDKTkrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 493
Cdd:cd14905 304 -DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 494 REGIEW-NFIDFGlDLQPCIDLIEKpagppgILALLDEECWFPKATDKSFVEKVVQEQGTHPKF-QKPKQlkdkadFCII 571
Cdd:cd14905 381 TERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV---SELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR---- 644
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLScgsn 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 645 --------------------------TVGQLYKeQLAKLMATLRNTNPN--FVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14905 528 npnnvnnpnnnsgggggggnsgggsgSGGSTYT-TYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLC 606
|
650 660
....*....|....*....|....*
gi 74180985 697 VLEGIRICRQGFP----NRVVFQEF 717
Cdd:cd14905 607 LLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-764 |
1.94e-67 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 241.57 E-value: 1.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 176 SGAGKTENTKKVIQYLAHVAsshksKKDQGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKtDLLLEPYNKYRFLSNGHVTIPG---------QQDKDMFQETME 324
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSklkyrrddpEGNVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 325 AMRIMGIPEDEQMGLLRVISGVLQLGNIAFKKerNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqgASF-----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 479
Cdd:cd14882 313 HTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 480 FNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIEKPAgppGILALLDEECwfPKATDKSFVEKVVQEQgtHPKF 556
Cdd:cd14882 390 YNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYIMDRIKEK--HSQF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 557 QKPKQlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMsetalpgaf 636
Cdd:cd14882 460 VKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 637 KTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14882 521 RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 74180985 717 FRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14882 598 FLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-722 |
5.45e-67 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 242.95 E-value: 5.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 98 LHNLKERYYSGLIYTYSGLFCVVINPYKNLPIY----------SEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRED 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 168 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKSKKDQGELE---RQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgEH---LKTDLLL-EPYNKYRFLSN-----GHVTIP 311
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 312 GQQDKDMfqetMEAMRIMGIPEDEQMGLLRVISGVLQLGNIAF-------KKERNTDQASMPDNTA------AQ--KVSH 376
Cdd:cd14893 243 ARDYRDL----MSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 377 LLGIN--VTD---FTRGILTpriKVGRDYVQ--KAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQG- 444
Cdd:cd14893 319 LLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 445 ---ASFIGILDIAGFEIFD--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCI 512
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 513 DLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD------------FCIIHYAGKVDYK 580
Cdd:cd14893 476 QLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 581 ADEWLMKNMDPLNDNIATLLHQSSDKfvselwkdVDRIIGLDQVA------GMSETALPGAF--KTRKGMFR-------- 644
Cdd:cd14893 554 GKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekAAKQTEERGSTssKFRKSASSaresknit 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 645 --TVGQLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14893 626 dsAATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
1.47e-59 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 202.57 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 117 FCVVINPYKNLPIYSEEIV-EMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 196 SSHKSKKD----------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd01363 81 FNGINKGEtegwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-762 |
3.59e-58 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 215.86 E-value: 3.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 175 ESGAGKTENTKKVIQYLAHVASSHKS------------------KKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 237 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 317 DMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNI----AFKKE----------------------RNTDQASMPDNTA 370
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 371 AQKV-SHLLGINVTDFTRGILTPRIkVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR--QGASF 447
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 448 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgpPGILAL 527
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 528 LDEECWFPKATDKS-FVEKVVQEQGTHPKFQKPKQLK-DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 605
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 606 KFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQ----LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA- 680
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 681 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 74180985 761 VF 762
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1830 |
1.68e-33 |
|
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: 141.73 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 933 YLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEE 1012
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARV 1092
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1093 EEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtlDSTAAQQELRSKREQEvsiL 1172
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEEL---L 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1173 KKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELaNEVKAllqgkgdsehkRKKVEA 1252
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQA-----------RLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1253 QLQELQVKFSEGERvrteladKVTKLQVELDSVTGLLSQSDSKSSKLTKdfsALESQLQDT-QELLQEENRQKLSLSTKL 1331
Cdd:TIGR02168 496 RLQENLEGFSEGVK-------ALLKNQSGLSGILGVLSELISVDEGYEA---AIEAALGGRlQAVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1332 KQMEDEKNSFREQLEEEEEAKRNLEkqiatlhaqvTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRL---EEKVAAY 1408
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGND----------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1409 DKLEKTKTR----------------LQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1472
Cdd:TIGR02168 636 ELAKKLRPGyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1473 EKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1552
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEA-------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1553 DAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKN 1632
Cdd:TIGR02168 789 AQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1633 REEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1712
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1713 ssgKGALALEEKRRLEARIAqleeeleeeqGNTELINDRLKKANLQIDQINTdlnlershaqKNENARQQLERQNKELKA 1792
Cdd:TIGR02168 948 ---EYSLTLEEAEALENKIE----------DDEEEARRRLKRLENKIKELGP----------VNLAAIEEYEELKERYDF 1004
|
890 900 910
....*....|....*....|....*....|....*...
gi 74180985 1793 KLQEMESAVKSKYKasiaaLEAKIaqleEQLDNETKER 1830
Cdd:TIGR02168 1005 LTAQKEDLTEAKET-----LEEAI----EEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1825 |
2.37e-32 |
|
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: 138.27 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1035 RLRREEKQRQeLEKTRRKLEgdstDLSDQIAELQAQIAELKMQ--LAKKEEELQAALARVEEE--AAQKNMALKKIRELE 1110
Cdd:TIGR02168 171 KERRKETERK-LERTRENLD----RLEDILNELERQLKSLERQaeKAERYKELKAELRELELAllVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1111 TQISELQEDLESERASRNKAEKQ---KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQI 1187
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1188 QEMRQKHSQAVEELADqleqtkrvkatLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERV 1267
Cdd:TIGR02168 326 EELESKLDELAEELAE-----------LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1268 RTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSalESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEE 1347
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1348 EEEAKRNLEKQIATLHAQVTDMKKKME--------------------DGVGCL----ETAEEAKRRLQKDLEGLSQ---- 1399
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQEnlegfsegvkallknqsglsGILGVLseliSVDEGYEAAIEAALGGRLQavvv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1400 -RLEEKVAAYDKLEKTK--------------TRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAeekTISAKYAEER 1464
Cdd:TIGR02168 553 eNLNAAKKAIAFLKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1465 DRAEAEAREKETKALSLARALEE-------AMEQKAELERLNKQFR-TEMEDLmsskddvGKSVHELEKSKRALEQQVEE 1536
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLDGdlvrpggVITGGSAKTNSSILERrREIEEL-------EEKIEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1537 MKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERdLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLE 1616
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1617 MDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK 1696
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1697 RQAQQERDELADEIanssgkgALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKN 1776
Cdd:TIGR02168 862 EELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 74180985 1777 ENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDN 1825
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
821-1654 |
1.71e-30 |
|
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: 132.10 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 821 RLRNWQWWRLFTKVKpllnsiRHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEqlqaetelcaEAE 900
Cdd:TIGR02168 221 ELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----------EIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 901 ELRARLTAKKQELEeichDLEARVeeeeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQ 980
Cdd:TIGR02168 285 ELQKELYALANEIS----RLEQQK-------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 981 IIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDL 1060
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1061 sdQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEE 1140
Cdd:TIGR02168 434 --ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1141 LEAlKTELEDTLDSTAAQQELRSKREQEVSI-----LKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATL 1215
Cdd:TIGR02168 512 LKN-QSGLSGILGVLSELISVDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1216 EKAKQTLENERGELANEVKALLQGKGDSEHKRKKV-----EAQLQELQVKFSEGERVRTELADKVTK------------- 1277
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddLDNALELAKKLRPGYRIVTLDGDLVRPggvitggsaktns 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1278 ----LQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKR 1353
Cdd:TIGR02168 671 sileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1354 NLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDldhQR 1433
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER---LE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1434 QSVSNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSK 1513
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1514 DDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEVNLQAMkaqferDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTLE------EAEALENKIEDDEEEARRRLKR 976
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1594 MEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANknreEAIKQLRKLQAQMKDCMREL 1654
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLT----EAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
991-1710 |
3.76e-30 |
|
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: 130.96 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 991 AKEKKLLEDR---VAEFttnlmeEEEKSKSLAKLK------NKHEAMITDLEERLRREEKQRQELEK----TRRKLEGDS 1057
Cdd:TIGR02169 152 PVERRKIIDEiagVAEF------DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQED-----------LESERAS 1126
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeLEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1127 RNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKhsqaVEELADQLE 1206
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1207 QTKRVKATLEKAKQTLENERGELANEVKALlqgkgdsehkrkkveaqLQELQVKFSEGERVRTELAD---KVTKLQVELD 1283
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRL-----------------QEELQRLSEELADLNAAIAGieaKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1284 SVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLH 1363
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1364 AQVTDMKKKMEDGVGCLETAeeAKRRLQK---DLEGLSQRL-----EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQS 1435
Cdd:TIGR02169 525 GTVAQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEAiellkRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1436 VsNLEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDRAEAEAR 1472
Cdd:TIGR02169 603 V-DLVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1473 EKEtkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1552
Cdd:TIGR02169 682 RLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1553 DAKLRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKN 1632
Cdd:TIGR02169 758 SELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1633 REEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
970-1554 |
3.45e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 970 EAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNK 1129
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1130 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvsilkktlEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTK 1209
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1210 RVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvkFSEGERVRTELADKVTKLQVELDSVTGLL 1289
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG--LRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1290 SQ----SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ 1365
Cdd:COG1196 548 LQnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1366 VTDmkkKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRqsvsnlEKKQKK 1445
Cdd:COG1196 628 VAA---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE------LELEEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1446 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskDDVGKSVHELEK 1525
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----EELERELERLER 774
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 74180985 1526 SKRAL--------------EQQVEEMKTQLEELEDELQATEDA 1554
Cdd:COG1196 775 EIEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEA 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1733 |
1.30e-27 |
|
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: 122.48 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 851 EAELTKVREKHLAAENRLTEMETMqsqlMAEKLQLQEQLQAETElcaEAEELRArLTAKKQELE--EICHDLEArveeee 928
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLI----IDEKRQQLERLRRERE---KAERYQA-LLKEKREYEgyELLKEKEA------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 929 ercqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEdqiimedqncklaKEKKLLEDRVAEFTTNL 1008
Cdd:TIGR02169 235 -----LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK-------------KIKDLGEEEQLRVKEKI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1009 MEEEEKSKSLaklknkhEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:TIGR02169 297 GELEAEIASL-------ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1089 LARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAqqelrskreqe 1168
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE----------- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1169 vsilkktLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELAnevkallqgkgdsehkrk 1248
Cdd:TIGR02169 439 -------LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA------------------ 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1249 KVEAQLQELQVKFSEGERVRTELADKVtklqvelDSVTGLLSQSDSKSSKLTKDF-SALESQLQ--------DTQELLQE 1319
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKASI-------QGVHGTVAQLGSVGERYATAIeVAAGNRLNnvvveddaVAKEAIEL 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1320 ENRQKLSLST-----KLKQMEDEKNSFREQ-----------------------------LEEEEEAKRNLEK-QIATLHA 1364
Cdd:TIGR02169 567 LKRRKAGRATflplnKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKyRMVTLEG 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1365 QVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKK-- 1442
Cdd:TIGR02169 647 ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKig 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1443 --QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQF--------RTEMEDLMSS 1512
Cdd:TIGR02169 720 eiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlsHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1513 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1593 EMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKENE 1672
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEI----PEEE 950
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1673 KKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1733
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1699 |
2.76e-27 |
|
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: 121.71 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 867 RLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQY----LQAEKKKMQ 942
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeLEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 943 QNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQiimEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLK 1022
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1023 NKHEamitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALArveeeaaqknma 1102
Cdd:TIGR02169 385 DELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL------------ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1103 lkKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELeDTLDSTAAQQELRSKREQEVSILKKTLEDEAKT 1182
Cdd:TIGR02169 449 --EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-AEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1183 HEAQIQEMRQKHSQAVEELADQLEQTKRVK--ATLEKAKQTLENERGELA-----NEVKA------LLQGKGDSEHKRKK 1249
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEVAAGNRLNNVVVEddAVAKEAIELLKRRKAGRAtflplNKMRDerrdlsILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1250 VEAQLQ-ELQVKFSEGERVRTELADKVTKLQVELDSVTgLLSQSDSKSSKLTKDFSALESQLQDTQELLQEEnrqkLSLS 1328
Cdd:TIGR02169 606 VEFDPKyEPAFKYVFGDTLVVEDIEAARRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL----QRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1329 TKLKQMEDEKNSFREQLeeeeeakRNLEKQIATLHAQVTDMKKKmedgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAY 1408
Cdd:TIGR02169 681 ERLEGLKRELSSLQSEL-------RRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1409 DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTisAKYAEERDRAEAEAREKETKALSLARALEEA 1488
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1489 MEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQatedaklrlevnlqamkaq 1568
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------- 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1569 ferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIdTANKNREEAIKQLRKLQAQMK 1648
Cdd:TIGR02169 886 ---DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQ 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1649 DCMRELDD-----TRASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1699
Cdd:TIGR02169 962 RVEEEIRAlepvnMLAIQeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1082-1910 |
3.42e-27 |
|
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: 121.33 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1082 EEELQAALARVEEeaaqknmALKKIRELETQISELQEDLESERASRNKAEKQKrdlgeeleALKTELEDTlDSTAAQQEL 1161
Cdd:TIGR02169 169 DRKKEKALEELEE-------VEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREY-EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1162 RSKREQEVSILKKTleDEAKTHEAQIQEMRQKHSQAVEELADQLEQ-TKRVKATLEKAKQTLENERGELANEVKALLQGK 1240
Cdd:TIGR02169 233 EALERQKEAIERQL--ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1241 GDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1321 NRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQR 1400
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1401 LEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQ-------LLAEEKTISAKYAEERD-----RAE 1468
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIEvaagnRLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1469 AEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQV-------EEMK 1538
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDgviGFAVDLVEFDPKYEPAFKYVfgdtlvvEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1539 TQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMD 1618
Cdd:TIGR02169 631 AARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1619 LKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQ 1698
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1699 AQ-QERDELADEIAnssgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDrlKKANLQIDQINTDlnlershAQKNE 1777
Cdd:TIGR02169 791 SRiPEIQAELSKLE----------EEVSRIEARLREIEQKLNRLTLEKEYLEK--EIQELQEQRIDLK-------EQIKS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1778 NARQQlerqnKELKAKLQEMESAVKSKykasiaalEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRN 1857
Cdd:TIGR02169 852 IEKEI-----ENLNGKKEELEEELEEL--------EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1858 AEQFKDQADKASTRLKQLKRQLEEAEEEAQrANASRRKLQRELEDATETADAM 1910
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1302-1925 |
1.05e-25 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 116.43 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1302 DFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ-------VTDMKKKME 1374
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARkqeleeiLHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1375 DGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEek 1454
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1455 tISAKYAEErdraeaearEKETKALSLARALEEAMEQKAElERLNKQfrtemedlmsskddvGKSVHELEKSKRALEQQV 1534
Cdd:pfam01576 164 -FTSNLAEE---------EEKAKSLSKLKNKHEAMISDLE-ERLKKE---------------EKGRQELEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1535 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKK 1614
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1615 LEMDLK----DLEAHIDTANKNREEAIKQLRKLqAQMKDCMREldDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:pfam01576 297 LGEELEalktELEDTLDTTAAQQELRSKREQEV-TELKKALEE--ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1691 AAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLER 1770
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1771 SHAQKNENARQQLERQNKELKAKLQEmESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQ 1850
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1851 VEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1925
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFD 607
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1252-1921 |
1.06e-25 |
|
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: 116.31 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1252 AQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKL 1331
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1332 KQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKL 1411
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1412 EKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTisAKYAEERDRAEAEAREKETKALSLARALEEAMEQ 1491
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1492 KAELERLNKQFRTEMEDLMSSKDDVGKSVHELE---KSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQA-MKA 1567
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1568 QFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANK---------------- 1631
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvd 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1632 NREEAIKQLRKLQAQMKdcMRELDDTRASREEILAQA---------------KENEKKLKSMEAEMIQLQEELAAAERAK 1696
Cdd:TIGR02168 630 DLDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1697 RQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELeeeqgntELINDRLKKANLQIDQINTDLNLERSHAQKN 1776
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-------AQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1777 ENARQQLERQNKELKAKLQEMESAVKSKyKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERR 1856
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1857 NAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-705 |
1.86e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 115.23 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 101 LKERYYSGLIYTYSGLFCV-VINPYKNL------PIYSEEIVEMYKGKKRHE--MPPHIYAI------------------ 153
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 154 --TDTAYRSMMQDReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------------------SSHKS---- 200
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKStiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 201 ---------------------------------------------------------KKDQGELERQL------------ 211
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 212 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KEERTFHI 276
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 277 FYYLLSGAGEH-----LKTDLLLEPYN--KYRFLSNGHVTIPG--------QQDKDMFQETMEAMRIMGIPEDEQMGLLR 341
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 342 VISGVLQLGNIAFKKERNTDQASMPDN---TAAQKVSHLLGI-NVTDFTRGILTPRIKV--GRDYVQKAQTKEQADFAIE 415
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 416 ALAKATYERMFRWLVLRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLqql 479
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 480 fnhtmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIEKPAGPPGILALLDEECWFPKAT----------DKSF 542
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLF 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 543 VEKVVQEQGThpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 611
Cdd:cd14894 628 VRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 612 WKDVDRiIGLD-----QVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMatlrntnPNFVRCIIPNHEKKAGKLDPH 686
Cdd:cd14894 706 LNESSQ-LGWSpntnrSMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNND 776
|
810
....*....|....*....
gi 74180985 687 LVLDQLRCNGVLEGIRICR 705
Cdd:cd14894 777 LVEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1351-1923 |
1.08e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1351 AKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLD 1430
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1431 HQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLM 1510
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1511 SSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrDEQSEEKKKQLVRQ 1590
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE--EEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1591 VREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAqmkdCMRELDDTRASREEILAQAKE 1670
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA----VAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1671 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIND 1750
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1751 RLkkanlqidqintdlnlershAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQldnetKER 1830
Cdd:COG1196 627 LV--------------------AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-----AEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1831 QAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET---- 1906
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppd 761
|
570
....*....|....*..
gi 74180985 1907 ADAMNREVSSLKNKLRR 1923
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1202-1922 |
2.09e-24 |
|
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: 112.07 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1202 ADQLEQTKRVKATLEKAKQTLE-NERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQV 1280
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1281 ELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEeeeeakrNLEKQIA 1360
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1361 TLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLE 1440
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1441 KKqkKFDQLLAEEKTISAKYAEERDRAEAEareKETKALSLARALEEAMEQKAELERLNKQFRTeMEDLMSSKDDVGKSV 1520
Cdd:TIGR02168 435 LK--ELQAELEELEEELEELQEELERLEEA---LEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1521 HELEKSKRALEQQVEEMKTQLE-----ELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD------EQSEEKKKQLVR 1589
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1590 QVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANkNREEAIKQLRKLQAQMKdcMRELDDTRASREEILAQA- 1668
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1669 --------------KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQL 1734
Cdd:TIGR02168 666 aktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1735 EEeleeeqgntelindrlkkanlQIDQIntDLNLERSHAQKNEnARQQLERQNKELKAKLQEMESavkskykasiaaLEA 1814
Cdd:TIGR02168 746 EE---------------------RIAQL--SKELTELEAEIEE-LEERLEEAEEELAEAEAEIEE------------LEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1815 KIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRR 1894
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
730 740
....*....|....*....|....*...
gi 74180985 1895 KLQRELEDATETADAMNREVSSLKNKLR 1922
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELE 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1198-1839 |
6.60e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.41 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1198 VEELADQLEQTKRVKAtLEKAKQTLENErgELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTK 1277
Cdd:COG1196 202 LEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1278 LQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEK 1357
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1358 QIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVS 1437
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1438 NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELErlnkqfrtEMEDLMSSKDDVG 1517
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL--------EAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1518 KSVHELEKSKRaLEQQVEEMKTQLEELEDELQATEDAKLRLEVNlqamkaqfERDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG1196 511 KAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1598 LEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1677
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1678 MEAEmiQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANL 1757
Cdd:COG1196 662 LTGG--SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1758 QIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMES----------AVKSKY----------KASIAALEAKIa 1817
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllaieeyeELEERYdflseqredlEEARETLEEAI- 818
|
650 660
....*....|....*....|...
gi 74180985 1818 qleEQLDNETKER-QAASKQVRR 1839
Cdd:COG1196 819 ---EEIDRETRERfLETFDAVNE 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1413 |
3.43e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 848 LAKEAELT------KVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLE 921
Cdd:COG1196 205 LERQAEKAeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE----LE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 922 ARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRV 1001
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1002 AEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK 1081
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1082 EEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDST-AAQQE 1160
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALlLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1161 LRSKREQEVSILKKTLEDEAKTHE-AQIQEMRQKHSQAVEELADQLEQTKRVKATL-------EKAKQTLENERGELANE 1232
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkirARAALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1233 VKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQD 1312
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1313 TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQK 1392
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570 580
....*....|....*....|.
gi 74180985 1393 DLEGLSQRLEEKVAAYDKLEK 1413
Cdd:COG1196 761 DLEELERELERLEREIEALGP 781
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1037-1605 |
1.56e-21 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 102.43 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1037 RREEKQRQELEKTRRKLEG-DSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmALKKIRELETQISE 1115
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE----VLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1116 LQEDLESERASRNKAEKQKRDLGEELEALK---TELEDTLDSTAAQQELRSKREQEVSILKKTLEDEakthEAQIQEMRQ 1192
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDR----DEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1193 KHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELA 1272
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1273 DKVTKLQVELDSVTGllsqsdsKSSKLTKDFSALESQLQDTQELLQE----ENRQKLSLSTKLKQMEDEknsfREQLEEe 1348
Cdd:PRK02224 412 DFLEELREERDELRE-------REAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEED----RERVEE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1349 eeakrnLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKdLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVD 1428
Cdd:PRK02224 480 ------LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1429 LDHQRQSVsnlEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKAL--SLARALEEAMEQKAELERLNKQFRTEM 1506
Cdd:PRK02224 553 AEEKREAA---AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiaDAEDEIERLREKREALAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1507 EDLMSSKDDVGKSVHEleKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER--DLQGRDEQSEEKK 1584
Cdd:PRK02224 630 AEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleELRERREALENRV 707
|
570 580
....*....|....*....|....*..
gi 74180985 1585 KQL------VRQVREMEAELEDERKQR 1605
Cdd:PRK02224 708 EALealydeAEELESMYGDLRAELRQR 734
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1010-1871 |
1.89e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.91 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1010 EEEEKSKSLAKLKNKHEamiTDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL-QAA 1088
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTE---TGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1089 LARVEEEAAQKNMALKKIreletQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQe 1168
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAE-----EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE- 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1169 vsilKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQtKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRK 1248
Cdd:PTZ00121 1242 ----AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1249 KVEAQ--LQELQVKFSEGERVRTEL--ADKVTKLQVELDSVTGLLSQSDSKSSKLTKdfsalESQLQDTQELLQEENRQK 1324
Cdd:PTZ00121 1317 ADEAKkkAEEAKKKADAAKKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-----EEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1325 LSLSTKLKQMEDEKNSfrEQLEEEEEAKRNLE--KQIATLHAQVTDMKKKMEDGvgclETAEEAKRRLQ--KDLEGLSQR 1400
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKA--DELKKAAAAKKKADeaKKKAEEKKKADEAKKKAEEA----KKADEAKKKAEeaKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1401 LEEKVAAYDKLEKTK-TRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLL-AEE--KTISAKYAEERDRAEAEAREKET 1476
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEakKADEAKKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1477 KALSLARALEEAmeQKAELERLNKQFRTEMEDlmssKDDVGKSVHELEKSKRALEQQVEEMKTQLEELE-DELQATEDAK 1555
Cdd:PTZ00121 1546 KKADELKKAEEL--KKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1556 LRLEvnlQAMKAQFER-DLQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAH---IDTANK 1631
Cdd:PTZ00121 1620 IKAE---ELKKAEEEKkKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1632 NREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKlksmEAEMIQLQEELAAAERAKRQAQQERDELADEIA 1711
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1712 NSSGKGALALEE--KRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLE------RSHAQKNENARQQL 1783
Cdd:PTZ00121 1772 EIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAikevadSKNMQLEEADAFEK 1851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1784 ERQNKELKAKLQEMESAVKSKYKASIAALEAKI--AQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVED-ERRNAEQ 1860
Cdd:PTZ00121 1852 HKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEyIKRDAEE 1931
|
890
....*....|.
gi 74180985 1861 FKDQADKASTR 1871
Cdd:PTZ00121 1932 TREEIIKISKK 1942
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
865-1717 |
2.18e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.53 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 865 ENRLTEMeTMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQEL---EEICHDLEARVEEEEERCQYLQAEKKKM 941
Cdd:PTZ00121 1086 DNRADEA-TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 942 QQNIQELEEQLEEEESARQKLQLEKVTteaKLKKLEEDQIIMEDQncKLAKEKKLLEDRVAEfttnlmeEEEKSKSLAKL 1021
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAAR--KAEEERKAEEARKAE-------DAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1022 KnkheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIaelKMQLAKKEEELQAALARVEEEAAQKNM 1101
Cdd:PTZ00121 1233 E----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1102 ALKKIRELETQIS------ELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKT 1175
Cdd:PTZ00121 1300 EKKKADEAKKKAEeakkadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1176 LED-EAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGelANEVKALLQGKGDSEHKRKKVEAQL 1254
Cdd:PTZ00121 1380 ADAaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1255 QELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDfsalESQLQDTQELLQEENRQKlslSTKLKQM 1334
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKK---ADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1335 EDEKNSFR----EQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEE----KVA 1406
Cdd:PTZ00121 1531 EEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1407 AYDKLEKTKTRlQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETkalslARALE 1486
Cdd:PTZ00121 1611 EAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-----AKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1487 EAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEledELQATEDAKlrlevnlqamK 1566
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE---DKKKAEEAK----------K 1751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1567 AQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEmDLKDLEAHIDTANK--------NREEAIK 1638
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK-DIFDNFANIIEGGKegnlvindSKEMEDS 1830
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1639 QLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAG 1909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1420 |
1.84e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 838 LNSIRHEDELLAKEAELTKVREKHLAAENRLTE--METMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEE 915
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 916 ichdLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKK 995
Cdd:COG1196 314 ----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 996 LLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELK 1075
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1076 MQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRN---------KAEKQKRDLGEELEALKT 1146
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligVEAAYEAALEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1147 EL--EDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLEN 1224
Cdd:COG1196 550 NIvvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1225 ERGELANEVKALLqgkgdsEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSvtgLLSQSDSKSSKLTKDFS 1304
Cdd:COG1196 630 ARLEAALRRAVTL------AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE---LAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1305 ALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMedgvgcletaE 1384
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL----------E 770
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 74180985 1385 EAKRRLQK----------DLEGLSQRLEEKVAAYDKLEKTKTRLQQ 1420
Cdd:COG1196 771 RLEREIEAlgpvnllaieEYEELEERYDFLSEQREDLEEARETLEE 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1591 |
2.67e-19 |
|
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: 95.52 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 846 ELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVE 925
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 926 EEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFT 1005
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1006 TNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA---ELKMQLAKKE 1082
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1083 EELQAALarveeEAAQKNMALKKIRELETQISELQEDLESERASR------NKAEKQKRDLGEELE-------------- 1142
Cdd:TIGR02169 535 ERYATAI-----EVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEdgvigfavdlvefd 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1143 -----ALKTELEDTLdstaAQQELRSKREQEVSILKKTLEDEAKTHEAQI----QEMRQKHSQAVEELAdQLEQTKRVKA 1213
Cdd:TIGR02169 610 pkyepAFKYVFGDTL----VVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPA-ELQRLRERLE 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1214 TLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSD 1293
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1294 SKSSKLTKDFSALESQLQDTQELLQEEnrqklslstKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQvtdmkkkm 1373
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHS---------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE-------- 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1374 edgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEE 1453
Cdd:TIGR02169 828 ------KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1454 KtisakyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkDDVGKSVHELEKSKRALE-- 1531
Cdd:TIGR02169 902 E-------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEpv 973
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1532 -----QQVEEMKTQLEELEDELqatedAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQV 1591
Cdd:TIGR02169 974 nmlaiQEYEEVLKRLDELKEKR-----AKLEEE----------RKAILERIEEYEKKKREVFMEA 1023
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1106-1932 |
3.25e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 95.19 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1106 IRELETQISELQEDLESeraSRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEA 1185
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1186 QiqemRQKHSQAVEELADQLEQTKRVKATLEKAKQTLEN--ERGELANEVKALLQGKGDSEHKRK---KVEAQLQELQVK 1260
Cdd:pfam15921 157 A----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilVDFEEASGKKIYEHDSMSTMHFRSlgsAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1261 FS-----------EGERVRTELADKVTKL-QVELDSVTGLLSQSDSKSSKLTKDFSALESQ---LQDTQELLQEENRQKL 1325
Cdd:pfam15921 233 ISylkgrifpvedQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1326 SLStkLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTdmkkkmedgvgcLETAEEAKRRLQKDleglsQRLEEKV 1405
Cdd:pfam15921 313 SMY--MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV------------LANSELTEARTERD-----QFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1406 AAYDKLEKTKTRLqqelddllvdldHQRQSVSNLEKKQKK--FDQLLAEEKTISAKYAEERDRaEAEAREKETKALSLAR 1483
Cdd:pfam15921 374 NLDDQLQKLLADL------------HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1484 ALEEAMEQK-AELERLNKQFR---TEMEDLMSSKDDVGKSVHELEKSKRALE---QQVEEMKTQLEELEDELQAT--EDA 1554
Cdd:pfam15921 441 ECQGQMERQmAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1555 KLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmamaarkkLEMDLKDLEAHIDTANKNRE 1634
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ----------IENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1635 EAIKqlrkLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSS 1714
Cdd:pfam15921 591 EKAQ----LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1715 GKGALALEEKRRLEARIaqlEEELEEEQGNTELINDRLKKANLQIDQI-NTDLNLERS--HAQKNENARQqlerqnKELK 1791
Cdd:pfam15921 667 NELNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSAQSELEQTrNTLKSMEGSdgHAMKVAMGMQ------KQIT 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1792 AKlqemesavkskyKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLL-------QVEDERRNAEQFKDQ 1864
Cdd:pfam15921 738 AK------------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmagELEVLRSQERRLKEK 805
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1865 ADKASTRLKQLKRQLEEAEEEAQR--ANASRRKLQRELeDATETADAMNREVSSLKNKLRRgdlPFVVTR 1932
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRqeQESVRLKLQHTL-DVKELQGPGYTSNSSMKPRLLQ---PASFTR 871
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1080-1710 |
3.63e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.75 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1080 KKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtLDSTAaqQ 1159
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELK--E 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1160 ELRSKREQevsilKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQ--TLENERGELANEVKALL 1237
Cdd:PRK03918 239 EIEELEKE-----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1238 QGKGDSEHKRKKVEAQLQELQVKFSEGErvrtELADKVTKLQVELDSVtgllsqsdSKSSKLTKDFSALESQLQDTQELL 1317
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL--------EERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1318 QEENRQKLSlsTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKK-KMEDGVGCLETAEEAKRRL----QK 1392
Cdd:PRK03918 382 TGLTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELleeyTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1393 DLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLlvdldhqrqsvSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1472
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKE-----------SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1473 EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1552
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1553 DAKLRLEVNLQAMKaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARK-----KLEMDLKDLEAHID 1627
Cdd:PRK03918 609 DAEKELEREEKELK-----KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1628 TANKNREEAIKQLRKLQaqmkdcmRELDDTRASREEIlaqakeneKKLKSMEAEMIQLQEELAAAE-RAKRQAQQERDEL 1706
Cdd:PRK03918 684 ELEKRREEIKKTLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEI 748
|
....
gi 74180985 1707 ADEI 1710
Cdd:PRK03918 749 ASEI 752
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
821-1611 |
4.37e-19 |
|
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: 94.75 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 821 RLRNWQWWRLFTKVKPLLNSIRH-EDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAE--KLQLQEQLQAET---E 894
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikDLGEEEQLRVKEkigE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 895 LCAEAEELRARLTAKKQELEeichDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK 974
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELE----DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 975 KLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERL-----RREEKQrQELEKT 1049
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneleeEKEDKA-LEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1050 RRKLEGDSTDLSD----------QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQED 1119
Cdd:TIGR02169 454 EWKLEQLAADLSKyeqelydlkeEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1120 LESERASRNKAekqkrdLGEELEALKteLEDTLDSTAAQQELRSKR------------EQEVSILKKTLEDEAKTHEAQI 1187
Cdd:TIGR02169 534 GERYATAIEVA------AGNRLNNVV--VEDDAVAKEAIELLKRRKagratflplnkmRDERRDLSILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1188 QEMRQKHSQAVEE-LADQLeqtkrVKATLEKAKQTLENER-----GELANEVKALLQG----KGDSEHKRKKvEAQLQEL 1257
Cdd:TIGR02169 606 VEFDPKYEPAFKYvFGDTL-----VVEDIEAARRLMGKYRmvtleGELFEKSGAMTGGsrapRGGILFSRSE-PAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1258 QVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDE 1337
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1338 KNSFREQLEEEEEAKRNLEKQIATLHAQVTDmkKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTR 1417
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1418 LQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1497
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1498 LNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQLEELEDELQATEDaklrleVNLQAMKaQFERDLQGRD 1577
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLD 989
|
810 820 830
....*....|....*....|....*....|....*
gi 74180985 1578 EQsEEKKKQLVRQVREMEAELED-ERKQRSMAMAA 1611
Cdd:TIGR02169 990 EL-KEKRAKLEEERKAILERIEEyEKKKREVFMEA 1023
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
960-1569 |
4.64e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 93.93 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 960 QKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAK--------------LKNKH 1025
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL---QAALARVEEEAAQKNMA 1102
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1103 L-------KKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV---SIL 1172
Cdd:TIGR04523 203 LsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnNKK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1173 KKTLEDEAKTHEAQIQEMRQKHSQaveeladqlEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKkvea 1252
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK---- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1253 qlqELQVKFSEGERVRTELADKVTKLQVeldsvtgLLSQSDSKSS---KLTKDFSALESQLQDTQELLQEENRQKLSLST 1329
Cdd:TIGR04523 350 ---ELTNSESENSEKQRELEEKQNEIEK-------LKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1330 KLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYD 1409
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1410 KLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLA--EEKTISAKYAEERDRAEAEAREKETKalslaraLEE 1487
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKE-------IEE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1488 AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1567
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
..
gi 74180985 1568 QF 1569
Cdd:TIGR04523 653 TI 654
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
961-1795 |
4.76e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.41 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 961 KLQLEKVTTEAKlKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEamitdleerlRREE 1040
Cdd:pfam15921 73 KEHIERVLEEYS-HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRES----------QSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEEEAAQK-----NMALKKIRELETQ 1112
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdSMSTMHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1113 ISELQEDLESERASrnkAEKQKRDLGEELEALKTELEDTLDSTAAQQELRskreqevsilkktLEDEAKTHEAQIQEMRQ 1192
Cdd:pfam15921 222 ISKILRELDTEISY---LKGRIFPVEDQLEALKSESQNKIELLLQQHQDR-------------IEQLISEHEVEITGLTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1193 KHSQAveeladqLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkgdsehkrkkvEAQLQELQVKFSEGERVrteLA 1272
Cdd:pfam15921 286 KASSA-------RSQANSIQSQLEIIQEQARNQNSMYMRQLSDL--------------ESTVSQLRSELREAKRM---YE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1273 DKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLqdtQELLQEENRQKLSLSTKLKQME-----DEKNSFREQLEE 1347
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADLHKREKELSLEKEQNKrlwdrDTGNSITIDHLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1348 EEEAKRNLEKQiaTLHAQVTDMKKKMEdgvGCLEtaeeakrRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQ---QELDD 1424
Cdd:pfam15921 419 RELDDRNMEVQ--RLEALLKAMKSECQ---GQME-------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRkvvEELTA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1425 LLVDLDHQRQSVSNLEKkqkkfdQLLAEEKTISAKYAE---ERDRAEAEARE-----KETKALSLARALEEAME-QKAEL 1495
Cdd:pfam15921 487 KKMTLESSERTVSDLTA------SLQEKERAIEATNAEitkLRSRVDLKLQElqhlkNEGDHLRNVQTECEALKlQMAEK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1496 ERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdELQATEDAKLrlevnlqamkaqfeRDLQG 1575
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDAKI--------------RELEA 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1576 RDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKN----REEAIKQLRKLQAQMKDCM 1651
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQ 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1652 RELDDTRASreeilaqakenekkLKSMEAE-------MIQLQEELaAAERAKRQAQQERDELADE-IANSSGKGALALEE 1723
Cdd:pfam15921 706 SELEQTRNT--------------LKSMEGSdghamkvAMGMQKQI-TAKRGQIDALQSKIQFLEEaMTNANKEKHFLKEE 770
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1724 KRRLEARIAQLEEELEEEQGNTELIndRLKKANLQIDQINTDLNLERSHAQKNEnARQQLERQNKE-LKAKLQ 1795
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVL--RSQERRLKEKVANMEVALDKASLQFAE-CQDIIQRQEQEsVRLKLQ 840
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1591-1909 |
9.46e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.46 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1591 VREMEAELEDERKQRSMAMAARKkLEMDLKDLEAhidtanknrEEAIKQLRKLQAQmkdcmreLDDTRASREEILAQAKE 1670
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRE-LKEELKELEA---------ELLLLKLRELEAE-------LEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1671 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIND 1750
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1751 RLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKyKASIAALEAKIAQLEEQLDNETKER 1830
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1831 QAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1548 |
2.18e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 857 VREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQY 933
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 934 LQAEKKKMQQniqeleeqleeEESARQKLQLEKVTTEAKLKKLEEDqiimedqncklakeKKLLEDRVAEFTTNLMEEEE 1013
Cdd:PRK03918 226 LEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEK--------------IRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1014 KSKSLAKLKNKHEAMITdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVE 1093
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1094 EEAAQKNMALKKIRELEtqiselqedleserasrnkaEKQKRDLGEELEALKTELEdtldstaaqqelrskreqEVSILK 1173
Cdd:PRK03918 359 ERHELYEEAKAKKEELE--------------------RLKKRLTGLTPEKLEKELE------------------ELEKAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1174 KTLEDEAKTHEAQIQEMRQKhsqaVEELADQLEQTKRVKATLEKAKQTL-ENERGELANEVKALLqgkgdsehkrKKVEA 1252
Cdd:PRK03918 401 EEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAEL----------KRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1253 QLQELQVKFSEGERVRTELaDKVTKLQVELDSVTGLLSQSDSKSSKLTK-DFSALESQLQDTQELLQEENRQKLSLSTKL 1331
Cdd:PRK03918 467 ELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1332 KQMEdEKNSFREQLEEEEEAKRNLEKQIATLHaqvtdmKKKMEDGVGCLEtaeeakrrlqkDLEGLSQRLEEKVAAYDKL 1411
Cdd:PRK03918 546 KELE-KLEELKKKLAELEKKLDELEEELAELL------KELEELGFESVE-----------ELEERLKELEPFYNEYLEL 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1412 EKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEErdraeaEAREKETKALSLARALEEAMEQ 1491
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRAE 681
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1492 KAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEqQVEEMKTQLEELEDEL 1548
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
997-1576 |
3.07e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 997 LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST---DLSDQIAELQAQIAE 1073
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1074 LkmqlakkEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQ--------------KRDLGE 1139
Cdd:PRK02224 291 L-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslredaddleerAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1140 ELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEakthEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAK 1219
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA----PVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1220 QTL-ENERGELANEVKALLQGKGDSEHkrkkVEAqLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLlsqsdsksSK 1298
Cdd:PRK02224 440 ERVeEAEALLEAGKCPECGQPVEGSPH----VET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--------VE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1299 LTKDFSALESQLQDTQELLqeenrqklslstklkqmEDEKNSFREQleeeeeakrnlEKQIATLHAQVTDMKKKMEDGVG 1378
Cdd:PRK02224 507 AEDRIERLEERREDLEELI-----------------AERRETIEEK-----------RERAEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1379 CLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLqqelddllVDLDHQRQSVSNLEKKQKKFDQLLAEEKTisa 1458
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL--------AAIADAEDEIERLREKREALAELNDERRE--- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1459 KYAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgksvheLEKSKRALEQQVEEmk 1538
Cdd:PRK02224 628 RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQAEIGAVENELEE-- 692
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 74180985 1539 tqLEELEDELQATEDAKLRLEV------NLQAMKAQFERDLQGR 1576
Cdd:PRK02224 693 --LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
983-1637 |
4.56e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 90.85 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 983 MEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD 1062
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELE 1142
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1143 ALKTELEDTLDSTAAQQELRSK---REQEVSILKKTLED----------EAKTHEAQIQEMRQKHSQAVEELAD---QLE 1206
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQiseLKKQNNQLKDNIEKkqqeinekttEISNTQTQLNQLKDEQNKIKKQLSEkqkELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1207 QTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEhkRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELdsvT 1286
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSE--LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---T 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1287 GLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENR---QKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLH 1363
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1364 AQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAA----YDKLEKTKTRLQQELDDLLVDLDHQRQSVSNL 1439
Cdd:TIGR04523 433 ETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1440 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARAL----------------EEAMEQKAELERLNKQFR 1503
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeideknkeiEELKQTQKSLKKKQEEKQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1504 TEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF-------------- 1569
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIkeirnkwpeiikki 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1570 -----------ERDLQGRDEQSEEKKKQLVRQVREME-AELEDERKQRSMAMaarKKLEMDLKDLEAHIDTANKNREEAI 1637
Cdd:TIGR04523 669 kesktkiddiiELMKDWLKELSLHYKKYITRMIRIKDlPKLEEKYKEIEKEL---KKLDEFSKELENIIKNFNKKFDDAF 745
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1198-1922 |
6.71e-18 |
|
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: 90.90 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1198 VEELADQLEQTKRVKATLEKAkQTLENERGELanEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTK 1277
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1278 LQVELDSVTGLLSQ-SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLE 1356
Cdd:TIGR02169 270 IEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1357 KQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSV 1436
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1437 SNLEKKQKKFDqllaeektisakyaEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDDV 1516
Cdd:TIGR02169 430 AGIEAKINELE--------------EEKEDKALEIKKQEWK-------LEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1517 GKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGR-------DEQSEEKKKQLVR 1589
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvveDDAVAKEAIELLK 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1590 QVREMEAELEDERKQRSMAMAARKKLE-------MDLKDLEAHI---------DTANKNREEAIKQLrKLQAQMKDCMRE 1653
Cdd:TIGR02169 569 RRKAGRATFLPLNKMRDERRDLSILSEdgvigfaVDLVEFDPKYepafkyvfgDTLVVEDIEAARRL-MGKYRMVTLEGE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1654 LDD--------TRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKR 1725
Cdd:TIGR02169 648 LFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1726 RLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLnlershaQKNENARQQLERQNKELKAKLQEMEsAVKSKY 1805
Cdd:TIGR02169 720 EIEKEI--------------EQLEQEEEKLKERLEELEEDL-------SSLEQEIENVKSELKELEARIEELE-EDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1806 KASIAALEAKIA-----QLEEQLDNETKERQAASKQVRRTEKKLKDVLL---QVEDERRNAEQ----FKDQADKASTRLK 1873
Cdd:TIGR02169 778 EEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEqridLKEQIKSIEKEIE 857
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 74180985 1874 QLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1922
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1520-1909 |
9.50e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1520 VHELEKSKRALEQQVE------EMKTQLEELEDELQATEDAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:COG1196 195 LGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAE----------LEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1594 MEAELEDERKQrsmamaarkklemdLKDLEAHIDTANKNREEAIKQLRKLQaqmkdcmRELDDTRASREEILAQAKENEK 1673
Cdd:COG1196 265 LEAELEELRLE--------------LEELELELEEAQAEEYELLAELARLE-------QDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1674 KLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDRLK 1753
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---------AEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1754 KANLQiDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAvkskyKASIAALEAKIAQLEEQLDNETKERQAA 1833
Cdd:COG1196 395 AAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1834 SKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQ-LKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
992-1866 |
9.59e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.42 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 992 KEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQE--------------LEKTRRKLEGDS 1057
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDL 1137
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1138 GEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEdeakTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEK 1217
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE----AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1218 AKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSS 1297
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1298 KLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGV 1377
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1378 GCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTIS 1457
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1458 AKYAEERDRAEAEAR--EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVE 1535
Cdd:pfam02463 629 LKDTELTKLKESAKAkeSGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1536 EMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKL 1615
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1616 EMDLKDLE-AHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAA-AE 1693
Cdd:pfam02463 789 EEEKEEKLkAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKeEL 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1694 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1773
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1774 QKNENARQQLERQNKELKAKLQEMESaVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVED 1853
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGK-VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFV 1027
|
890
....*....|...
gi 74180985 1854 ERRNAEQFKDQAD 1866
Cdd:pfam02463 1028 SINKGWNKVFFYL 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1238 |
4.80e-17 |
|
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: 88.19 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 847 LLAKEAELTKVREKhlaaenrlteMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELeeicHDLEARVEE 926
Cdd:TIGR02168 672 ILERRREIEELEEK----------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI----SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 927 EEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTT 1006
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1007 NLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQ 1086
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1087 AALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLgeeLEALKTELEDTLDSTAAQQELRSKRE 1166
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDE 967
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1167 QEvsilkktLEDEAKTHEAQIQEMRQKHSQAVEELADQ---LEQTKRVKATLEKAKQTLENERGELANEVKALLQ 1238
Cdd:TIGR02168 968 EE-------ARRRLKRLENKIKELGPVNLAAIEEYEELkerYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1029-1557 |
8.03e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.28 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1029 ITDLEERLRREEKQRQELEKTRRKLEgDSTDLSDQIAELQAQIAELKMQLAKKE-EELQAALARVEEEAAQknmalkkir 1107
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELAR--------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1108 eLETQISELQEDLESERASRNKAEKQKRDL-GEELEALKTELEDtldstaAQQELRsKREQEVSILKKTLED---EAKTH 1183
Cdd:COG4913 307 -LEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIER------LERELE-ERERRRARLEALLAAlglPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1184 EAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGK----GDSEHKRKKVEAQLQE--- 1256
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLdea 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1257 --------LQVKFSE-------------------------------------GERVRTELADKVTK----LQVELDSVTG 1287
Cdd:COG4913 459 elpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlRGRLVYERVRTGLPdperPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1288 LLSQSDSK-----SSKLTKDFSAL----ESQLQD-----TQE----------------------LLQEENRQKL-SLSTK 1330
Cdd:COG4913 539 KLDFKPHPfrawlEAELGRRFDYVcvdsPEELRRhpraiTRAgqvkgngtrhekddrrrirsryVLGFDNRAKLaALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1331 LKQMEDEKNSFREQLEEEEEAKRNLEKQ----------------IATLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDL 1394
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELER----LDASSDDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1395 EGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEK----TISAKYAEERDRAEAE 1470
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaaaLGDAVERELRENLEER 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1471 AREKETKALSLARALEEAMEQkaelerLNKQFRTEMEDLMSSKDDVGKSVHELEK-SKRALEQQVEEMKTQLEELEDELQ 1549
Cdd:COG4913 775 IDALRARLNRAEEELERAMRA------FNREWPAETADLDADLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFV 848
|
....*...
gi 74180985 1550 ATEDAKLR 1557
Cdd:COG4913 849 ADLLSKLR 856
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1682 |
1.67e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 86.25 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 845 DELLAKEAELTKVREKHLAAE-------NRLTEMETMQSQLMaeklQLQEQLQAETELCAEAEELRARLTAKK------- 910
Cdd:TIGR00606 224 DQITSKEAQLESSREIVKSYEneldplkNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMekvfqgt 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 911 -QELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCK 989
Cdd:TIGR00606 300 dEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 990 LAKEKKLLEDRVAEFTTNLMEE--EEKSKSLAKLKNkheamitDLEERLRREEKQRQELEKTR----RKLEGDSTDLSDQ 1063
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIErqEDEAKTAAQLCA-------DLQSKERLKQEQADEIRDEKkglgRTIELKKEILEKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1064 IAELQAQIAELKM------QLAKKEEELQAALARVEEEAAQKNMALKKIRELETQiselQEDLESERASRNKAEKQKrDL 1137
Cdd:TIGR00606 453 QEELKFVIKELQQlegssdRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQ----NEKADLDRKLRKLDQEME-QL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1138 GEELEALKTELEDTLDSTAAQQELRSKREQEVSIL---------KKTLEDEAKTHEAQIQEMRQKHSQAVEELAdQLEQT 1208
Cdd:TIGR00606 528 NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA-SLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1209 KRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVE---AQLQELQVKFSEGERVRTELADKVTKLQVELDSV 1285
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEkssKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1286 TGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ 1365
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1366 VTDMKKKMEDGVGCLETAEEAK------RRLQKDLEGLSQRLEEKVAAYD--KLEKTKTRLQQELDDLLVDLDHQRQSVS 1437
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1438 NLEK----KQKKFDQL------LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEME 1507
Cdd:TIGR00606 847 LNRKliqdQQEQIQHLksktneLKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1508 DLMSSKDDVGKSVH-ELEKSKRALEQQVEEMKTQLEELEDelqATEDAKLRLEVNLQAMKAQFerdlqgrdEQSEEKKKQ 1586
Cdd:TIGR00606 927 ELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEK 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1587 LVRQVREMEAELEDERKQRSMAM--AARKKLEMDLKDLEAHIDTANKNREEaiKQLRKLQAQMKDCMRELDDTRASREEI 1664
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
890
....*....|....*...
gi 74180985 1665 LAQAKENEKKLKSMEAEM 1682
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKEL 1091
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1442 |
4.65e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.19 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 849 AKEAELTKVREKHLAAENRLTEMETMQSQL---MAEKLQLQEQLQAETELCAEAEELRARLTAKKQ------ELEEICHD 919
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadeakkKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 920 LEARVEEEEERCQ---YLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEEDQIIMEDQNCKLAKEKKL 996
Cdd:PTZ00121 1434 DEAKKKAEEAKKAdeaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 997 LEDRVAEFTTNL-----MEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRrklEGDSTDLSDQIAELQAQI 1071
Cdd:PTZ00121 1513 DEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---AEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1072 AELK----MQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESErasRNKAEKQKRDlgEELEALKTE 1147
Cdd:PTZ00121 1590 EEARieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKA--EEENKIKAA 1664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1148 LEdtldstaAQQELRSKREQEVsiLKKTLEDEAKTHEAQIQEMRQKhsQAVEELADQLEQTKRVKATLEKAkqtlENERG 1227
Cdd:PTZ00121 1665 EE-------AKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKA----EEENK 1729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1228 ELANEVKallqgKGDSEHKRKKVEAQLQE------LQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTK 1301
Cdd:PTZ00121 1730 IKAEEAK-----KEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1302 DFSALESQLQDTQELLQeeNRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLE 1381
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVI--NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1382 TAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDhQRQSVSNLEKK 1442
Cdd:PTZ00121 1883 EIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEE-TREEIIKISKK 1942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-1922 |
5.47e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1612 RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMR------ELDDTRAS-----REEILAQAKENEKKLKSMEA 1680
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERyrelkeELKELEAEllllkLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1681 EMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQID 1760
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1761 QINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKyKASIAALEAKIAQLEEQLDNETKERQAASKQVRRT 1840
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1841 EKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
..
gi 74180985 1921 LR 1922
Cdd:COG1196 493 LL 494
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
965-1707 |
7.21e-16 |
|
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: 84.25 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 965 EKVTTEAKLKKLEEDQII--MEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSK--SLAKLKNKHEAMITDLEERLRREE 1040
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLalMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYheRKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1041 KQRQELEKT--RRKLEGDSTDLSDQIAELQAQIAELkmQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQE 1118
Cdd:TIGR00618 244 YLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1119 DLESERASRNKAEKQKRDLGEELEALKTELedtldstaaQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQkhsqav 1198
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ------ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1199 eeladQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKL 1278
Cdd:TIGR00618 387 -----QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1279 QveldsvtgllsqsdskssKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEeeakrNLEKQ 1358
Cdd:TIGR00618 462 Q------------------ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP-----NPARQ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1359 IATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSN 1438
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1439 LEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLAraLEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGK 1518
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRVLPKELLA 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1519 SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDA--KLRLEVN-LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1595
Cdd:TIGR00618 677 SRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHieEYDREFNeIENASSSLGSDLAAREDALNQSLKELMHQARTVL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1596 AELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEK-K 1674
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsR 836
|
730 740 750
....*....|....*....|....*....|...
gi 74180985 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1380-1879 |
9.43e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1380 LETAEEAKRRLQkDLEGLSQRLEEKVAAYDKLEKTKTRL-----QQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLL 1450
Cdd:COG4913 244 LEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAElerlEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1451 AEEKTISAKYAE-----------ERDRAEAEAREKETKALSLARALEeAMEQKAELERlnKQFRTEMEDLMSSKDDVGKS 1519
Cdd:COG4913 323 EELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLA-ALGLPLPASA--EEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL--------------QGRDEQSE---- 1581
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALgldeaelpfvgeliEVRPEEERwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1582 ----------------------------EKKKQLVR--QVREMEAELEDER-KQRSMAM-------AARKKLEMDLKDLE 1623
Cdd:COG4913 480 iervlggfaltllvppehyaaalrwvnrLHLRGRLVyeRVRTGLPDPERPRlDPDSLAGkldfkphPFRAWLEAELGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1624 AHIDTANknrEEAIKQLRK---LQAQMKD--CMRELDDTRASREE-ILAQakENEKKLKSMEAEMIQLQEELAAAERAKR 1697
Cdd:COG4913 560 DYVCVDS---PEELRRHPRaitRAGQVKGngTRHEKDDRRRIRSRyVLGF--DNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1698 QAQQERDeladeianssgkgalALEEKRRLEARIAQLEEELeeeqgntelinDRLKKANLQIDQintdLNLERSHAQKNE 1777
Cdd:COG4913 635 ALEAELD---------------ALQERREALQRLAEYSWDE-----------IDVASAEREIAE----LEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1778 NARQQLERQNKELKAKLQEMESAVKSKYKAsIAALEAKIAQLEEQLDNETKERQAASKQVR-----RTEKKLKDVLLQvE 1852
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGD-A 762
|
570 580
....*....|....*....|....*..
gi 74180985 1853 DERRNAEQFKDQADKASTRLKQLKRQL 1879
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEEL 789
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1006-1730 |
1.22e-15 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 83.35 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1006 TNLMEEEEKSKSL-AKLKNKHEAmITDLEERLRREEKQRQELEKTRR-KLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:pfam12128 244 TKLQQEFNTLESAeLRLSHLHFG-YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1084 ELQAA--------LARVEEEAAQKNMALKKIRELETQ-------------ISELQEDLESERASRNKAE----KQKRD-L 1137
Cdd:pfam12128 323 ELEALedqhgaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRDiagiKDKLAkI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1138 GEELEALKTELEDTLDstAAQQELRSKREQEvsilKKTLEDEAKTHEAQIQEM--RQKHSQAVEELADQLEQTkrvKATL 1215
Cdd:pfam12128 403 REARDRQLAVAEDDLQ--ALESELREQLEAG----KLEFNEEEYRLKSRLGELklRLNQATATPELLLQLENF---DERI 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1216 EKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSK 1295
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1296 --SSKLTK----DFSALESQLQDTQEL----LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ 1365
Cdd:pfam12128 554 viSPELLHrtdlDPEVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1366 VTDMKKKMEDGVGCLETAEEAKRRLQkdleglsqrlEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSvsnLEKKQKK 1445
Cdd:pfam12128 634 LEKASREETFARTALKNARLDLRRLF----------DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1446 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMedlmsskddvgksvheleK 1525
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS-GAKAELKALETWYKRDL------------------A 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1526 SKRALEQQVEEMKTQLEELEDELQatedaklRLEVNLQAMkAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkqr 1605
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIE-------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISE----- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1606 smamaarkkLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDtRASREEILAQAKENEKKLKSMEAEMIQL 1685
Cdd:pfam12128 826 ---------LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC-EMSKLATLKEDANSEQAQGSIGERLAQL 895
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 74180985 1686 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1730
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDH 940
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
855-1717 |
3.20e-15 |
|
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: 81.94 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 855 TKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYL 934
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEK 1014
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1015 SKSLAKLKNKHEamITDLEERLRREEKQRQELEKTR-----------RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:pfam02463 325 KAEKELKKEKEE--IEELEKELKELEIKREAEEEEEeeleklqekleQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1084 ELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASrnkaEKQKRDLGEELEALKTELEDTLDSTAAQQELRS 1163
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK----LTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1164 KREQEVSILKKtLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQG---K 1240
Cdd:pfam02463 479 LVKLQEQLELL-LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVsatA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1241 GDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1321 NRQKLSLSTKLKQMEDEKnsfREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEdgvgcLETAEEAKRRLQKDLEGLSQR 1400
Cdd:pfam02463 638 KESAKAKESGLRKGVSLE---EGLAEKSEVKASLSELTKELLEIQELQEKAESE-----LAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1401 LEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQ-------LLAEEKTISAKYAEERDRAEAEARE 1473
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLkkeekeeEKSELSLKEKELAEEREKTEKLKVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1474 KETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATED 1553
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1554 AKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMaaRKKLEMDLKDLEAHIDTANKNR 1633
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE--EAEILLKYEEEPEELLLEEADE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1634 EEAIKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1712
Cdd:pfam02463 948 KEKEENNKEEEEERNKRLlLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFV 1027
|
....*
gi 74180985 1713 SSGKG 1717
Cdd:pfam02463 1028 SINKG 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1102-1920 |
5.08e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1102 ALKKIRELETQISELQEDLESERASRNKAE---KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLED 1178
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEearKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1179 EAKTHEAQIQEMRQKhsqavEELADQLEQTKRVKAtLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:PTZ00121 1163 ARKAEEARKAEDAKK-----AEAARKAEEVRKAEE-LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1259 VKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKdfsalesqlqdTQELLQEENRQKlslSTKLKQMEDEK 1338
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK-----------ADELKKAEEKKK---ADEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1339 NSfrEQLEEEEEAKRNLEkqiatlhaqvtDMKKKMEDGVgclETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRL 1418
Cdd:PTZ00121 1303 KA--DEAKKKAEEAKKAD-----------EAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1419 QQELDDLLVDLDHQRQSVSNLEKKQKkfdqllAEEktisAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERL 1498
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKK------ADE----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1499 NKQFRTEME-DLMSSKDDVGKSVHELEKsKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD 1577
Cdd:PTZ00121 1437 KKKAEEAKKaDEAKKKAEEAKKAEEAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQmkdcmrELDDT 1657
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1658 RASREEILAQAKENEKKLKSmeaemiqlqEELAAAERAKRQAQQERDELADEIANSSGKGALAlEEKRRLEariaqleee 1737
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKA---------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAE--------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1738 leeeqgntelindRLKKANlqidqintdlnlershaQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAAL-EAKI 1816
Cdd:PTZ00121 1651 -------------ELKKAE-----------------EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkEAEE 1700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1817 AQLEEQLDNETKERQAASKQVRRTEKKLKdvlLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKL 1896
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
810 820
....*....|....*....|....
gi 74180985 1897 QRELEDATETADAMNREVSSLKNK 1920
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
850-1393 |
1.06e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 850 KEAELTKVREKHLAAENRLTEMETMQSQLmaeKLQLQEQLQAEtELCAEAEELRARLTAKKQELEEICHDLEARVEEEEE 929
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 930 RCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEEDQIIMEDQNCKLAKEKKLLEdrvaefttnLM 1009
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADE---------AK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelEKTRRKLEgdstdlsdqiAELQAQIAELKMQLAKKEEELQaal 1089
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAE----------EAKKADEAKKKAEEAKKADEAK--- 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1090 aRVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRdlgEELEALKTELEDTLDSTAAQQELRSKREQEV 1169
Cdd:PTZ00121 1490 -KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1170 SILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKA----TLEKAKQTLENERGELANEVKALLQGKGDSEH 1245
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1246 KRKKVEAQLQELQVKFSEGERVRTELADK-----VTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1321 NRQKLSLStKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKD 1393
Cdd:PTZ00121 1726 EENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1161-1730 |
1.27e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1161 LRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELAnEVKALlqgk 1240
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETL---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1241 gdsehkrkkvEAQLQELQVKFSEGERVRTELADKVTKLQVEL----DSVTGLLSQSDsksskltkdfsaLESQLQDTQEL 1316
Cdd:PRK02224 257 ----------EAEIEDLRETIAETEREREELAEEVRDLRERLeeleEERDDLLAEAG------------LDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1317 LQEE-NRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLE 1395
Cdd:PRK02224 315 RREElEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1396 GLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAkyaeerdraeaearEKE 1475
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEC--------------GQP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1476 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLmSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDak 1555
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-- 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1556 lRLEvNLQAMKAQFERDLQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREE 1635
Cdd:PRK02224 538 -RAE-ELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1636 aikqlRKLQAQMKDCMRELDDTRASREEILAqAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1715
Cdd:PRK02224 615 -----REALAELNDERRERLAEKRERKRELE-AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
570
....*....|....*
gi 74180985 1716 KgalaLEEKRRLEAR 1730
Cdd:PRK02224 689 E----LEELEELRER 699
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
924-1851 |
1.42e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 80.09 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 924 VEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTT---EAKLKKLEEDQIIMEDQNCKLAKekklLEDR 1000
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVksyENELDPLKNRLKEIEHNLSKIMK----LDNE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1001 VAEFTTNLMEEEEKSKSLAKLKNK----HEAMITDLEERLRRE----EKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1072
Cdd:TIGR00606 271 IKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTvrekERELVDCQRELEKLNKERRLLNQEKTELLVEQG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1073 ELKMQlakkeeelqaalARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:TIGR00606 351 RLQLQ------------ADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1153 DSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHS---QAVEELADQLEQTKRVKATLEKAKQTLENERGE- 1228
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKelqQLEGSSDRILELDQELRKAERELSKAEKNSLTEt 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1229 LANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQveldSVTGLLSQSDSKSSKLTKDFSAlES 1308
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE----QIRKIKSRHSDELTSLLGYFPN-KK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1309 QLQDTQEllqeenrqklSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGClETAEEAKR 1388
Cdd:TIGR00606 574 QLEDWLH----------SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1389 RLQKDLEGLSQR---LEEKVAAY------------------DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFD 1447
Cdd:TIGR00606 643 RLKEEIEKSSKQramLAGATAVYsqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1448 QLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaleEAMEQKAELERLNKQFRTEMEDLMSSKD---DVGksvhele 1524
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLGTIMPEEESAKVcltDVT------- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1525 kSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD-----LQGRDEQSEEKKKQlVRQVREMEAELE 1599
Cdd:TIGR00606 793 -IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskIELNRKLIQDQQEQ-IQHLKSKTNELK 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1600 DERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMrelddtraSREEILAQAKENEKKLKSME 1679
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ--------QEKEELISSKETSNKKAQDK 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1680 AEMI--QLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaQLEEELEEEQGNTELINDRLKKANL 1757
Cdd:TIGR00606 943 VNDIkeKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-NEDMRLMRQDIDTQKIQERWLQDNL 1021
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1758 QIDQINTDLN-LERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKykasiaalEAKIAQLEEQLDNETK--ERQAAS 1834
Cdd:TIGR00606 1022 TLRKRENELKeVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRN--------HVLALGRQKGYEKEIKhfKKELRE 1093
|
970
....*....|....*..
gi 74180985 1835 KQVRRTEKKLKDVLLQV 1851
Cdd:TIGR00606 1094 PQFRDAEEKYREMMIVM 1110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1185-1921 |
2.41e-14 |
|
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: 79.34 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1185 AQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENergelanevkalLQGKGDSEHKRKKVEAQLQELQVkfseg 1264
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------------LRREREKAERYQALLKEKREYEG----- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1265 ervrTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLStklkqmEDEKNSFREQ 1344
Cdd:TIGR02169 226 ----YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1345 LeeeeeakRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELdd 1424
Cdd:TIGR02169 296 I-------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1425 llvdldhqRQSVSNLEKKQKKFDQLLAEEKtisakyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRT 1504
Cdd:TIGR02169 367 --------EDLRAELEEVDKEFAETRDELK-------DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1505 EMEDLMSSKDDVGKSVHELEKSkralEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERdLQGRDEQSEEKK 1584
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERV 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1585 KQLVRQVREMEAELE------------DERKQRSMAMAARKKLEMDLKDLEAhidtankNREEAIKQLRKLQA------- 1645
Cdd:TIGR02169 507 RGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDDA-------VAKEAIELLKRRKAgratflp 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1646 --QMKDCMRELD------------------------------DT------------------------------------ 1657
Cdd:TIGR02169 580 lnKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgDTlvvedieaarrlmgkyrmvtlegelfeksgamtggs 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1658 RASREEILAQAKENEK------KLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARI 1731
Cdd:TIGR02169 660 RAPRGGILFSRSEPAElqrlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1732 AQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERshAQKNENARQQLERQNKELKAKLQEMESAVkSKYKASIAA 1811
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE--EALNDLEARLSHSRIPEIQAELSKLEEEV-SRIEARLRE 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1812 LEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANA 1891
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
810 820 830
....*....|....*....|....*....|
gi 74180985 1892 SRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1385-1901 |
4.41e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1385 EAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEER 1464
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1465 DRAEaEAREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQL 1541
Cdd:PRK03918 266 ERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1542 EELEDELQATEDAKLRLEVNLQAmkaqFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKD 1621
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1622 LEAHIdtanKNREEAIKQLRKLQAQMKDCMRELDDTRasREEILAqakENEKKLKSMEAEMIQLQEELAAAERAKRQAQQ 1701
Cdd:PRK03918 417 LKKEI----KELKKAIEELKKAKGKCPVCGRELTEEH--RKELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1702 ERD---------ELADEIANSSGK-GALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERS 1771
Cdd:PRK03918 488 VLKkeseliklkELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1772 HAQKNENARQQLERQN----KELKAKLQEMESAVK-----SKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEK 1842
Cdd:PRK03918 568 LEEELAELLKELEELGfesvEELEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1843 KLKDVLLQVEDERRnaEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELE 1901
Cdd:PRK03918 648 ELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
833-1452 |
4.68e-14 |
|
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: 78.09 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 833 KVKPLLNSIRHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRArltakKQE 912
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS-----QEI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 913 LEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKL--KKLEEDQIIMEDQNCKL 990
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsaFRDLQGQLAHAKKQQEL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 991 AKEKKLLEDRVAEFTTN--LMEEEEKSKSLAKLKNKHEaMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQceKLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1069 AqiaelKMQLAKKEEELQAALARVEEEAAQKNMALKKIR----ELETQISELQEDLESERASRNKAEKQKRDLGEELEAL 1144
Cdd:TIGR00618 515 P-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1145 KTELEDTLDSTAAQQELRSKREQEVSILKKTLEdeaktHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTlen 1224
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ-----PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR--- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1225 ergelanevKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSV---TGLLSQSDSKSSKLTK 1301
Cdd:TIGR00618 662 ---------EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeyDREFNEIENASSSLGS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1302 DFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQL-EEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCL 1380
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1381 ETAEEAK----RRLQKDLEGLSQRLEEkvaaydklektKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAE 1452
Cdd:TIGR00618 813 PSDEDILnlqcETLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
931-1709 |
4.98e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 77.84 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 931 CQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK----KLEEDQIIMEDQNcKLAKEKKLLEDRVaefTT 1006
Cdd:pfam05483 59 CHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1007 NLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAelqaqiaelKMQLAKKEEELQ 1086
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIE---------KMILAFEELRVQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1087 AALARVEEEAaqknmalkKIRELETQISELQEDLESERasrNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKRE 1166
Cdd:pfam05483 206 AENARLEMHF--------KLKEDHEKIQHLEEEYKKEI---NDKEKQVSLLLIQITEKENKMKDL---TFLLEESRDKAN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1167 QevsilkktLEDEAKTHEAQIQEMRQKHSQAVEELADqleqtkrVKATLEKAKQTLENERGELANEVKALLQgkgdsehK 1246
Cdd:pfam05483 272 Q--------LEEKTKLQDENLKELIEKKDHLTKELED-------IKMSLQRSMSTQKALEEDLQIATKTICQ-------L 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1247 RKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1327 LSTKLKQME---DEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEE 1403
Cdd:pfam05483 410 LKKILAEDEkllDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1404 KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKfdqLLAEEKTISAKYAEERDRAEAEAREKETKALSLAR 1483
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1484 ALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQ 1563
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1564 AMKAQFERDLQGRDEQSEEKK---KQLVRQVREMEAELEDERK-QRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQ 1639
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKlQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSE 726
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1640 LrklqAQMKDCMRELDDTRASREEILAQAKENEKKLKSmeaemiQLQEELAAAERAKRQAQQERDELADE 1709
Cdd:pfam05483 727 L----GLYKNKEQEQSSAKAALEIELSNIKAELLSLKK------QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
846-1413 |
8.34e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 846 ELLAKEAELTKVREKHLAAENRLTEMETMQ---SQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEa 922
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKeeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 923 RVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvtteAKLKKLEEDQIIMEdqncKLAKEKKLLEDRVA 1002
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE-------ERIKELEEKEERLE----ELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1003 EFTTNLmEEEEKSKSLAKLKNKHEAMITDLEerLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKE 1082
Cdd:PRK03918 356 ELEERH-ELYEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1083 EELQAA------LARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKteLEDTLDsta 1156
Cdd:PRK03918 429 EELKKAkgkcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAE--- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1157 aqqELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQ--AVEELADQLEQTKRVKATLEKAKQTLENERGELANEVK 1234
Cdd:PRK03918 504 ---QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1235 ALlqGKGDSEHKRKKVEaQLQELQVKFSEGERVRTELADKVTKLQVELDSvtglLSQSDSKSSKLTKDFSALESQLQDTQ 1314
Cdd:PRK03918 581 EL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1315 ELLQEENRQKlsLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLqkdl 1394
Cdd:PRK03918 654 KKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE----LEKLEKALERV---- 723
|
570
....*....|....*....
gi 74180985 1395 eglsQRLEEKVAAYDKLEK 1413
Cdd:PRK03918 724 ----EELREKVKKYKALLK 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
878-1419 |
2.62e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 878 LMAEKLQLQEQLQAETElCAEAEELRARLTAKKQELEEICHDLEarveeeeercqYLQAEKKKMQQNIQELEEQLEEEES 957
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIE-EKEEKDLHERLNGLESELAELDEEIE-----------RYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 958 ARQKLQlekvTTEAKLKKLEEDqiIMEDQncklaKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERL- 1036
Cdd:PRK02224 249 RREELE----TLEAEIEDLRET--IAETE-----REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRe 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1037 ---RREEKQRQELEKTR---RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQknmalkkIRELE 1110
Cdd:PRK02224 318 eleDRDEELRDRLEECRvaaQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE-------IEELE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1111 TQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQEVSILK--------KTLEDEAkt 1182
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL---EATLRTARERVEEAEALLEagkcpecgQPVEGSP-- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1183 HEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERG--ELANEVKALLQGKGDSEHKRKKVEAQLQELQVK 1260
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1261 FSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALEsQLQDTQELLQEENRQKLSLSTKLKQMEDEKNS 1340
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1341 FREQLEEEEEAKRNLEKQ-----IATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTK 1415
Cdd:PRK02224 625 RRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALE 704
|
....
gi 74180985 1416 TRLQ 1419
Cdd:PRK02224 705 NRVE 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1706 |
3.07e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.34 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1056 DSTDLSDQIAELQAQIAELkmqlakkeEELQAALarveEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKR 1135
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1136 DLG-EELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHE-AQIQEMRQKHSQAVEELADQLEQTKRVKA 1213
Cdd:COG4913 287 QRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1214 TLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADkvtklqvELDSVTGLLSQSD 1293
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLERRKSNIP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1294 SKSSKLTKdfsALESQLQDTQ-------ELLQ---EENR-----------QKLSL---STKLKQMED--EKNSFREQLEE 1347
Cdd:COG4913 440 ARLLALRD---ALAEALGLDEaelpfvgELIEvrpEEERwrgaiervlggFALTLlvpPEHYAAALRwvNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1348 EEEAKRNLEKQIATLHAQVTdmkkkmedgVGCLETAE-EAKRRLQKDLEGLSQRLeeKVAAYDKLEKTKTRLQQELDDLL 1426
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSL---------AGKLDFKPhPFRAWLEAELGRRFDYV--CVDSPEELRRHPRAITRAGQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1427 VDLDHQ--------RQSV---SNLEKKQKKFDQLLAEEKTIsAKYAEERDRAEAEAREKETKALSLARALEEAMEQK--- 1492
Cdd:COG4913 586 NGTRHEkddrrrirSRYVlgfDNRAKLAALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIdva 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1493 ---AELERLNKQfrteMEDLMSSKDDVgksvhelekskRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF 1569
Cdd:COG4913 665 saeREIAELEAE----LERLDASSDDL-----------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1570 ERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAmaarkklemdlKDLEAHIDTANKNREEAIKQLRKLQAQMK- 1648
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR-----------ENLEERIDALRARLNRAEEELERAMRAFNr 798
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1649 ---DCMRELDDTRASREEILA-------------QAKENEKKLKSMEAEMIQLQEELaaaERAKRQAQQERDEL 1706
Cdd:COG4913 799 ewpAETADLDADLESLPEYLAlldrleedglpeyEERFKELLNENSIEFVADLLSKL---RRAIREIKERIDPL 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1326-1921 |
5.67e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1326 SLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKV 1405
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1406 AAYDKLEKTK--------------TRLQQELDDLLVDLDHQRQSVSNLEKKQKKF-DQLLAEEKTIsakyaeerDRAEAE 1470
Cdd:TIGR04523 124 VELNKLEKQKkenkknidkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1471 AREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQ---QVEEMKTQLEELEDE 1547
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1548 LQATEDAKLRLEVNLQAMKAQFErDLqgRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHID 1627
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEIS-DL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1628 TANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELaaaerakRQAQQERDELA 1707
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-------KKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1708 DEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1788 KELKAKLQEMESAVKSkYKASIAALEAKIAQLEEQLDNetKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADK 1867
Cdd:TIGR04523 506 KELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1868 ASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1034-1852 |
5.94e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 74.60 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1034 ERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKnmalKKIRELE 1110
Cdd:COG3096 282 ELSERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQTALRQQ----EKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1111 TQISELQEDLESERASRNKAEKQKRDLGEELEA-------LKTELED---TLDS--TAA---QQELRSKRE-QEVSILKK 1174
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1175 TLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLEN-----ERGELANEVKALLQGKGDSEH---K 1246
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQAlaqR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1247 RKKVEAQLQELQVKFSEGERVRTELADkvtklqveldsvtglLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEE---------------FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1327 LSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVtdmkkkmedgvGC-LETAEEAKRRLQKDLEglsqRLEEKV 1405
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS-----------GEaLADSQEVTAAMQQLLE----REREAT 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1406 AAYDKLEKTKTRLQQElddllvdldhqrqsVSNLEKKQKKFD-QLLAEEKTISAKYAEE-------RDRAEAEAREKETK 1477
Cdd:COG3096 644 VERDELAARKQALESQ--------------IERLSQPGGAEDpRLLALAERLGGVLLSEiyddvtlEDAPYFSALYGPAR 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1478 ALSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEK------SKRAL--------------- 1530
Cdd:COG3096 710 HAIVVPDLSAVKEQLAGLEDC-------PEDLYliegdpDSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraa 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1531 -EQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED--- 1600
Cdd:COG3096 783 rEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQhra 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1601 -ERKQRSMAMAARKKLEMdLKDLEAHI-----DTANKNREEAIKQLRKLQaQMKDCMRELDDTRASREEILAQakenekk 1674
Cdd:COG3096 858 qEQQLRQQLDQLKEQLQL-LNKLLPQAnlladETLADRLEELREELDAAQ-EAQAFIQQHGKALAQLEPLVAV------- 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN----SSGKGALALEEKR----RLEARIAQLEEELEEEqgnte 1746
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphfSYEDAVGLLGENSdlneKLRARLEQAEEARREA----- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1747 liNDRLKKANLQIDQINTDL-NLERSHaqknENARQQLerqnKELKAKLQEMESAV-----------KSKYKASIAALEA 1814
Cdd:COG3096 1004 --REQLRQAQAQYSQYNQVLaSLKSSR----DAKQQTL----QELEQELEELGVQAdaeaeerarirRDELHEELSQNRS 1073
|
890 900 910
....*....|....*....|....*....|....*...
gi 74180985 1815 KIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVE 1852
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1450-1923 |
7.07e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.31 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1450 LAEEKTISAKYAEERDRAEA----------EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS 1519
Cdd:PRK02224 215 LAELDEEIERYEEQREQAREtrdeadevleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERdLQGRDEQSEEKKKQLVRQVREMEAELE 1599
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1600 DERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSME 1679
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1680 A-EMIQLQEELAAAERAKrQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEEEQGnTELINDRLKKANLQ 1758
Cdd:PRK02224 454 CpECGQPVEGSPHVETIE-EDRERVEELEAELED-------LEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1759 IDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKAsIAALEAKIAQLEEQLDNETK------ERQA 1832
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE-VAELNSKLAELKERIESLERirtllaAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1833 ASKQVRRTEKKLKDvLLQVEDERRnaeqfkDQADKASTRLKQLKRQ-----LEEAEEEAQRANASRRKLQRELEDATETA 1907
Cdd:PRK02224 604 AEDEIERLREKREA-LAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
490
....*....|....*.
gi 74180985 1908 DAMNREVSSLKNKLRR 1923
Cdd:PRK02224 677 DDLQAEIGAVENELEE 692
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
991-1852 |
1.14e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.84 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 991 AKEKKLLEDRVAEFTTNLMEEEeksKSLAKLKNKHEAMitdleerlRREEkqrQELEKTRRKLEGDSTDLSDQIAELQAq 1070
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSR---RQLAAEQYRLVEM--------AREL---AELNEAESDLEQDYQAASDHLNLVQT- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1071 iaelKMQLAKKEEELQAALARVEEEAAQKNMALKKIREletQISELQEDLESERASRNKAEKQKRDLGEELEALKTEled 1150
Cdd:PRK04863 343 ----ALRQQEKIERYQADLEELEERLEEQNEVVEEADE---QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTR--- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1151 TLDSTAAQQELRSKRE--QEVSILKKTLEDEAKTHEAQIQEMrqkhSQAVEELADQLEQTKRVKATLEKAKQTL-----E 1223
Cdd:PRK04863 413 AIQYQQAVQALERAKQlcGLPDLTADNAEDWLEEFQAKEQEA----TEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1224 NERGELANEVKALLQgkgdsEHKRKKVEA-QLQELQVKFSEGERvRTELADKVTKLQVELDSVTGLLSQSDSksskltkD 1302
Cdd:PRK04863 489 VSRSEAWDVARELLR-----RLREQRHLAeQLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------E 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1303 FSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMkkkmedgvgcLET 1382
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1383 AEEAKRRLQKDLEglsqRLEEKVAAYDKLEKTKTRLQQelddllvdldhQRQSVSNLEKKQKKFDQLLAEE---KTISAK 1459
Cdd:PRK04863 626 SQDVTEYMQQLLE----RERELTVERDELAARKQALDE-----------EIERLSQPGGSEDPRLNALAERfggVLLSEI 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1460 YA--EERDRAEAEAREKETKALSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----- 1526
Cdd:PRK04863 691 YDdvSLEDAPYFSALYGPARHAIVVPDLSDAAEQLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvki 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1527 -----------------KRALEQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEK 1583
Cdd:PRK04863 764 adrqwrysrfpevplfgRAAREKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAE 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1584 KKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANK-NREEAIKQLRKLQAQMKDCmreLDDTR--AS 1660
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADETLADRVEEIREQLDEA---EEAKRfvQQ 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1661 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleE 1740
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------K 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1741 EQGNTELINDRLKKANLQIDQINTDLNLERS-HAQKNE------NARQQLERQNKELKAKLQEM-----------ESAVK 1802
Cdd:PRK04863 983 NSDLNEKLRQRLEQAEQERTRAREQLRQAQAqLAQYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadsgaeerARARR 1062
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1803 SKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVE 1852
Cdd:PRK04863 1063 DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1477-1923 |
1.27e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1477 KALSL-ARALeeAMEQkaeLERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQ---LEELEDELQATE 1552
Cdd:COG4913 192 KALRLlHKTQ--SFKP---IGDLDDFVREYMLEEPDTFEAADALVEHFDDLERA-HEALEDAREQielLEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1553 DAKLRLEVN------LQAMKAQFERDL-QGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMD-LKDLEA 1624
Cdd:COG4913 266 AARERLAELeylraaLRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1625 HIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEmiqLQEELAAAERAKRQAQQERD 1704
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1705 ELADEIANSSGKGALALEEKRRLEARIAQLEEELEEE---------------------------QGNT------------ 1745
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggFALTllvppehyaaal 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1746 ELINDRLKKANLQIDQINTDL-NLERSHAQKNENAR-----------------------------QQLER---------- 1785
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLpDPERPRLDPDSLAGkldfkphpfrawleaelgrrfdyvcvdspEELRRhpraitragq 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1786 --QNKELKAKlqEMESAVKSKY------KASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEK------KLKDV---- 1847
Cdd:COG4913 583 vkGNGTRHEK--DDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqRLAEYswde 660
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1848 --LLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:COG4913 661 idVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1633-1926 |
2.44e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1633 REEAIKQLRKLQAQM---KDCMRELDdtraSREEILAQAKENEKKLKSMEAEMIQLQEELAAAERakRQAQQERDELADE 1709
Cdd:COG1196 174 KEEAERKLEATEENLerlEDILGELE----RQLEPLERQAEKAERYRELKEELKELEAELLLLKL--RELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1710 IANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKE 1789
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1790 LKAKLQEmESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKAS 1869
Cdd:COG1196 328 LEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1870 TRLKQLKRQLE-----EAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDL 1926
Cdd:COG1196 407 EAEEALLERLErleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1924 |
2.65e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskdD 1515
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1516 VGKSVHELEKSKRALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1593 EMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNRE-EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1671
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1672 -------EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQgN 1744
Cdd:COG4717 283 lgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-E 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1745 TELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKA-SIAALEAKIAQLEEQL 1823
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1824 DNETKERQAASKQVRRTEKKLKdvllQVEDERRnaeqfkdqADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:COG4717 442 EELEEELEELREELAELEAELE----QLEEDGE--------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
490 500
....*....|....*....|..
gi 74180985 1904 TET-ADAMNREVSSLKNKLRRG 1924
Cdd:COG4717 510 REErLPPVLERASEYFSRLTDG 531
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1240 |
2.69e-12 |
|
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: 70.56 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 999 DRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1079 AKKEEELQAALArveeeAAQKNMALKKIRELETQiselQEDLESERASR--NKAEKQKRDLGEELEALKTELEDTLDSTA 1156
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSP----EDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1157 AQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKAL 1236
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 74180985 1237 LQGK 1240
Cdd:COG4942 251 LKGK 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1042-1298 |
3.28e-12 |
|
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: 70.56 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1042 QRQELEKTRRKLEgdstDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNmalKKIRELETQISELQEDLe 1121
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1122 serasrNKAEKQKRDLGEELEALKTELEDTLDstAAQQelRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:COG4942 86 ------AELEKEIAELRAELEAQKEELAELLR--ALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1202 ADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVE 1281
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*..
gi 74180985 1282 LDSVTGLLSQSDSKSSK 1298
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1686-1937 |
3.37e-12 |
|
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: 70.56 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1686 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTD 1765
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1766 LNLERSHAQKNENARQQLERQNKeLKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLK 1845
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1846 DVLLQVEDERRNAEQFKDQADKAstrLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1925
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
250
....*....|..
gi 74180985 1926 LPFVVTRRIVRK 1937
Cdd:COG4942 255 LPWPVSGRVVRR 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1721 |
4.24e-12 |
|
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: 70.18 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1478 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1557
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1558 LEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAmAARKKLEMDLKDLEAHIDTANKNREEAI 1637
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1638 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
....
gi 74180985 1718 ALAL 1721
Cdd:COG4942 254 KLPW 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1066-1796 |
4.68e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.20 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1066 ELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERasrNKAEKQKRDLGEELEALK 1145
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1146 TEledtldstaaqQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQaVEELADQLEQTKRVKATLEKAKQTLENE 1225
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1226 RGELANEVKallqgkgDSEHKRKKVEAQLQELQVKFSEgervRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSA 1305
Cdd:TIGR04523 182 KLNIQKNID-------KIKNKLLKLELLLSNLKKKIQK----NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1306 LESQLQDTQELLQEENRQklsLSTKLKQMEDEKNSFReqleeeeeakrNLEKQIATLHAQVTDMKKKMEDGV-----GCL 1380
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIK-----------ELEKQLNQLKSEISDLNNQKEQDWnkelkSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEK-KQKKFDQLLAEEKTISAk 1459
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQIND- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1460 yaeerdrAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:TIGR04523 396 -------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1540 QLEELEDELQATEdaklrlevnlqamkaqferdlqgrdEQSEEKKKQLVRQVREMEaELEDERKQrsmamaarkkLEMDL 1619
Cdd:TIGR04523 469 QLKVLSRSINKIK-------------------------QNLEQKQKELKSKEKELK-KLNEEKKE----------LEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1620 KDLEAHIDTANKNREEAIKQLRKLQAQMKDCMREL--DDTRASREEILAQAKENEKKLKsmeaemiQLQEELAAAERAKR 1697
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIE-------ELKQTQKSLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1698 QAQQERDELADEIANSSGKgalaLEEKrrlEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1777
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKE----IEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
730
....*....|....*....
gi 74180985 1778 NARQQLERQNKELKAKLQE 1796
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1527-1879 |
6.82e-12 |
|
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: 71.24 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1527 KRALEQQVEEMKTQLEELEDELQATEDAKLRLEvnLQAMKAQFERDLqgRDEQSEEKKKQLVRQVREMEAELEDERKQRS 1606
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLE--RQAEKAERYKEL--KAELRELELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1607 MAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAqmkdcmrELDDTRASREEILAQAKENEKKLKSMEAEMIQLQ 1686
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK-------ELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1687 EELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL 1766
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1767 nlershaqknENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDnetkERQAASKQVRRTEKKLKD 1846
Cdd:TIGR02168 403 ----------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE----ELQEELERLEEALEELRE 468
|
330 340 350
....*....|....*....|....*....|...
gi 74180985 1847 VLLQVEDERRnaeQFKDQADKASTRLKQLKRQL 1879
Cdd:TIGR02168 469 ELEEAEQALD---AAERELAQLQARLDSLERLQ 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1003-1324 |
1.06e-11 |
|
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: 70.15 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1003 EFTTNLME--EEEKSKSLAKLKNKHEAMitdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK 1080
Cdd:pfam17380 269 EFLNQLLHivQHQKAVSERQQQEKFEKM---EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1081 KEEEL----QAALARVEEEAAQKNMALK--KIRELETQISELQEDLESERASRNKAEKQKRdLGEELEALKTELEDTLDS 1154
Cdd:pfam17380 346 RERELerirQEERKRELERIRQEEIAMEisRMRELERLQMERQQKNERVRQELEAARKVKI-LEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1155 TAAQQElrSKREQEVsilkKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQ----TLENERGELA 1230
Cdd:pfam17380 425 IRAEQE--EARQREV----RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKILE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1231 NEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRteLADKVTKLQVELDSVTGLLSQSdSKSSKLTKDFSALESQL 1310
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEMEERRRIQEQM-RKATEERSRLEAMERER 575
|
330
....*....|....
gi 74180985 1311 QDTQELLQEENRQK 1324
Cdd:pfam17380 576 EMMRQIVESEKARA 589
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1196-1915 |
1.14e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1196 QAVEELADQLEQTKRVKATLEKAKQtlenergelanEVKALLQGKGD-SEHKRKKVEAQLQELQVKFSEGERVRTELAdk 1274
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELaERYAAARERLAELEYLRAALRLWFAQRRLE-- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1275 vtKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQD-TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLeeeeeakR 1353
Cdd:COG4913 292 --LLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRR-------A 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1354 NLEKQIATLHAQVTDMKkkmedgvgclETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQR 1433
Cdd:COG4913 363 RLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1434 QSVSNLEKKQKKFDQLLAEEKTISAK----YAEERDRAEAEAR-----EKE--TKALSL------ARALEEAMEQKAELE 1496
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEAelpfVGELIEVRPEEERwrgaiERVlgGFALTLlvppehYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1497 RLNKQF-RTEMEDLMSSKDDVGKSVHELE----KSKRALEQQVEEMK-----TQLEELEDELQA-TEDAKLRLEvnlqam 1565
Cdd:COG4913 513 RLVYERvRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLEAELGRRFdyvcvDSPEELRRHPRAiTRAGQVKGN------ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1566 KAQFERDLQGRDEQ-------SEEKKKQLVRQVREMEAELEDerkqrsmamaarkkLEMDLKDLEAHIDTANKnREEAIK 1638
Cdd:COG4913 587 GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQE-RREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1639 QLRKLQAQMKDcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkga 1718
Cdd:COG4913 652 RLAEYSWDEID-VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ------ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1719 lALEEKRRLEARIAQLEEELEEEQgnTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKAKLQEME 1798
Cdd:COG4913 725 -AEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEELERAM 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1799 SAVKSKYKASIAALEAKIAQLEE------QLDNE---TKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQfkdqadkas 1869
Cdd:COG4913 794 RAFNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKE--------- 864
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1870 tRLKQLKRQLEEAE---------EEAQRANASRRKLQRELEDATETADAMNREVS 1915
Cdd:COG4913 865 -RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1060-1698 |
1.27e-11 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 69.85 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1060 LSDQIAELQAQIAELKMQLAKKEEELQAALARVE---EEAAQKNMALKKirELETQISELQEdleserasrnkaekQKRD 1136
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKtfwSPELKKERALRK--EEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1137 LGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAvEELADQLEQTKR----VK 1212
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH-ERQAKELFLLRKtleeME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1213 ATLEKAKQTLeNERGELANEVKALLQGKG--------DSEHKRKKVEAQLQ------ELQVKFSEGERVRTELADKVTKL 1278
Cdd:pfam10174 144 LRIETQKQTL-GARDESIKKLLEMLQSKGlpkksgeeDWERTRRIAEAEMQlghlevLLDQKEKENIHLREELHRRNQLQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1279 Q--VELDSVTGLLSQSDSKSSKLTKDFSALESQLQ--DTQELLQEENRQKlslstKLKQMEDEKNSFR------EQLEEE 1348
Cdd:pfam10174 223 PdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREE-----EIKQMEVYKSHSKfmknkiDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1349 EEAKRN----LEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDD 1424
Cdd:pfam10174 298 LSKKESellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1425 LLVDLDHQRQSVSNLEKK----QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLArALEEAMEQKAE-LERLN 1499
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ------ATEDAKLR-LEVNLQAMKAQFERd 1572
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSK- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1573 LQGRD------EQSEEKKKQLVRQVREMEAELEDERKQRSMA-------MAARKKLEMDLKDLEAHIDTANKNREEAIKQ 1639
Cdd:pfam10174 536 LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAqaeverlLGILREVENEKNDKDKKIAELESLTLRQMKE 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1640 LRKLQAQMKDCMRELddtRASREEILAQAKENEKKLKSMEAEmIQLQEELAAAERAKRQ 1698
Cdd:pfam10174 616 QNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQ-LQLEELMGALEKTRQE 670
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1277-1936 |
2.32e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.38 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1277 KLQVELDSVTGLLSQSDSKS-SKLTKDFSaleSQLQDTQELLQEEN----RQK-------LSLSTKLKQMEDEKNSFREQ 1344
Cdd:pfam15921 56 KYEVELDSPRKIIAYPGKEHiERVLEEYS---HQVKDLQRRLNESNelheKQKfylrqsvIDLQTKLQEMQMERDAMADI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1345 LEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDD 1424
Cdd:pfam15921 133 RRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMST 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1425 LlvdldHQRQSVSNLEKKQKKFDqllAEEKTISAKYAEERDRAEAEAREKETKalslaraleeameqkaeLERLNKQFRT 1504
Cdd:pfam15921 213 M-----HFRSLGSAISKILRELD---TEISYLKGRIFPVEDQLEALKSESQNK-----------------IELLLQQHQD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1505 EMEDLMSSKDDVGKSVHELEKSKRAleqQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK 1584
Cdd:pfam15921 268 RIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1585 KQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEI 1664
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1665 LAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQGN 1744
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK-------EMLRKVVEELTAKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1745 TELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESavkskYKASIAALEAKIAQLEEQLD 1824
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-----LKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1825 NETK-----ERQAASKQVRRTEKKLkdvllQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQR-ANASRRKLqR 1898
Cdd:pfam15921 573 NMTQlvgqhGRTAGAMQVEKAQLEK-----EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKlVNAGSERL-R 646
|
650 660 670
....*....|....*....|....*....|....*...
gi 74180985 1899 ELEDATETADAMNREVSSLKNKLRRGDLPFVVTRRIVR 1936
Cdd:pfam15921 647 AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1012-1498 |
2.45e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1092 VEEEAAQKNMAL--KKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1169
Cdd:COG4717 132 QELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1170 SILKKTLEDEAKTHEAQIQEMRQKhsQAVEELADQLEQTKRVK------ATLEKAKQTLENERGELANEVKALLQ----G 1239
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLLLliaaalLALLGLGGSLLSLILTIAGVLFLVLGllalL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1240 KGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQlqdTQELLQE 1319
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL---EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1320 ENRQKLSLSTKLKQMEDEKnSFREQLeEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEeakrrLQKDLEGLSQ 1399
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEE-ELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1400 RLEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsVSNLEKkqkkfDQLLAEektisAKYAEERDRAEAEAREKETKAL 1479
Cdd:COG4717 440 ELEELEEELEELREELAELEAE--------------LEQLEE-----DGELAE-----LLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*....
gi 74180985 1480 SLARALEEAMEQKAELERL 1498
Cdd:COG4717 496 KLALELLEEAREEYREERL 514
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1270-1913 |
2.50e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1270 ELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSfreQLEEEE 1349
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNG---ELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1350 EAKRNLEKQIATLHAQvtdMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQ---ELDDLL 1426
Cdd:pfam12128 315 AAVAKDRSELEALEDQ---HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1427 VDLDHQRQSVSnlekKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEA--------------MEQK 1492
Cdd:pfam12128 392 IAGIKDKLAKI----REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1493 AELERLNK------QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQA---TEDAKLRLEVNL- 1562
Cdd:pfam12128 468 NFDERIERareeqeAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLRKEAPDw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1563 -QAMKAQFERDLQGR-DEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQL 1640
Cdd:pfam12128 548 eQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1641 RKLQAQMKDCMRELDDTRASreeiLAQAKENEKKLKS-MEAEMIQLQEelaAAERAKRQAQQERDELADEIANSSGKGAL 1719
Cdd:pfam12128 628 VQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1720 ALEEKRR--LEARIAQLEEELeeeqgntELINDRlkkaNLQIDQINTDLNLERSHAQKNENArqqLERQNK-ELKAKlqE 1796
Cdd:pfam12128 701 WLEEQKEqkREARTEKQAYWQ-------VVEGAL----DAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASL--G 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1797 MESAVKSKYKASIAALEAKIAQLE---------EQLDNET--KERQAASKQVRRTEKKLKDvlLQVEDERRNAEqfkdqa 1865
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQETwlQRRPRLATQLSNIERAISE--LQQQLARLIAD------ 836
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 74180985 1866 dkASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:pfam12128 837 --TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1888 |
2.60e-11 |
|
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: 69.23 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDL 1120
Cdd:TIGR00618 124 KKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1121 ESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevsilkktledeaKTHEAQIQEMRQKHSQAVEE 1200
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLRE------ALQQTQQSHAY-------------LTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1201 LADQLEQTKRVKATLEKAkqtleNERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRteladkvtklqv 1280
Cdd:TIGR00618 265 LRARIEELRAQEAVLEET-----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL------------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1281 eldsvtgllsqsdSKSSKLTKDFSALESQLQDTQELLQEENRqklslstkLKQMEDEKNSFREQLEEEEEakrnLEKQIA 1360
Cdd:TIGR00618 328 -------------MKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQHT----LTQHIH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1361 TLHAQVTDMKKKMEdgVGCLETAEEAKRRLQKDLEGLSQRLEE--KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSN 1438
Cdd:TIGR00618 383 TLQQQKTTLTQKLQ--SLCKELDILQREQATIDTRTSAFRDLQgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1439 LEKKQKKFDQLLAEEKtisakyaeerDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMEDLMSSKDDVGK 1518
Cdd:TIGR00618 461 LQESAQSLKEREQQLQ----------TKEQIHLQETRKKAVVLARLLELQ-EEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1519 ------SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdeqseekkkQLVRQVR 1592
Cdd:TIGR00618 530 mqrgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----------ITVRLQD 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1593 EMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLrklqaqmkdcmrelddTRASREEILAQAKENE 1672
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT----------------ALHALQLTLTQERVRE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1673 KKLKSMEAEMI---QLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIN 1749
Cdd:TIGR00618 663 HALSIRVLPKEllaSRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1750 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAvkskykasIAALEAKIAQLEEQLDNETKE 1829
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL--------REEDTHLLKTLEAEIGQEIPS 814
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1830 RQAAskqvrrtekklkdVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQR 1888
Cdd:TIGR00618 815 DEDI-------------LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1134-1716 |
3.46e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1134 KRDLGEELEALKTELeDTLDstAAQQELRSKREQeVSILKKtLEDEAKTHEAQIQEMRQ-----------KHSQAVEELA 1202
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLE--RAHEALEDAREQ-IELLEP-IRELAERYAAARERLAEleylraalrlwFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1203 DQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKK-VEAQLQELQVKFSEGERVRTELADKVTKLQVE 1281
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1282 LDSVTgllsqsdsksskltKDFSALESQLQDTQELLQEENRQklsLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIAT 1361
Cdd:COG4913 375 LPASA--------------EEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1362 LHAQVTDMKKKMEDGVGCLETA----------EEAKRRLQKDLEGL--SQRL--------EEKVAAYDKLEKTKTRLQQE 1421
Cdd:COG4913 438 IPARLLALRDALAEALGLDEAElpfvgelievRPEEERWRGAIERVlgGFALtllvppehYAAALRWVNRLHLRGRLVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1422 LDDLLVDLDHQRQSVSN-----LEKKQKKFDQLLAEEktisakYAEERDRA---EAEAREKETKALSlaraleeameqka 1493
Cdd:COG4913 518 RVRTGLPDPERPRLDPDslagkLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAIT------------- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1494 eLERLNKQFRTemedlMSSKDDvgksvHELEKSKRAL----EQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF 1569
Cdd:COG4913 579 -RAGQVKGNGT-----RHEKDD-----RRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1570 ERdLQGRDEQSEEKKKqlVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKD 1649
Cdd:COG4913 648 EA-LQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1650 CMRELDDTRASREEILAQAKENekkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGK 1716
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLE---LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1294-1898 |
3.62e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1294 SKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEK---NSFREQLEEEEEAKRNLEKQIATLHAQVTDMK 1370
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1371 KKMEDGVGCLETAEEAKRRLqKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLL 1450
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1451 AEEKTISAKYAEERDRAEAeareketkalslaraLEEAMEQKAELERLNKQFRTEmedlmsSKDDVGKSVHELEKSKRAL 1530
Cdd:PRK03918 345 KKLKELEKRLEELEERHEL---------------YEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1531 EQQVEEMKTQLEELEDELQATEDAKLRLEvnlqamKAQFERDLQGRdEQSEEKKKQLVRqvrEMEAELEDERKQRSMAMA 1610
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGR-ELTEEHRKELLE---EYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1611 ARKKLEMDLKDLEAHIdtankNREEAIKQLRKLQAQMKDCMRELDDTRAsrEEILAQAKENEK---KLKSMEAEMIQLQE 1687
Cdd:PRK03918 474 KERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEKlkeKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1688 ELAAAERAKrqaqqerdeladeianssGKGALALEEKRRLEARIAqleeeleeeqgntELINDRLKKANLQIDQINTDLN 1767
Cdd:PRK03918 547 ELEKLEELK------------------KKLAELEKKLDELEEELA-------------ELLKELEELGFESVEELEERLK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1768 -LERSHAQKNE--NARQQLERQNKELKAKLQEMESAVK--SKYKASIAALEAKIAQLEEQLDNETKERqaASKQVRRTEK 1842
Cdd:PRK03918 596 eLEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEelAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSR 673
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1843 KLKDVLLQVEDERRNAEQFKDQADKastrLKQLKRQLEEAEEEAQRANASRRKLQR 1898
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEK----LKEELEEREKAKKELEKLEKALERVEE 725
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1443-1846 |
3.86e-11 |
|
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: 67.61 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1443 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1523 LEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKaqferdlqgrdeqseEKKKQLVRQVREMEAELEDER 1602
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1603 KQRSMAMAARKKLEMDLKDLEAHIDtankNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1683 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGA---LALEEKRrleariAQLEEELEEEQGNTELINDRLKKANLQI 1759
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdasLALREGR------ARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1760 DQINTDLNLERSHAQK-----------NENARQQLERQNKELKAKLQEMESAvKSKYKASIAALEAKIAQLEEQLDNET- 1827
Cdd:pfam07888 328 QRLEERLQEERMEREKlevelgrekdcNRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVAd 406
|
410 420
....*....|....*....|
gi 74180985 1828 -KERQAASKQVRRTEKKLKD 1846
Cdd:pfam07888 407 aKWSEAALTSTERPDSPLSD 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1031-1205 |
3.98e-11 |
|
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: 64.95 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1031 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAlKKIRELE 1110
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1111 TqiseLQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKREQEVSILKKTLEDEAKTHEAQIQEM 1190
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 74180985 1191 RQKHSQAVEELADQL 1205
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
870-1468 |
5.33e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 870 EMETMQSQLMA-EKL-QLQEQLQAETELCAEAEELRARLTA-----KKQELEEICHDLEARVEEEEERCQYLQAEKKKMQ 942
Cdd:COG4913 243 ALEDAREQIELlEPIrELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 943 QNIQELEEQLEEEESAR-QKLQLEKVTTEAKLKKLEEDQIIMEDQ----NCKLAKEKKLLEDRVAEFTTNLMEEEEKSKS 1017
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE-LQAQIAELK-----MQLAKKEEELQAALAR 1091
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1092 ----------VEEEAAQKnmALKKIRELEtqiseLQEDLESERASRNKAEKQKRDLGEEleALKTELEdtLDSTAAQQEL 1161
Cdd:COG4913 483 vlggfaltllVPPEHYAA--ALRWVNRLH-----LRGRLVYERVRTGLPDPERPRLDPD--SLAGKLD--FKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1162 RSKREQEVSILKKTLEDEAKTHEAQIQEMRQ-KHSQAVEELADQleqtKRVKATL------EKAKQTLENERGELANEVK 1234
Cdd:COG4913 552 EAELGRRFDYVCVDSPEELRRHPRAITRAGQvKGNGTRHEKDDR----RRIRSRYvlgfdnRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1235 ALLQGKGDSEHKRKKVEAQLQELQ--VKFSEGERVRTELADKVTKLQVELDSvtglLSQSDSKSSKLTKDFSALESQLQD 1312
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1313 TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKR-----NLEKQIATLHAQvtdmkkkmedgvgclETAEEAK 1387
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGD---------------AVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1388 RRLQKDLEGLSQRLEEkvaAYDKLEKTKTRLQQELDDLLV------------DLDHQRQSVSNLEKKQKKFDQLLAEEKT 1455
Cdd:COG4913 769 ENLEERIDALRARLNR---AEEELERAMRAFNREWPAETAdldadleslpeyLALLDRLEEDGLPEYEERFKELLNENSI 845
|
650
....*....|....*...
gi 74180985 1456 -----ISAKYAEERDRAE 1468
Cdd:COG4913 846 efvadLLSKLRRAIREIK 863
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1535-1923 |
1.99e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1535 EEMKTQLEELEDELQATEDAKLRLEVN-LQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRsmamAARK 1613
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERR----EELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1614 KLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE 1693
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1694 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1773
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1774 QKNENARQQLERQNKELKAKLQEMESAVK---------------------------SKYKASIAALEAKIAQLEEQLD-- 1824
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEev 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1825 ----NETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQranasrrKLQREL 1900
Cdd:PRK02224 495 eerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA-------EAEEEA 567
|
410 420
....*....|....*....|...
gi 74180985 1901 EDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIES 590
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
794-1589 |
2.25e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.30 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 794 LARKAFAKRQQQ---LTAMKVLQRNCaaylRLRNWQWWRLFTKVKPLLNSIRHE--DELLAKEAELTKVREKHLAAENRL 868
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQA----RNQNSMYMRQLSDLESTVSQLRSElrEAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 869 TEMETMQSQLMAEKLQLQEQLQA--------ETELCAEAEE---LRARLTAKKQELEEICHDLEARVEEEEERCQYLQAE 937
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 938 KKKMQQNIQELEEQLEEEESARQKL-----QLE-------KVTTEAKLKK--LEEDQIIMEDQNCKLAKEKKLLEDRVAE 1003
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEKVssltaQLEstkemlrKVVEELTAKKmtLESSERTVSDLTASLQEKERAIEATNAE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1004 FTTNLMEEEEKSKSLAKLKNKHEAMITDLEE----RLRREEKQRQeLEKTRRKLEgDSTDLSDQIAELQAQIAELKMQLa 1079
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQMAEKDKV-IEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQL- 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1080 kkEEELQAALARVEEEAAQKNMALKKIRELETQISELQedLESERASRNKAEKQK--RDLGEELEALKTELEDTldstaa 1157
Cdd:pfam15921 596 --EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--LEKVKLVNAGSERLRavKDIKQERDQLLNEVKTS------ 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1158 QQELRSKREqEVSILKKTLEDEAKTHEAQIQEMRQkhsqaveeladqleQTKRVKATLEKAKQTLENERGELANEVKALL 1237
Cdd:pfam15921 666 RNELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKM--------------QLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1238 QGKGDSEHKRKKVEA---QLQELQVKFSEGERVRTELADKVTKLQVELDSV-------TGLLSQSDSKSSKLTKDFSALE 1307
Cdd:pfam15921 731 GMQKQITAKRGQIDAlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVateknkmAGELEVLRSQERRLKEKVANME 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1308 S-------QLQDTQELLQEENRQKLSLstKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATL--HAQVTDMKKKMEDGVG 1378
Cdd:pfam15921 811 ValdkaslQFAECQDIIQRQEQESVRL--KLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTrtHSNVPSSQSTASFLSH 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1379 CLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLLAEEK 1454
Cdd:pfam15921 889 HSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRsdicHSSSNSLQTEGS 968
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS--KDDVG--------KSVHELE 1524
Cdd:pfam15921 969 KSSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSsaEGSIGsssqyrsaKTIHSPD 1048
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1525 KSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVR 1589
Cdd:pfam15921 1049 SVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMI-RNQEKRIQKVKDQEKMLLK 1112
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1273-1852 |
3.24e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1273 DKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAK 1352
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1353 RNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAaydKLEKTKTRLQQELDDLLVDLDHQ 1432
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEINEKTT---EISNTQTQLNQLKDEQNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1433 RQSVSNLEKKQKKFDQLLAEEKTIsakyaeerdRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1512
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQL---------KSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1513 KDDVG---KSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE------RDLQGRDEQSEEK 1583
Cdd:TIGR04523 341 NEQISqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeklnQQKDEQIKKLQQE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1584 KKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREE 1663
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1664 ILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalaleekrrleariaqleeeleeeqg 1743
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK------------------------------- 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1744 ntelINDRLKKANLQIDQINTDLNLERSHAQKNEnarqqLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQL 1823
Cdd:TIGR04523 550 ----DDFELKKENLEKEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQKEKEKK-DLIKEIEEKEKKISSLEKEL 619
|
570 580
....*....|....*....|....*....
gi 74180985 1824 DNETKERQAASKQVRRTEKKLKDVLLQVE 1852
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
843-1370 |
3.50e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 843 HEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEA 922
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 923 RVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEdqiIMEDQNCKLAKEkkllEDRVA 1002
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1003 EFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEK---QRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL- 1078
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLt 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1079 ---------AKKEEELQAALARVE----EEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALK 1145
Cdd:pfam05483 461 aiktseehyLKEVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1146 ---TELEDTLDSTaaQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKH----------------SQAVEELADQLE 1206
Cdd:pfam05483 541 ekeMNLRDELESV--REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenkcnnlkkqienkNKNIEELHQENK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1207 QTKRVKATLEKAKQTLENERGELANEVKALLQGKGD-SEHKRKKVEAQLQELQVKFSEGERVRTeLADKVTKLQVELD-- 1283
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEiIDNYQKEIEDKKISEEKLLEEVEKAKA-IADEAVKLQKEIDkr 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1284 ---SVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIA 1360
Cdd:pfam05483 698 cqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
570
....*....|
gi 74180985 1361 TLHAQVTDMK 1370
Cdd:pfam05483 778 ENTAILKDKK 787
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1508 |
3.50e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 851 EAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEICHDLEARVEEEEER 930
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 931 CQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKlledrvaefttNLME 1010
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE-----------AQME 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1011 EEEKSKSLAKL-KNKHEAMITDLEERLRREEkqrQELEKTrrklegdstdlsdqiaelQAQIAELKMQLAKKEEELqaal 1089
Cdd:pfam05483 339 ELNKAKAAHSFvVTEFEATTCSLEELLRTEQ---QRLEKN------------------EDQLKIITMELQKKSSEL---- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1090 arvEEEAAQKNMALKKIRELETQISELQEDLESerasrnkaEKQKRDLGEELEAlkteledtldstaaqqelrskREQEV 1169
Cdd:pfam05483 394 ---EEMTKFKNNKEVELEELKKILAEDEKLLDE--------KKQFEKIAEELKG---------------------KEQEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1170 SILKKTLEDEAKTHEAQIQEMR---QKHSQAVEELADQL--EQTKRVKATLEKAKQTLENER--GELANEVKALLQGKGD 1242
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELekEKLKNIELTAHCDKLLLENKEltQEASDMTLELKKHQED 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1243 SEHKRKKVEAQLQELQvkfsegervrtELADKVTKLQVELDSVTGLLSQSDSKsskltkdfsaLESQLQDTQELLQEENR 1322
Cdd:pfam05483 522 IINCKKQEERMLKQIE-----------NLEEKEMNLRDELESVREEFIQKGDE----------VKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1323 QKLSLSTKLKQMEDEKNSFREQLEeeeeakrNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLE 1402
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIE-------NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1403 EKVAAYDK--------LEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREK 1474
Cdd:pfam05483 654 EIIDNYQKeiedkkisEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
650 660 670
....*....|....*....|....*....|....*
gi 74180985 1475 ETKALSLARALE-EAMEQKAELERLNKQFRTEMED 1508
Cdd:pfam05483 734 EQEQSSAKAALEiELSNIKAELLSLKKQLEIEKEE 768
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-72 |
4.79e-10 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 56.28 E-value: 4.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 74180985 27 AAKKLVWVPSSKNGFEPASLKEEVGEEAIVELvENGKKVKVNKDDI 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1296 |
6.09e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 842 RHE---DELLAKEAELTKVREKHLAAEnrlTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRA---RLTAKKQELEE 915
Cdd:PRK02224 245 EHEerrEELETLEAEIEDLRETIAETE---REREELAEEVRDLRERLEELEEERDDLLAEAGLDDAdaeAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 916 ICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQ--------- 986
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 987 ------------NCKLAKEKKLLEDRVAEFTTNLM-----------------------------------EEEEKSKSLA 1019
Cdd:PRK02224 402 dapvdlgnaedfLEELREERDELREREAELEATLRtarerveeaealleagkcpecgqpvegsphvetieEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1020 KLKNKHEAMITDLEERLRREEkQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQA--ALARVEEEAA 1097
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleAEAEEKREAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1098 QKNM-----ALKKIRELETQISELQEDLESERASRNKAEKQKrDLGEELEALKTELEDtldsTAAQQELRSKREQEVSIL 1172
Cdd:PRK02224 561 AEAEeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA----LAELNDERRERLAEKRER 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1173 KKTLEDEAKthEAQIQEMRQKHSQAVEELADQLEQTKRvkatLEKAKQTLENERGELANEVKALLQGKgdseHKRKKVEA 1252
Cdd:PRK02224 636 KRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDE----LREERDDLQAEIGAVENELEELEELR----ERREALEN 705
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1253 QLQELQVKFSEGE-------RVRTEL-ADKVTKLQVELDSVTGLLSQSDSKS 1296
Cdd:PRK02224 706 RVEALEALYDEAEelesmygDLRAELrQRNVETLERMLNETFDLVYQNDAYS 757
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1305-1557 |
7.58e-10 |
|
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: 63.24 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1305 ALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLeeeeeakRNLEKQIATLHAQVTDMKKKMEDGVGCLETAE 1384
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1385 EAKRRLQKDLEGLSQRLEEKVAAydklektktrLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEER 1464
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRA----------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1465 DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1544
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 74180985 1545 EDELQATEDAKLR 1557
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1381-1920 |
8.46e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKY 1460
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1461 AEERDRAEAEAREKETKALSLARALE------EAMEQKAELERLNKQFR--TEMEDLMSSKDDVGKSVHELEKSKRALEQ 1532
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEkmilafEELRVQAENARLEMHFKlkEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1533 QVEEMKTQLEELEDELQATEDAKLRLEvnlqamkaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAAR 1612
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLE---------------EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1613 KKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE----NEKKLKSMEAEMIQLQEE 1688
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1689 LAAAERAKRQAQQERDELADEIanssGKGALALEEKRRLEaRIAQleEELEEEQGNTELINDRLKKANLQIDQINTDLNL 1768
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFE-KIAE--ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1769 ERSHAQKNENARQQLERQ---NKELKAKlQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQV---RRTEK 1842
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEklkNIELTAH-CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIenlEEKEM 544
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1843 KLKDVLLQVEDE-RRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:pfam05483 545 NLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1392-1822 |
8.69e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1392 KDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDqLLAEEKTISAKYAEERDRAEA-E 1470
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1471 AREKETKAL--SLARALEEAMEQKAELERLNKQF----RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1544
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1545 EDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ------------------LVRQVREMEAELEDERKQRS 1606
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1607 MAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCmreldDTRASREEILAQAKENEKKLKSMEAEMIQLQ 1686
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA-----EELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1687 EELAAAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINT 1764
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1765 DLNLERshaqknenARQQLERQNKELKAKLQEmesavKSKYKASIAALEAKIAQLEEQ 1822
Cdd:COG4717 468 DGELAE--------LLQELEELKAELRELAEE-----WAALKLALELLEEAREEYREE 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1470-1917 |
1.29e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1470 EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1549
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1550 ATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKdLEAHID 1627
Cdd:PRK03918 225 KLEKEVKELEelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1628 TANKNREEAIKQLRKLQAQMKDCMRELDDtrasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKrQAQQERDELA 1707
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1708 DEIANssgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:PRK03918 379 KRLTG---------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1788 K-----ELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQLDNE---TKERQAAsKQVRRTEKKLKDVLLQ-VEDERRNA 1858
Cdd:PRK03918 450 RkelleEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKEselIKLKELA-EQLKELEEKLKKYNLEeLEKKAEEY 527
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1859 EQFKDQADKASTRLKQLKRQLEEAEEEAQRanasRRKLQRELEDATETADAMNREVSSL 1917
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEEL 582
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
838-1122 |
2.98e-09 |
|
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: 62.06 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 838 LNSIRHEDellaKEAELTKVREKHLAAE-NRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEI 916
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 917 CHDLEarvEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNcklakeKKL 996
Cdd:pfam17380 426 RAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------RKI 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 997 LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQIAELK 1075
Cdd:pfam17380 497 LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMERERE 576
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 74180985 1076 MQLAKKEEELQaalaRVEEEAAQKNMALKKIreLETQISELQ-EDLES 1122
Cdd:pfam17380 577 MMRQIVESEKA----RAEYEATTPITTIKPI--YRPRISEYQpPDVES 618
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1107-1907 |
3.94e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.28 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1107 RELETQISELQEDLESERASRNKAEKQKRDLGEELEALK---TELEDTLDS---------TAAQQELRSKREQEvsilkk 1174
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSareSDLEQDYQAasdhlnlvqTALRQQEKIERYQE------ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1175 tlEDEAKTHEAQIQEMrqkhsqAVEELADQLEqtkRVKATLEKAKQTLENERGELANEVKALlqgkgDSEHKRKkveaqL 1254
Cdd:COG3096 355 --DLEELTERLEEQEE------VVEEAAEQLA---EAEARLEAAEEEVDSLKSQLADYQQAL-----DVQQTRA-----I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1255 QELQ-VKFSEGERVRTELADkvtklqveldsvtgllsqsdsksskLTKDfsALESQLQDTQELLQEENRQKLSLSTKLKQ 1333
Cdd:COG3096 414 QYQQaVQALEKARALCGLPD-------------------------LTPE--NAEDYLAAFRAKEQQATEEVLELEQKLSV 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1334 MEDEKNSFRE----------------------QLEEEEEAKRNLEKQIATLHAQVTDmkkkmedgvgcLETAEEAKRRLQ 1391
Cdd:COG3096 467 ADAARRQFEKayelvckiageversqawqtarELLRRYRSQQALAQRLQQLRAQLAE-----------LEQRLRQQQNAE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1392 KDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEA 1471
Cdd:COG3096 536 RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL---EQLRARIKELAARAPAWLAAQDALE 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1472 REKETKALSLA--RALEEAMEQKAELERLNKQfrtemedlmsSKDdvgksvhELEKSKRALEQQVEEMK-------TQLE 1542
Cdd:COG3096 613 RLREQSGEALAdsQEVTAAMQQLLEREREATV----------ERD-------ELAARKQALESQIERLSqpggaedPRLL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1543 ELEDELQAT-----------EDAK--------LR---LEVNLQAMKAQF-------------ERDLQGRDEQS----EEK 1583
Cdd:COG3096 676 ALAERLGGVllseiyddvtlEDAPyfsalygpARhaiVVPDLSAVKEQLagledcpedlyliEGDPDSFDDSVfdaeELE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1584 KKQLV----RQVR--------------------EMEAELEDERKQRSMAMAARKKLEMDLKDLEA----HIDTA-NKNRE 1634
Cdd:COG3096 756 DAVVVklsdRQWRysrfpevplfgraarekrleELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggHLAVAfAPDPE 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1635 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAkRQAQQERDElADEIANSS 1714
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE-TLADRL-EELREELDA-AQEAQAFI 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1715 GKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQInTDLnLERSHAQKNENARQQLERQ---NKELK 1791
Cdd:COG3096 913 QQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL-SEV-VQRRPHFSYEDAVGLLGENsdlNEKLR 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1792 AKLQEMESAvKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDE-----RRNAEQFKDQAD 1866
Cdd:COG3096 991 ARLEQAEEA-RREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEaeeraRIRRDELHEELS 1069
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 74180985 1867 KASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA 1907
Cdd:COG3096 1070 QNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1178-1410 |
4.02e-09 |
|
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: 60.93 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1178 DEAKTHEAQIQEMRQKhsqaVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQEL 1257
Cdd:COG4942 20 DAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1258 QVKFsegERVRTELADKVTKLQV--ELDSVTGLLSQSDSksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQME 1335
Cdd:COG4942 96 RAEL---EAQKEELAELLRALYRlgRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1336 DEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDK 1410
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAE----LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1018-1176 |
5.19e-09 |
|
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: 58.78 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL--AKKEEELQAALARVEEE 1095
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1096 AAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQEVSILKKT 1175
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE------AELEELEAEREELAAKIPPE 175
|
.
gi 74180985 1176 L 1176
Cdd:COG1579 176 L 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
826-1640 |
5.53e-09 |
|
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: 61.52 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 826 QWWRLFTKVKPLLNSIRHEDELLAKEAELTK--VREKHLAAENRLTEMETMQSQLMAEKLQLQE---QLQAETELCAEae 900
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQshaYLTQKREAQEE-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 901 elrarltakKQELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQ 980
Cdd:TIGR00618 255 ---------QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 981 IIMEDQNckLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEamITDLEERLRREEKQRQELEKTRRKLEGDSTDL 1060
Cdd:TIGR00618 326 LLMKRAA--HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE--ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1061 SDQIAELQAQIAELkmQLAKKEEELQAALARVEEEAAQKNMALKKIR-ELETQISELQEDLESERASRNKAEKQKrdLGE 1139
Cdd:TIGR00618 402 LDILQREQATIDTR--TSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREQQ--LQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1140 ELEALKTELEDTLDSTAAQQELrskREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEqtkrvkatlekak 1219
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLEL---QEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE------------- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1220 QTLENERGELANEVKallqgkgdsehKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVtgllsqsdsksskl 1299
Cdd:TIGR00618 542 TSEEDVYHQLTSERK-----------QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL-------------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1300 tkdfsalesqLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRnLEKQIATLHAQVTDMKKkmedgvgc 1379
Cdd:TIGR00618 597 ----------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE-LALKLTALHALQLTLTQ-------- 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1380 lETAEEAKRRLQKDLEglsQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAK 1459
Cdd:TIGR00618 658 -ERVREHALSIRVLPK---ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1460 YAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSskddvgksvhELEKSKRALEQQVEEMKT 1539
Cdd:TIGR00618 734 LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA----------EIQFFNRLREEDTHLLKT 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1540 QLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdeqseEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDL 1619
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
810 820
....*....|....*....|.
gi 74180985 1620 KDLEAHIDTANKNREEAIKQL 1640
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKF 896
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1062-1265 |
5.54e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1062 DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLEserASRNKAEKQKRDLGEEL 1141
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1142 EALKTE------LEDTLDSTAAQQELrskreQEVSILKKTLEDEAKTHEaQIQEMRQKHSQAVEELADQLEQTKRVKATL 1215
Cdd:COG3883 93 RALYRSggsvsyLDVLLGSESFSDFL-----DRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1216 EKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGE 1265
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1051-1253 |
6.84e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1051 RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLeserASRNKA 1130
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1131 EKQKRDLGEELEALK--TELEDTLDSTAAQQELRSKREQEVSILKKtLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQT 1208
Cdd:COG3883 95 LYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74180985 1209 KRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQ 1253
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1083-1550 |
9.48e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1083 EELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKR--DLGEELEALKTELEDT---LDSTAA 1157
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1158 QQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALl 1237
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1238 qgkgDSEHKRKKVEAQLQELQVkfsegervrteladkvtkLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL 1317
Cdd:COG4717 233 ----ENELEAAALEERLKEARL------------------LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1318 QEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQkdLEGL 1397
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1398 SQRLEEKVAAYDklektktrlqQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR--EKE 1475
Cdd:COG4717 369 EQEIAALLAEAG----------VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEleELE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1476 TKALSLARALEEAMEQKAELErlnkqfrTEMEDLMSSkddvgksvHELEKskraLEQQVEEMKTQLEELEDELQA 1550
Cdd:COG4717 439 EELEELEEELEELREELAELE-------AELEQLEED--------GELAE----LLQELEELKAELRELAEEWAA 494
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1199-1821 |
1.47e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.92 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1199 EELADQLEQTKRVKATLEKAKQTLENERGELAN--EVKALLQGKGDS-EHKRKKVEAQLQELQVKFSEGERVRTELADKV 1275
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNidYLEEKLKSSNLElENIKKQIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1276 TKLQVELDSVTGLLSQSDSKSsKLTKDFSALESQLQdtqeLLQEENRQKLSLSTKLKQMEDEKnsfreqleeeEEAKRNL 1355
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKN-RYESEIKTAESDLS----MELEKNNYYKELEERHMKIINDP----------VYKNRNY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1356 EKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQkDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDldhqrqs 1435
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEA--------------REKETKALSLARALEEAMEQKAELER---- 1497
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPdaikkelneinvklQDISSKVSSLNQRIRALRENLDELSRnmem 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1498 LNKQFR-----TEMEDLMSSK--DDVGKSVHELEKSKRALEQQV---EEMKTQLEELEDELQATEDAKLRLEVN-LQAMK 1566
Cdd:PRK01156 449 LNGQSVcpvcgTTLGEEKSNHiiNHYNEKKSRLEEKIREIEIEVkdiDEKIVDLKKRKEYLESEEINKSINEYNkIESAR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1567 AQFERDL--QGRDEQSEEKKKQLVRQVREMEAE-LEDERKQRSMAMAARKKLEmdlkdleahIDTANKNREEAIKQLRKL 1643
Cdd:PRK01156 529 ADLEDIKikINELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWLNALAVISLID---------IETNRSRSNEIKKQLNDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1644 QAQMKDCMRELDDTRASreeilaqakeNEKKLKSMEAEMIQLQEELAAAERAKRQaqqeRDELADEIANssgkgalalee 1723
Cdd:PRK01156 600 ESRLQEIEIGFPDDKSY----------IDKSIREIENEANNLNNKYNEIQENKIL----IEKLRGKIDN----------- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1724 krrLEARIAQLEEeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKS 1803
Cdd:PRK01156 655 ---YKKQIAEIDS-----------IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
650 660
....*....|....*....|
gi 74180985 1804 KYK--ASIAALEAKIAQLEE 1821
Cdd:PRK01156 721 INEtlESMKKIKKAIGDLKR 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1636-1927 |
1.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1636 AIKQLRKLQAQMKDCMreLDDTRAsrEEILAQAKENEKKLKSMEAEMIQLQEELAAAERAkRQAQQERDELADEIAnssg 1715
Cdd:COG4913 202 SFKPIGDLDDFVREYM--LEEPDT--FEAADALVEHFDDLERAHEALEDAREQIELLEPI-RELAERYAAARERLA---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1716 kgalaleEKRRLEARIaqleeeleeeqgntelindRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQ 1795
Cdd:COG4913 273 -------ELEYLRAAL-------------------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1796 EMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEkklkdvlLQVEDErrnAEQFKDQADKASTRLKQL 1875
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG-------LPLPAS---AEEFAALRAEAAALLEAL 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1876 KRQLEEAEEEAQRANASRRKLQRELEDATetadamnREVSSLKNklRRGDLP 1927
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELE-------AEIASLER--RKSNIP 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1614 |
1.69e-08 |
|
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: 59.01 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1383 AEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLLAEEKTISA 1458
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaalEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1459 KYAEERDR-------AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALE 1531
Cdd:COG4942 98 ELEAQKEElaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1532 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAA 1611
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 74180985 1612 RKK 1614
Cdd:COG4942 250 ALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1129-1846 |
1.72e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.74 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1129 KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQE---MRQKHSQAVEELADQL 1205
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnaTRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1206 EQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGER-VRTELADKVTKlqvelds 1284
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeYKKEINDKEKQ------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1285 VTGLLSQSDSKSSKLtKDFSALESQLQDTQELLQEENRQKlslSTKLKQMEDEKNSFREQLEeeeeakrnlekqiatlha 1364
Cdd:pfam05483 242 VSLLLIQITEKENKM-KDLTFLLEESRDKANQLEEKTKLQ---DENLKELIEKKDHLTKELE------------------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1365 qvtDMKKKMEDGVGCLETAEEakrRLQKDLEGLSQRLEEKVAAYDKLEKTKTR----LQQELDDLLVDLDHQRQSVSNLE 1440
Cdd:pfam05483 300 ---DIKMSLQRSMSTQKALEE---DLQIATKTICQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1441 KKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARAlEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSV 1520
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED-EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1521 HELE-------KSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQ 1590
Cdd:pfam05483 453 HDLEiqltaikTSEEHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1591 VREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE 1670
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1671 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEEleeeqgnTELIND 1750
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK-------AKAIAD 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1751 RLKKANLQID-----QINTDLNLERSHAQKNENARQQLERQNKELKAKLQEmESAVKSKYKASIAALEAKIAQLEEQLDN 1825
Cdd:pfam05483 686 EAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEI 764
|
730 740
....*....|....*....|.
gi 74180985 1826 ETKERQAASKQVRRTEKKLKD 1846
Cdd:pfam05483 765 EKEEKEKLKMEAKENTAILKD 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1443-1905 |
1.95e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.68 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1443 QKKFDQLLAEEKTISAkyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERlnKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1523 LEKSKRALeQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDER 1602
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1603 KQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLK--SMEA 1680
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1681 EMIQLQEELAAAERAKRQAQQERDELADEIansSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqiD 1760
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEK---KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL-----D 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1761 QINTDLNLERSHAQKNENarqqLERQNKELKAKLQEMESAVKSKykasiAALEAKIAQLE------EQLDNETKERQAAS 1834
Cdd:TIGR00606 478 QELRKAERELSKAEKNSL----TETLKKEVKSLQNEKADLDRKL-----RKLDQEMEQLNhhtttrTQMEMLTKDKMDKD 548
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1835 KQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1905
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1631-1913 |
2.46e-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: 59.30 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1631 KNREEAIKQLRKLQ---AQMKDCMRELD------DTRASREEILA--QAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1699
Cdd:TIGR02168 172 ERRKETERKLERTRenlDRLEDILNELErqlkslERQAEKAERYKelKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1700 QQERDELADEIANSSGKgalaLEEkrrLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINtdlnlershaqkneNA 1779
Cdd:TIGR02168 252 EEELEELTAELQELEEK----LEE---LRLEVSELEEEIEELQKELYALANEISRLEQQKQILR--------------ER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1780 RQQLERQNKELKAKLQEMESavkskykaSIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAE 1859
Cdd:TIGR02168 311 LANLERQLEELEAQLEELES--------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1860 QFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1534 |
2.82e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 833 KVKPLLNSIRHEDELLAKEAELTK-VREKHLAAENRLTEmetmqSQLMAEKLQLQEQLQAETELCAEAEELRAR------ 905
Cdd:TIGR00606 459 VIKELQQLEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhttt 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 906 ------LTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEkvtteakLKKLEED 979
Cdd:TIGR00606 534 rtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE-------LASLEQN 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 980 QIIMEDQNCKLAKEKKLLEDRVAEFTT---------NLMEEEEKSKS----LAKLKNKHEAMITDLEERLRREEKQRQEL 1046
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVCGsqdeesdleRLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1047 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERAS 1126
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1127 RNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEEL---AD 1203
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLTDV---TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELdtvVS 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1204 QLEQTKRVKATLEKAKQTLENERGELANEvkallqgkgdsehkrkkveaqlqelQVKFSEGERVRTELADKVTKLQVELD 1283
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSE-------------------------KLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1284 SVTGLLSQsdsKSSKLTKDFSALESQLQDTQELLQEENRQKlslstklKQMEDEKNSFREQLEEEEEAKRNLEKQIAT-L 1362
Cdd:TIGR00606 899 SLIREIKD---AKEQDSPLETFLEKDQQEKEELISSKETSN-------KKAQDKVNDIKEKVKNIHGYMKDIENKIQDgK 968
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1363 HAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQElddllvdldhqrQSVSNLEKK 1442
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE------------NELKEVEEE 1036
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1443 QKKFDQLLAEEKTISAKYAEERDRAEAEA-REKETKALSLARALEEAMEQkAELERLNKQFRTEME---DLMSSKDDVGK 1518
Cdd:TIGR00606 1037 LKQHLKEMGQMQVLQMKQEHQKLEENIDLiKRNHVLALGRQKGYEKEIKH-FKKELREPQFRDAEEkyrEMMIVMRTTEL 1115
|
730
....*....|....*.
gi 74180985 1519 SVHELEKSKRALEQQV 1534
Cdd:TIGR00606 1116 VNKDLDIYYKTLDQAI 1131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
827-1219 |
3.10e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 827 WWRLFTKVKPLLNSIRhedELLAKEAELT--KVREKHLAAENRLTEMETMQSQLMAEKLQLQ---EQLQAETELCAEA-- 899
Cdd:PRK03918 360 RHELYEEAKAKKEELE---RLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAkg 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 900 ----------EELRARLTAK-KQELEEIchdlEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVT 968
Cdd:PRK03918 437 kcpvcgreltEEHRKELLEEyTAELKRI----EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 969 TEAKLKKLEEDqiimedqncklAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAmitdLEERLRREEKQRQELEK 1048
Cdd:PRK03918 513 KKYNLEELEKK-----------AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLK 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1049 TRRKLE-GDSTDLSDQIAELQ-------------AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQIS 1114
Cdd:PRK03918 578 ELEELGfESVEELEERLKELEpfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1115 ELQ-EDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLED-----------EAKT 1182
Cdd:PRK03918 658 EEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERveelrekvkkyKALL 737
|
410 420 430
....*....|....*....|....*....|....*..
gi 74180985 1183 HEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAK 1219
Cdd:PRK03918 738 KERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1531-1733 |
3.21e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1531 EQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMA 1610
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1611 ARKKLEMDLKDLEAHIDtaNKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:COG3883 94 ALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74180985 1691 AAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1733
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
958-1421 |
3.40e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 958 ARQKLQLEKvTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAefttnLMEEEEKSKSLAKLKNKHEAMITDLEERLR 1037
Cdd:COG4717 76 LEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1038 REEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQL-AKKEEELQAALARVEEEAAQKNMALKKIRELETQISEL 1116
Cdd:COG4717 150 ELEERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1117 QEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLedeAKTHEAQIQEMRQKHSQ 1196
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1197 AVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVkfsegERVRTELADKVT 1276
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-----EELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1277 KLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDtqellQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLE 1356
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE-----LLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1357 KQIATLHAQVTDMKKKmedgvGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQE 1421
Cdd:COG4717 453 EELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1628-1845 |
3.44e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1628 TANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1708 DEIANSSGKGAL--ALEEKRRLEARIAQLEEELEEEQGNTELINDrLKKANLQIDQINTDLnlershaqknENARQQLER 1785
Cdd:COG3883 93 RALYRSGGSVSYldVLLGSESFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAEL----------EAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1786 QNKELKAKLQEMESAvKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLK 1845
Cdd:COG3883 162 LKAELEAAKAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1666-1910 |
3.98e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1666 AQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDeladeIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNT 1745
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1746 ELINDRLKKANLQIDQINTDLNLershaqknenarQQLERQNKELKAKLQEMESAVKSKYKAsIAALEAKIAQLEEQLDN 1825
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1826 ETKErqaaskqvrrtekklkdVLLQVEDERRNAEQfkdQADKASTRLKQLKRQLEEAEEEAQRAnasrRKLQRELEDATE 1905
Cdd:COG3206 310 EAQR-----------------ILASLEAELEALQA---REASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARE 365
|
....*
gi 74180985 1906 TADAM 1910
Cdd:COG3206 366 LYESL 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1658-1923 |
4.51e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1658 RASREEiLAQAKENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKgalALEEKRRLEARIAQ 1733
Cdd:TIGR02169 173 EKALEE-LEEVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLKEKEA---LERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1734 leeeleeeqgntelINDRLKKANLQIDQINtdlnlERSHAqknenARQQLERQNKELKAKLQEMESAVKSK---YKASIA 1810
Cdd:TIGR02169 249 --------------LEEELEKLTEEISELE-----KRLEE-----IEQLLEELNKKIKDLGEEEQLRVKEKigeLEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1811 ALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRAN 1890
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270
....*....|....*....|....*....|...
gi 74180985 1891 ASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1652-1871 |
6.86e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1652 RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEE--LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1729
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1730 RIAQLEEELEEEQGNTELINDRLkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASI 1809
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRA-----QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1810 AALEAKIAQLEEQLDNETKErqaaSKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTR 1871
Cdd:COG3206 323 EALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
795-1277 |
7.32e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 795 ARKAFAKRQQQLTAMKVLQRNCAAYLRLRN-----------WQWWRLFTKVKPLLNSIRHEDELLAK-EAELTKVREKHL 862
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLWFAQRRLELLEAELEELRAELARlEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 863 AAENRLTEMETMQSQLMAEKL-QLQEQLQAETELCAEAEELRARLTAK----KQELEEICHDLEARVEEEEERCQYLQAE 937
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 938 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQnckLAKEKKLLEDR---VAE----------- 1003
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAElpfVGElievrpeeerw 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1004 ----------FTTNLMEEEEKSKSLAKLKNKHeamitDLEERLRREEKQRQELEKTRRKLEGDStdLSDQIA-ELQAQIA 1072
Cdd:COG4913 477 rgaiervlggFALTLLVPPEHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDPDS--LAGKLDfKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1073 ELKMQLAKK--------EEELQ--------AALARVEEEAAQKNM-------------ALKKIRELETQISELQEDLESE 1123
Cdd:COG4913 550 WLEAELGRRfdyvcvdsPEELRrhpraitrAGQVKGNGTRHEKDDrrrirsryvlgfdNRAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1124 RASRNKAEKQKRDLGEELEALKTELE---DTLDSTAAQQELRSKREQ---------EVSILKKTLED---EAKTHEAQIQ 1188
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAElerldassdDLAALEEQLEEleaELEELEEELD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1189 EMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvkfSEGERVR 1268
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR---ARLNRAE 786
|
....*....
gi 74180985 1269 TELADKVTK 1277
Cdd:COG4913 787 EELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1125 |
7.57e-08 |
|
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: 56.70 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 897 AEAEELRARLTAKKQELEEICHDLEArveeeeercqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL 976
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-----------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 977 EEDQIIMEDQnckLAKEKKLLEDRVAEFTTN-------LMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG4942 89 EKEIAELRAE---LEAQKEELAELLRALYRLgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERA 1125
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
838-1226 |
8.55e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 838 LNSIRHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEic 917
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 918 hdlearveEEEERCQYLQAEKKKMQQNIQELEEqleeeesARQKLQLEKVTTEAKLKKLEEDQIIMEDQNC-KLAKEKKL 996
Cdd:COG4717 189 --------ATEEELQDLAEELEELQQRLAELEE-------ELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 997 LEDRVAEFTTNLMEEEEKSKSLA------------------KLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1058
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1059 -------DLSDQIAELQAQIAEL-----KMQLAKKEEELQAALARV----EEEAAQKNMALKKIRELETQISELQEDLES 1122
Cdd:COG4717 334 lspeellELLDRIEELQELLREAeeleeELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1123 ERASRNK--AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKtledeakthEAQIQEMRQKHSQAVEE 1200
Cdd:COG4717 414 LLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAELLQELEELKAE 484
|
410 420
....*....|....*....|....*....
gi 74180985 1201 LADQLEQTKRVK---ATLEKAKQTLENER 1226
Cdd:COG4717 485 LRELAEEWAALKlalELLEEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1026-1230 |
8.57e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1106 IRELETQISELQEDLESE-------RASR-NKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLE 1177
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldRLSAlSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1178 DEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELA 1230
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
997-1631 |
8.59e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 997 LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITD---LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAE 1073
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1074 LKmQLAKKEEELQAALARVEEeaaQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLD 1153
Cdd:PRK04863 598 LA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL------SQP 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1154 STAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMR---QKHSQAVEELADqleqtkrVKATLEkakqTLENERGEL- 1229
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLSD-------AAEQLA----GLEDCPEDLy 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1230 --ANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSE-------GERVRTELADkvtKLQVELDSVTGLLSQSDSKSSKLT 1300
Cdd:PRK04863 737 liEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpevplfGRAAREKRIE---QLRAEREELAERYATLSFDVQKLQ 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1301 KDFSALESQL---------QDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHA-QVTDMK 1370
Cdd:PRK04863 814 RLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADETLA 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1371 KKMEDGVGCLETAEEAKRRLQKDLEGLSQrleekvaaydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLl 1450
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFVQQHGNALAQ-----------LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL- 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1451 aeektisakyAEERDRAEAEAREKETKALSLARALEEAMEQK-AELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRA 1529
Cdd:PRK04863 962 ----------TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1530 LEQQVEEMKTQLEELedELQATEDAKLRLevnlqamkAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmam 1609
Cdd:PRK04863 1032 KRQMLQELKQELQDL--GVPADSGAEERA--------RARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK----- 1096
|
650 660
....*....|....*....|..
gi 74180985 1610 aaRKKLEMDLKDLEAHIDTANK 1631
Cdd:PRK04863 1097 --LRKLERDYHEMREQVVNAKA 1116
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1522-1720 |
9.19e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQ---FERDLQGRDEQSEEKKKQLVRQVREME--- 1595
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1596 ---------------AELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRAS 1660
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1661 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1720
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1406-1918 |
1.04e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1406 AAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTIsakyAEERDRAEAEAREKETKALSLARAL 1485
Cdd:PRK01156 166 RNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT----LKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1486 EEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR-----------------ALEQQVEEMKTQLEELEDEL 1548
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1549 QATEDAKLRLEVnLQAMKAQFERDLQGRDE---------QSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLemdL 1619
Cdd:PRK01156 322 NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDlnnqileleGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI---L 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1620 KDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEI-------------------LAQAKENE------KK 1674
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELsrnmemlngqsvcpvcgttLGEEKSNHiinhynEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK 1754
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1755 ANLQI-DQINTDLNleRSHAQKN----ENARQQLERQNKELK---AKLQEMESA---VKSKYKASIAALEAKIAQLEEQL 1823
Cdd:PRK01156 558 LKLEDlDSKRTSWL--NALAVISlidiETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1824 dNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:PRK01156 636 -NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
570
....*....|....*
gi 74180985 1904 TETADAMNREVSSLK 1918
Cdd:PRK01156 715 SDRINDINETLESMK 729
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1012-1228 |
1.10e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.14 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALAR 1091
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1092 VEEEAAQknmALKKIRELETQISELQ--EDLESERASRNKAEkqkrdlgEELEALKTELEDTLDSTAAQQELR-SKREQE 1168
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYASVkaHELIEARKRLNKAN-------EKKEKKKKKQKEKQEELKVGDEVKyLSLGQK 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1169 VSILKKTLEDEAkTHEAQIQEMRQKHSQaVEELADQLEQTKRVKATLEKAKQTLENE---RGE 1228
Cdd:PRK00409 652 GEVLSIPDDKEA-IVQAGIMKMKVPLSD-LEKIQKPKKKKKKKPKTVKPKPRTVSLEldlRGM 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1310 |
1.25e-07 |
|
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: 55.93 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1085 LQAALARVEEEAAQKNMALKKIRELE-------TQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAA 1157
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEkelaalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1158 QQELRSKREQEVSILKKTLEDEAKTHE----------AQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERG 1227
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1228 ELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSklTKDFSALE 1307
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP--AAGFAALK 252
|
...
gi 74180985 1308 SQL 1310
Cdd:COG4942 253 GKL 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1053-1287 |
1.39e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1053 LEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR--VEEEAAQKNMALKKIRELETQISELQEDLESERASRNKA 1130
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1131 EKQKRDLGEELEALKteledtldSTAAQQELRSKREQEvsilkktledeakthEAQIQEMRQK---HSQAVEELADQLEQ 1207
Cdd:COG3206 246 RAQLGSGPDALPELL--------QSPVIQQLRAQLAEL---------------EAELAELSARytpNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1208 TKR-VKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRK---KVEAQLQELQVKFSEGERVRTELADKVTKLQVELD 1283
Cdd:COG3206 303 LRAqLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
....
gi 74180985 1284 SVTG 1287
Cdd:COG3206 383 LTVG 386
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1620-1923 |
1.49e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.84 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1620 KDLEAHIDTANKNREeaikqlrkLQAQMKDCMRELDDTRASREEILAQAKENEkklksmeaemiQLQEELAAAERAKRQA 1699
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETE-----------QLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1700 QQERDELADEiANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDL-----NLERSHAQ 1774
Cdd:PRK11281 100 QAELEALKDD-NDEETRETLSTLSLRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQLvslqtQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1775 KNENAR--QQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNET-------KERQAASKQVRRTEKKLK 1845
Cdd:PRK11281 165 LYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllqKQRDYLTARIQRLEHQLQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1846 dvLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANasrRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
897-1335 |
1.57e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 897 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQK----LQLE 965
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqaelNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 966 KVTTEAKLKKLEEDqiimEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLaklknKHEAMitDLEERLRREEKQRQE 1045
Cdd:pfam05557 82 KKYLEALNKKLNEK----ESQLADAREVISCLKNELSELRRQIQRAELELQST-----NSELE--ELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1046 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEE------------ELQAALARVEEEAAQKNMALKKIRELETQI 1113
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaripELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1114 SELQEDLESERASRNKA---EKQKRDLGEELEALKTELEDTLDSTAAQQELRSK------REQEVSILKKTLEDEAKTHE 1184
Cdd:pfam05557 231 EDLKRKLEREEKYREEAatlELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1185 AQIQEMRQKHSQA---VEELADQLEQTKRVKATLEKAKQTLENERG-------------ELANEVKALLQGKGDSEHKRK 1248
Cdd:pfam05557 311 KARRELEQELAQYlkkIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyrailesydkelTMSNYSPQLLERIEEAEDMTQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1249 KVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKltKDFSALESQLQDTQELLQEENRQKLSLS 1328
Cdd:pfam05557 391 KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNELE 468
|
....*..
gi 74180985 1329 TKLKQME 1335
Cdd:pfam05557 469 MELERRC 475
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1010-1324 |
1.64e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 56.83 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1010 EEEEKSKSLAKLKNkheAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAal 1089
Cdd:PLN02939 114 EQQTNSKDGEQLSD---FQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1090 arveeeAAQKNMalkKIRELETQISELQEDLESERASRNKAEKQkrdLGEELEALKTE---LEDtlDSTAAQQELRSKRE 1166
Cdd:PLN02939 189 ------AAQEKI---HVEILEEQLEKLRNELLIRGATEGLCVHS---LSKELDVLKEEnmlLKD--DIQFLKAELIEVAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1167 QEVSILKktLEDEAKTHEAQIQEMRQKHSQAVEELADQleQTKRVKATLEKAkQTLENERGELANEVK---ALLQGKGDS 1243
Cdd:PLN02939 255 TEERVFK--LEKERSLLDASLRELESKFIVAQEDVSKL--SPLQYDCWWEKV-ENLQDLLDRATNQVEkaaLVLDQNQDL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1244 EHKRKKVEAQLQELQV-KFSegervrtelADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENR 1322
Cdd:PLN02939 330 RDKVDKLEASLKEANVsKFS---------SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
..
gi 74180985 1323 QK 1324
Cdd:PLN02939 401 KR 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1317-1888 |
1.86e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1317 LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEA-KRNLEKQIATLHAQVTDM----KKKMEDGVGCLETAEEAkRRLQ 1391
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASAlKRQLDRESDRNQELQKRIrlleKREAEAEEALREQAELN-RLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1392 KDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERD------ 1465
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQnlekqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1466 --RAEAEAREKE--------TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQvE 1535
Cdd:pfam05557 163 ssLAEAEQRIKElefeiqsqEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-E 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1536 EMKTQLEELEDELQATEdAKLRLEVNLQAMKAQFER---DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsmamaar 1612
Cdd:pfam05557 242 KYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1613 KKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSME--AEMIQLQE 1687
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1688 ELAAAERAkrqaqqeRDELADEIANSSGKGALALEekRRLEARIAQLEEELeeeQGNTELINDRLKKANlqidqinTDLN 1767
Cdd:pfam05557 394 AHNEEMEA-------QLSVAEEELGGYKQQAQTLE--RELQALRQQESLAD---PSYSKEEVDSLRRKL-------ETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1768 LERshaqknenarQQLERQNKELKAKLQEMESAVKSKYKASiaaleaKIAQLEEQLDNETKERQAASKQVRRTE-KKLKD 1846
Cdd:pfam05557 455 LER----------QRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQQRKNQLEKLQAEiERLKR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 74180985 1847 VLLQVEDERRNAEQFKDQADK-ASTRLKQLKRQLEEAEEEAQR 1888
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTmNFKEVLDLRKELESAELKNQR 561
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1226 |
2.09e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 844 EDELLAKEAELTKVREKHLAAENRLTEMETMQS--QLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEICHDLE 921
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 922 ARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDR- 1000
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1001 -------VAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQrqeLEKTRRKLEGDSTDLSDQIAELQAQIAE 1073
Cdd:COG4717 251 llliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS---LGKEAEELQALPALEELEEEELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1074 LKMQLAKKEEELQAALARVEEeaaqknmalkkIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1154 STAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENER 1226
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1141-1602 |
2.28e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1141 LEALKTELEDTLDstAAQQELRSKREQEVSILKKTLEDEakthEAQIQEMRQKHSQaVEELADQLEQTKRVKATLEKAKQ 1220
Cdd:COG4717 40 LAFIRAMLLERLE--KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEE-YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1221 TLENERGELANEVKA--LLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELA---DKVTKLQVELDSVTGLLSQSDSK 1295
Cdd:COG4717 113 ELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEeleAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1296 S-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKnsFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKME 1374
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1375 DGVGCLETA-------EEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFD 1447
Cdd:COG4717 271 LILTIAGVLflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1448 QLLAEEKTISAKYAEERDRAEAEAREKETKA------LSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKsvH 1521
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--E 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEE-KKKQLVRQV-REMEAE 1597
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEwAALKLALELlEEAREE 508
|
....*
gi 74180985 1598 LEDER 1602
Cdd:COG4717 509 YREER 513
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
842-1559 |
2.29e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.91 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 842 RHEDELLAKEAELTKVREKHLAAENRLTemetmqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHDLE 921
Cdd:pfam07111 70 RQLQELRRLEEEVRLLRETSLQQKMRLE----------AQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 922 ARVEEEEERCQYLQAEkkkmQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQncklaKEKKLLEDRV 1001
Cdd:pfam07111 136 EGSQRELEEIQRLHQE----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLRKQL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1002 AEfttnLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK 1081
Cdd:pfam07111 207 SK----TQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1082 EEELQ---AALARVEEEAAQKNMALkkIRELETQISELQEDLESERASRNKAEKQKRDLGEELealkteledtldstaaq 1158
Cdd:pfam07111 283 EEELTrkiQPSDSLEPEFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL----------------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1159 QELRSKREQEVSILKKTLEDeaKTHEAQIQEMRQKHSQAveELADQLEQTKRVKATLEKAKQTLENERGELaNEVKALLQ 1238
Cdd:pfam07111 344 QEQVTSQSQEQAILQRALQD--KAAEVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAM-SSTQIWLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1239 GkgdSEHKRKKVEAQLQELQVKFSEGER----VRTELADKVTKLQVELDSvtgllSQSDSKSSKLTKDFSAlesqlqDTQ 1314
Cdd:pfam07111 419 T---TMTRVEQAVARIPSLSNRLSYAVRkvhtIKGLMARKVALAQLRQES-----CPPPPPAPPVDADLSL------ELE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1315 ELLQEENRQKLSLSTKLKQMEDEKNSFREQ----LEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGV-GCLETAEEA--- 1386
Cdd:pfam07111 485 QLREERNRLDAELQLSAHLIQQEVGRAREQgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARqGQQESTEEAasl 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1387 KRRLQKDLEGLSQRLEEKVAaydkleKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISakyaEERDR 1466
Cdd:pfam07111 565 RQELTQQQEIYGQALQEKVA------EVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN----QELRR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1467 AEAEAREKEtkALSLARALEE----------AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV-- 1534
Cdd:pfam07111 635 LQDEARKEE--GQRLARRVQElerdknlmlaTLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPIPAAVpt 712
|
730 740
....*....|....*....|....*.
gi 74180985 1535 -EEMKTQLEELEDELQATEDAKLRLE 1559
Cdd:pfam07111 713 rESIKGSLTVLLDNLQGLSEAISREE 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1100 |
2.43e-07 |
|
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: 55.16 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 862 LAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKM 941
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 942 QQNIQELEEQLEEEESARQKLQLekvTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKL 1021
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGR---QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1022 KNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKN 1100
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1250-1611 |
2.81e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 55.07 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1250 VEAQLQEL---QVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEenrQKLS 1326
Cdd:pfam19220 36 IEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEE---LRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1327 LSTKLKQMEDEKNsfreQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVA 1406
Cdd:pfam19220 113 LRDKTAQAEALER----QLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1407 AYDKLEKTKTRLQQELDDllvdldhQRQSVSNLEKKqkkfdqlLAEEKTisakyaeERDRAEAEAREK----ETKALSLA 1482
Cdd:pfam19220 189 ELAELTRRLAELETQLDA-------TRARLRALEGQ-------LAAEQA-------ERERAEAQLEEAveahRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1483 RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN- 1561
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERa 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1562 ------LQAMKAQFER------DLQGRDEQS----EEKKKQLVRQVREMEAELEDERKQRSMAMAA 1611
Cdd:pfam19220 328 emltkaLAAKDAALERaeeriaSLSDRIAELtkrfEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
990-1222 |
2.81e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 55.07 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 990 LAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQA 1069
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1070 QIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQ-------ISELQEDLESERASRNKAEKQkrdLGEELE 1142
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQldatrarLRALEGQLAAEQAERERAEAQ---LEEAVE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1143 ALKTELE------DTLDSTAAQ-----QELRSK---REQEVSILKKTLED---EAKTHEAQIQEMRQKHSQAVEELADql 1205
Cdd:pfam19220 238 AHRAERAslrmklEALTARAAAteqllAEARNQlrdRDEAIRAAERRLKEasiERDTLERRLAGLEADLERRTQQFQE-- 315
|
250
....*....|....*..
gi 74180985 1206 eqTKRVKATLEKAKQTL 1222
Cdd:pfam19220 316 --MQRARAELEERAEML 330
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1061-1328 |
2.81e-07 |
|
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: 55.16 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1061 SDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEE 1140
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1141 LEALKTELEDTLDstAAQqelRSKREQEVSILKKTledeakTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQ 1220
Cdd:COG4942 99 LEAQKEELAELLR--ALY---RLGRQPPLALLLSP------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1221 TLEnergelanevkallqgkgdsehkrkkveAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLT 1300
Cdd:COG4942 168 ELE----------------------------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|....*...
gi 74180985 1301 KDFSALESQLQDTQELLQEENRQKLSLS 1328
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1063-1239 |
2.94e-07 |
|
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: 53.39 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEeaaqknmALKKIRELETQISELQEDLESERASRNKAEKQKRDLG--EE 1140
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEA-------AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1141 LEALKTELEdtldstaaQQELRskreqevsilKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQ 1220
Cdd:COG1579 91 YEALQKEIE--------SLKRR----------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170
....*....|....*....
gi 74180985 1221 TLENERGELANEVKALLQG 1239
Cdd:COG1579 153 ELEAELEELEAEREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1102-1922 |
3.02e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1102 ALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKT------ELEDTLDSTAAQQElrskREQEVSILKKT 1175
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLE----SSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1176 LEDEAKTHEAQIQEMRQKhsqaVEELADQLEQTKRVKATLEKAKQTLENER-------GELANEVKALLQGKGDS-EHKR 1247
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSK----IMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtDEQLNDLYHNHQRTVREkEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1248 KKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVtgllsQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL 1327
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH-----QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1328 STKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEA---KRRLQKDLEGLSQRLEEK 1404
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1405 VAAYDKLEKTKTRLQQElddllvdldhqrqsvSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKET--KALSLA 1482
Cdd:TIGR00606 477 DQELRKAERELSKAEKN---------------SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1483 RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNL 1562
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1563 QAMKAQFERDLQGRDEQSEekkkqlvrqVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRK 1642
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESD---------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1643 LQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalalE 1722
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ----------R 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1723 EKRRLEARIAQLEEELEEEQGNTELINDrlkKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVK 1802
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEESAKVCLTD---VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1803 skykasiaaleaKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEA 1882
Cdd:TIGR00606 840 ------------TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 74180985 1883 EEEAQRANASRRKLQRELEDATETADAMNR----EVSSLKNKLR 1922
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEELISSKETSNKkaqdKVNDIKEKVK 951
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1383-1923 |
3.23e-07 |
|
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: 55.75 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1383 AEEAKRRLQKDLEGLSQRLEEKVAAYDKL-EKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYA 1461
Cdd:pfam02463 206 AKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1462 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1542 EELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEqsEEKKKQLVRQVREMEAELEDERKQRsmamaARKKLEMDLKD 1621
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE--EEKEAQLLLELARQLEDLLKEEKKE-----ELEILEEEEES 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1622 LEAHIDTANKNREEAIKQLRKLqaQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIqLQEELAAAERAKRQAQQ 1701
Cdd:pfam02463 439 IELKQGKLTEEKEELEKQELKL--LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER-SQKESKARSGLKVLLAL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1702 ERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQ 1781
Cdd:pfam02463 516 IKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1782 QLE-----RQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERR 1856
Cdd:pfam02463 596 VLEidpilNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1857 NAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
842-1644 |
3.37e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 842 RHEDELLAKEAELTKVREKHLAAENRLTEMetmqsqlmAEKLQLQEQLQA--ETELCAEAEELRARLTAKKQ-------- 911
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEM--------ARELEELSARESdlEQDYQAASDHLNLVQTALRQqekieryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 912 -ELEEICHDLEAR---VEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMedQN 987
Cdd:COG3096 354 eDLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC--GL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 988 CKLAKEKklLEDRVAEFTtnlmeeeekskslAKLKNKHEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAEL 1067
Cdd:COG3096 432 PDLTPEN--AEDYLAAFR-------------AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1068 QAQiaelkmQLAKKEEELQAALARVEEEAAQknmalkkIRELEtQISELQEDLESERASRNKAEKQKRDLGEELEALKTE 1147
Cdd:COG3096 496 TAR------ELLRRYRSQQALAQRLQQLRAQ-------LAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1148 LEDTLDStaAQQELRSKREQevsilKKTLEDEAKTHEAQIQEMRQKH------SQAVEELADQLEQT-KRVKATLEKAKQ 1220
Cdd:COG3096 562 LEAQLEE--LEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEAlADSQEVTAAMQQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1221 TLENERG-------------ELANEVKALLQGKG--DSEHKRKK------------------------------------ 1249
Cdd:COG3096 635 LLEREREatverdelaarkqALESQIERLSQPGGaeDPRLLALAerlggvllseiyddvtledapyfsalygparhaivv 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1250 -----VEAQLQELQ-----VKFSEGE--------RVRTELADKVT-----------------------------KLQVEL 1282
Cdd:COG3096 715 pdlsaVKEQLAGLEdcpedLYLIEGDpdsfddsvFDAEELEDAVVvklsdrqwrysrfpevplfgraarekrleELRAER 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1283 DSVTGLLSQSD---SKSSKLTKDFSALESQ------LQDTQELLQEENRQklslstkLKQMEDEKNSFREQLEEEEEAKR 1353
Cdd:COG3096 795 DELAEQYAKASfdvQKLQRLHQAFSQFVGGhlavafAPDPEAELAALRQR-------RSELERELAQHRAQEQQLRQQLD 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1354 NLEKQIATLHAQV--------TDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQrLEEKVAAYDKLEKTKTRLQQELDDL 1425
Cdd:COG3096 868 QLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEAQAFIQQHGKALAQ-LEPLVAVLQSDPEQFEQLQADYLQA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1426 LVDLDHQRQSVSNLEkkqkkfdqllaeektisakyaEERDRAEAEAREKETKALSLARALEEAMEQK---AELERLnkQF 1502
Cdd:COG3096 947 KEQQRRLKQQIFALS---------------------EVVQRRPHFSYEDAVGLLGENSDLNEKLRARleqAEEARR--EA 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1503 RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQATEDAKLRLEVNLQAMKAQFERDLQGRDE---- 1578
Cdd:COG3096 1004 REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQlekq 1081
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1579 --QSEEKKKQLVRQVREMEAELEDERKQ---------RSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQ 1644
Cdd:COG3096 1082 ltRCEAEMDSLQKRLRKAERDYKQEREQvvqakagwcAVLRLARDNDVERRLHRRELAYLSADELRSMSDKALGALR 1158
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1026-1826 |
3.72e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.83 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1026 EAMITDLEERLRREEKQRQELEKTRRKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARV 1092
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDY 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1093 EEEAAQKNMALKKIRELETQISElQEDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVsil 1172
Cdd:TIGR01612 775 AKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM--- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1173 kKTLEDEAKTHEAQIQEMRQKHSQAVEELADQL-EQTKRVKATLEKAKQTLE----NERGELANEVKALLQGKGDSEHKR 1247
Cdd:TIGR01612 838 -KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1248 KKVEAQLQELQVKFSEGERVRtelaDKVTKLQVELDSVTGLLSQSDS---------------KSSKLTKDFS--ALESQL 1310
Cdd:TIGR01612 917 KKVDEYIKICENTKESIEKFH----NKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1311 QDTQELLQEENRQKLSLSTklkqmeDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVgcLETAEEAKRRL 1390
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEI 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1391 QKDLEGLSQRLEEKVAAydklektktrlqqelddllvdldhqrqSVSNLEKKQKK-----FDQLLAEEktiSAKYAEERD 1465
Cdd:TIGR01612 1065 GKNIELLNKEILEEAEI---------------------------NITNFNEIKEKlkhynFDDFGKEE---NIKYADEIN 1114
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1466 RAeaeareketkalslaraleeameqKAELERLNKQfrtemedlmsskddVGKSVHELEKSKRALEQQVEEMKTQLEELE 1545
Cdd:TIGR01612 1115 KI------------------------KDDIKNLDQK--------------IDHHIKALEEIKKKSENYIDEIKAQINDLE 1156
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1546 DELQAT---EDAKlRLEVNLQAMKAQFERDLQGRDEQseekkKQLVRQVREMEAELEDERKQRSMAMAARKKLEmdlKDL 1622
Cdd:TIGR01612 1157 DVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEI-----KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLF 1227
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1623 EAHIDTANKNREEAIKQLRKLqaqmkdcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEelaaaERAKRQAQQE 1702
Cdd:TIGR01612 1228 LEKIDEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD-----DKDHHIISKK 1295
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1703 RDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK-AN----LQIDQINTDLNLERSHAQKne 1777
Cdd:TIGR01612 1296 HDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEiANiyniLKLNKIKKIIDEVKEYTKE-- 1373
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 74180985 1778 narqqLERQNKELKAKLQEMESAVKsKYKASIAALEAKiAQLEEQLDNE 1826
Cdd:TIGR01612 1374 -----IEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SKIESTLDDK 1415
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1272-1497 |
4.21e-07 |
|
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: 54.38 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1272 ADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEA 1351
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1352 KRNLEKQIATLHAQVTDMKKkmEDGVGCL---ETAEEAKRRLQkDLEGLSQRLEEKVaayDKLEKTKTRLQQELDDLLVD 1428
Cdd:COG4942 99 LEAQKEELAELLRALYRLGR--QPPLALLlspEDFLDAVRRLQ-YLKYLAPARREQA---EELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1429 LDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1497
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1032-1226 |
4.53e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1032 LEERLrreEKQRQELEKTRRKLEG-----DSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKI 1106
Cdd:COG3206 180 LEEQL---PELRKELEEAEAALEEfrqknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1107 REL--ETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELedtldstaaqQELRSKREQEVSILKKTLEDEAKTHE 1184
Cdd:COG3206 257 PELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI----------AALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74180985 1185 AQIQEMRQKhsqaVEELADQLEQTKRVKATLEKAKQTLENER 1226
Cdd:COG3206 327 AREASLQAQ----LAQLEARLAELPELEAELRRLEREVEVAR 364
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1466-1879 |
5.91e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1466 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1521
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrqqekIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1587
Cdd:PRK04863 356 DLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAvQALERAKQLcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1588 -VRQVREMEAELEDERKQRSMAM-AARKKLEMDlkdleahiDTANKNREEAIKQLRKLQAQMkdcmrelddtraSREEIL 1665
Cdd:PRK04863 436 tADNAEDWLEEFQAKEQEATEELlSLEQKLSVA--------QAAHSQFEQAYQLVRKIAGEV------------SRSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1666 AQAKENEKKLKSMEAEMIQLQE---ELAAAERAKRQaQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEeleeeq 1742
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQlrmRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE------ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1743 gntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKAKLQEMEsavkSKYKASIAALEAkIAQLEEQ 1822
Cdd:PRK04863 569 ----------------------SLSESVSEARER---RMALRQQLEQLQARIQRLA----ARAPAWLAAQDA-LARLREQ 618
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1823 LDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKAS-------TRLKQLKRQL 1879
Cdd:PRK04863 619 SGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedPRLNALAERF 682
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1026-1160 |
5.96e-07 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 54.09 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1026 EAMITDLEERLRRE--EKQRQELEKTRRKLEGDSTDLSD------------QIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1092 VEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQkrdlgEELEALKTEL---EDTLDSTAAQQE 1160
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
909-1260 |
6.70e-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: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 909 KKQELEEICHDLEARVEEEEERCQYLQAEKKKmqqniqeleeqleeeesarqklqlekvtteaklkkleedQIIMEDQNC 988
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKAR---------------------------------------QAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 989 KLAKEKKLLEDRVAEFttNLMEEEEKSKSLAKLKNKHEAM----ITDLE----ERLRREEKQRQELEKTRRKlegdSTDL 1060
Cdd:pfam17380 335 IYAEQERMAMEREREL--ERIRQEERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKV----KILE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1061 SDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKIREletqiSELQEDLESERASRNKAEKQKRDLGEE 1140
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE---MERVRL-----EEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1141 LEALKTELEDTLDSTAAQQELRSKREQ--EVSILKKTLEDEAKTHEAQIQEmRQKHSQAVEELADQLEQTKRVKATLEKA 1218
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYE-EERRREAEEERRKQQEMEERRRIQEQMR 559
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 74180985 1219 KQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVK 1260
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
899-1287 |
9.72e-07 |
|
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: 53.75 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 899 AEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQqniqeleEQLEEEESARQKLQLEKVTTEAKLKKLEE 978
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE-------RQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 979 DQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1058
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1059 DLSDQIAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLG 1138
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVL----QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1139 EELEALKTELEDTldstaaQQELRSKREQ--EVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEqtkRVKATLE 1216
Cdd:pfam07888 258 EELSSMAAQRDRT------QAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIE---KLSAELQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1217 KAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQE----LQVKFSEGERVRT---ELADKVTKLQVELDSVTG 1287
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKEQLQAekqELLEYIRQLEQRLETVAD 406
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
881-1525 |
1.00e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 881 EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKK--------------MQQNIQ 946
Cdd:pfam10174 68 ENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERqakelfllrktleeMELRIE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 947 ELEEQLEEEESARQKLqLEKVTTEAKLKKLEEDQ-------IIMEDQNCKL-----AKEKKLLEDRVAEFTTN-LMEEEE 1013
Cdd:pfam10174 148 TQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEDwertrriAEAEMQLGHLevlldQKEKENIHLREELHRRNqLQPDPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1014 KSKSLAKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQA----------QIAELKMQLAKKEE 1083
Cdd:pfam10174 227 KTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKES 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1084 ELQAALARVEE------------EAAQKNMALKKIRE--LETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELE 1149
Cdd:pfam10174 304 ELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1150 DTLDstaaqqeLRSKREQEVSILKKTLE---DEAKTHEAQIQEMRqkhsQAVEELADQLEQTKRVKATLEKA----KQTL 1222
Cdd:pfam10174 384 DLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLK----ERVKSLQTDSSNTDTALTTLEEAlsekERII 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1223 ENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKD 1302
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1303 FSALESQLQDTQElLQEENRQKLSLSTKLKQMEDEKNSFREQ--------------LEEEEEAKRNLEKQIATLHAQVTD 1368
Cdd:pfam10174 533 CSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEEsgkaqaeverllgiLREVENEKNDKDKKIAELESLTLR 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1369 MKKKMEDGVGCLETAEEAKRRlqkdleGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDhqRQSVSNLEKKQKKFDQ 1448
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKK------KGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQQ 683
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1449 LLAEEKTISAKYAEERDRAEAEAREKETKALsLArALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEK 1525
Cdd:pfam10174 684 SLAEKDGHLTNLRAERRKQLEEILEMKQEAL-LA-AISEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1018-1152 |
1.11e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1018 LAKLKNKHEAmiTDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEE 1094
Cdd:COG2433 382 LEELIEKELP--EEEPEAEREKEHEERELTEEEEEIR----RLEEQVERLEAEVEELEAELEEKDeriERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1095 EAAQKNMALKKIRELETQISELQEDLESErasRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1052-1662 |
1.26e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1052 KLEGDSTDLSDQIAELQAQIAE---LKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQIselqedleserasrN 1128
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNidyLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY--------------N 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1129 KAEKQKRDLGEELEALKTeledtldstaaqqelrskreqevsilkktLEDEAKTHEAQIQEMRQKhsqaveeLADQLEQT 1208
Cdd:PRK01156 229 NAMDDYNNLKSALNELSS-----------------------------LEDMKNRYESEIKTAESD-------LSMELEKN 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1209 KRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvKFSEGERVRTELA---DKVTKLQVELDSV 1285
Cdd:PRK01156 273 NYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEIN-KYHAIIKKLSVLQkdyNDYIKKKSRYDDL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1286 TGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ 1365
Cdd:PRK01156 352 NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQR 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1366 VTDMKKKMED--------------GVGCLETAEEAKRRLQKDLEGLSQRLEEKVaayDKLEKTKTRLQQELDdllvdldH 1431
Cdd:PRK01156 432 IRALRENLDElsrnmemlngqsvcPVCGTTLGEEKSNHIINHYNEKKSRLEEKI---REIEIEVKDIDEKIV-------D 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1432 QRQSVSNLEKKqkKFDQLLAEEKTISAKYAEERD--RAEAEAREKETKALSLARALE----EAMEQKAE--LERLNKQFR 1503
Cdd:PRK01156 502 LKKRKEYLESE--EINKSINEYNKIESARADLEDikIKINELKDKHDKYEEIKNRYKslklEDLDSKRTswLNALAVISL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1504 TEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT----QLEELEDELQATEDAKLRLEVNLQAMKaQFERDLQGRDEQ 1579
Cdd:PRK01156 580 IDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIE-KLRGKIDNYKKQ 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1580 SEEKKKQLVRQ--VREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDT 1657
Cdd:PRK01156 659 IAEIDSIIPDLkeITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL 738
|
....*
gi 74180985 1658 RASRE 1662
Cdd:PRK01156 739 KRLRE 743
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1703 |
1.33e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 873 TMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqylQAEK-KKMQQNIQELEEQ 951
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 952 LEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFtTNLMEEEEKSKSLAKLKNKHEAMITD 1031
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-QQAVQALERAKQLCGLPDLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1032 LEERLRREEKQR-QELEKTRRKLegdstDLSDQIAELQAQIAELKMQLAKKEEELQA------ALARVEEE---AAQKNM 1101
Cdd:PRK04863 443 WLEEFQAKEQEAtEELLSLEQKL-----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvareLLRRLREQrhlAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1102 ALKKIRELEtQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQELRSKREQevsilKKTLEDEAK 1181
Cdd:PRK04863 518 LRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES--LSESVSEARER-----RMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1182 THEAQIQEMRQKHSQ------AVEELADQleqtkrVKATLEKAkQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQ 1255
Cdd:PRK04863 590 QLQARIQRLAARAPAwlaaqdALARLREQ------SGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1256 EL-QVKFSEGERVRTeLADKVTKLQVEL--DSVT--------GLLSQsdSKSSKLTKDFSALESQLQ---DTQE--LLQE 1319
Cdd:PRK04863 663 RLsQPGGSEDPRLNA-LAERFGGVLLSEiyDDVSledapyfsALYGP--ARHAIVVPDLSDAAEQLAgleDCPEdlYLIE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1320 ENRQKL------------SLSTKLKQMEDEKNSFREQLEEEEEAKrnlEKQIATLHAQVTDMKKKmedgvgcLETAEEAK 1387
Cdd:PRK04863 740 GDPDSFddsvfsveelekAVVVKIADRQWRYSRFPEVPLFGRAAR---EKRIEQLRAEREELAER-------YATLSFDV 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1388 RRLQKDLEGLSQRLEEKVA-AYD-----KLEKTKTRLQQ---ELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISA 1458
Cdd:PRK04863 810 QKLQRLHQAFSRFIGSHLAvAFEadpeaELRQLNRRRVElerALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1459 KYAEERdraeaeareketkalslARALEEAMEQKAELERLNKQFrtemedlmsskddvGKSVHELEKSKRAL---EQQVE 1535
Cdd:PRK04863 890 ETLADR-----------------VEEIREQLDEAEEAKRFVQQH--------------GNALAQLEPIVSVLqsdPEQFE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1536 EMKTQLEELEDELQATeDAKLRLEVNLQAMKAQFE-RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKK 1614
Cdd:PRK04863 939 QLKQDYQQAQQTQRDA-KQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1615 LEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELddTRASREEILAQAKEN-------EKKLKSMEAEMIQLQE 1687
Cdd:PRK04863 1018 YNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEER--ARARRDELHARLSANrsrrnqlEKQLTFCEAEMDNLTK 1095
|
890
....*....|....*.
gi 74180985 1688 ELAAAERAKRQAQQER 1703
Cdd:PRK04863 1096 KLRKLERDYHEMREQV 1111
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1353-1900 |
1.62e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1353 RNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLlvdldHQ 1432
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1433 RQSVSNLEKKQKKFDQLLAE----EKTISA---KYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTE 1505
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKaeglEKSLNSletKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1506 MEDLMSS------KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER-------- 1571
Cdd:pfam07111 231 VPPEVHSqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKkcrsllnr 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1572 ----------DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAM------AARKKLE-MDLKDLEAHIDTANKNRE 1634
Cdd:pfam07111 311 wrekvfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQralqdkAAEVEVErMSAKGLQMELSRAQEARR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1635 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM------IQLQEELAAAERAKRQAQQERDELAD 1708
Cdd:pfam07111 391 RQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkVHTIKGLMARKVALAQLRQESCPPPP 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1709 EIANSSGKGALALEEKR----------RLEARIAQLEEELEEEQGNTEliNDRLKKANLQIDQ---------INTDLNLE 1769
Cdd:pfam07111 471 PAPPVDADLSLELEQLReernrldaelQLSAHLIQQEVGRAREQGEAE--RQQLSEVAQQLEQelqraqeslASVGQQLE 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1770 RSHAQKNE------NARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQL-EEQLDNETKERQAASKQVRrtEK 1842
Cdd:pfam07111 549 VARQGQQEsteeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEArREQAKAVVSLRQIQHRATQ--EK 626
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1843 KLKDVLLQVEDERRnaeqfKDQADKASTRLKQLKR-QLEEAEEEAQRANASRRKLQREL 1900
Cdd:pfam07111 627 ERNQELRRLQDEAR-----KEEGQRLARRVQELERdKNLMLATLQQEGLLSRYKQQRLL 680
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1337-1733 |
1.67e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1337 EKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGvgcletaEEAKRRLQKDLEglsqrleekvAAYDKLEKTKT 1416
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEEL-------SARESDLEQDYQ----------AASDHLNLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1417 RLQQELDDLlvdldHQRQSVSNLEKKqkkfdqlLAEEKTISAKYAEERDRAEAEAREKETKALSLARALeeAMEQKA--E 1494
Cdd:COG3096 342 ALRQQEKIE-----RYQEDLEELTER-------LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL--ADYQQAldV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1495 LERLNKQFRtemedlmsskddvgKSVHELEKSKRALEQ---QVEEMKTQLEELEDELQATEDAKLRLEVNL---QAMKAQ 1568
Cdd:COG3096 408 QQTRAIQYQ--------------QAVQALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1569 FERDLQ------GRDEQSE--EKKKQLVRQVRE----------MEAELEDERKQRSMAMAARKKLE----------MDLK 1620
Cdd:COG3096 474 FEKAYElvckiaGEVERSQawQTARELLRRYRSqqalaqrlqqLRAQLAELEQRLRQQQNAERLLEefcqrigqqlDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1621 DLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE------- 1693
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQevtaamq 633
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 74180985 1694 ---RAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQ 1733
Cdd:COG3096 634 qllEREREATVERDELA--------------ARKQALESQIER 662
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1440-1922 |
1.74e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1440 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKEtkalslaraleeamEQKAELERLNKQFRTEmedlmssKDDVGKS 1519
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE--------------ERQETSAELNQLLRTL-------DDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELE 1599
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL----ENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1600 DERKQRSMAMAArkKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMrelddtrasrEEILAQAKENEKKLKSME 1679
Cdd:pfam12128 379 RRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL----------EAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1680 AEMIQLQEELAAAERAKRQ--AQQERDELADEIANSSGKGALALE-EKRRLEARIAQLEEELEEEQGNTELINDRLKKAN 1756
Cdd:pfam12128 447 GELKLRLNQATATPELLLQleNFDERIERAREEQEAANAEVERLQsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1757 LQID-QINTDLNLERSHAQKNEN------ARQQLERQNKE----------------LKAKLQEMESavkSKYKASIAALE 1813
Cdd:pfam12128 527 LQLFpQAGTLLHFLRKEAPDWEQsigkviSPELLHRTDLDpevwdgsvggelnlygVKLDLKRIDV---PEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1814 AKIAQLEEQLDNETKERQAASKQVRRTEKKLkdvllqvederrnaeqfkdqaDKASTRLKQLKRQLEEAEEEAQRANASR 1893
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGEL---------------------EKASREETFARTALKNARLDLRRLFDEK 662
|
490 500 510
....*....|....*....|....*....|
gi 74180985 1894 RKLQRELEDATETA-DAMNREVSSLKNKLR 1922
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLK 692
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1491-1920 |
2.04e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1491 QKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1567
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1568 QFERDLQGRDEQSEEKKKqlvrqvreMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQM 1647
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNK--------LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1648 KDCMRELDDTRASR---EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1724
Cdd:TIGR04523 183 LNIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1725 RRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDQINTDLnlERSHAQKNENARQQLERQNKELKAKLQEMESAVkSK 1804
Cdd:TIGR04523 263 NKIKKQLSEK-------QKELEQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI-SQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1805 YKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVL--------------LQVEDERRNAEQFKDQADKAST 1870
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykqeiknleSQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1871 RLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1065-1330 |
2.11e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1065 AELQAQIAELKmqlakKEEELQAalarvEEEAAQKNmaLKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEAL 1144
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQD--LEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1145 KTELEDTLDSTAAQQELRskreqevsilkkTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLEn 1224
Cdd:PRK11281 107 KDDNDEETRETLSTLSLR------------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1225 ergELANEVKALLQGKGDSEHKRK-KVEAQLQ--ELQVKFSegervRTELADKvTKLQvELdsvtgLLSQSDSKSSKLTK 1301
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQAllNAQNDLQ-----RKSLEGN-TQLQ-DL-----LQKQRDYLTARIQR 238
|
250 260
....*....|....*....|....*....
gi 74180985 1302 dfsaLESQLQDTQELLqeeNRQKLSLSTK 1330
Cdd:PRK11281 239 ----LEHQLQLLQEAI---NSKRLTLSEK 260
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
958-1170 |
2.22e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 958 ARQKLQlekvTTEAKLKKLEEDQIIMEdqnckLAKEKKLLEDRVAEFTT-------NLMEEEEKSKSLAKLKNKHEAMIT 1030
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESqlaearaELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1031 DLEE--RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALARVEEEAAQknmALKKIRE 1108
Cdd:COG3206 258 ELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEA---LQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1109 LETQISELQEDLESErasrNKAEKQKRDLGEELEALKTELEDTLdstAAQQELRSKREQEVS 1170
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1538-1820 |
2.56e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 52.64 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1538 KTQLEELEDELQATEDAKLRLEvnlqAMKAQFERDLQGRdeqsEEKKKQLVRQVRemeAELEDERkQRSMAMAARKKLEM 1617
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----ARQARLEREKAAR----EARHKKAAEARA---AKDKDAV-AAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1618 DLKDLEAHIDTANKNREEAIKQLRKLQAqmkdcmrelddtRASREEILAQAKENEKKLKsmeaemIQlqeelAAAERAK- 1696
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAADPKKAA------VA-----AAIARAKa 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1697 RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQLEEELEEEQGNTELINDR------------LKKANLQIDQINT 1764
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVA-AAIARAKAKKAAQQAASAEPEEQVAEVDPKkaavaaaiarakAKKAEQQANAEPE 638
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1765 DLNLERSHAQKNENARqqlerqNKELKAKLQEMESAVKSKYKASIAALEAKIAQLE 1820
Cdd:PRK05035 639 EPVDPRKAAVAAAIAR------AKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
963-1345 |
2.60e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.27 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 963 QLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ 1042
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1043 RQELEKTRRKLEgdstdlsdqiaelQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkiRELETQISELQEDLES 1122
Cdd:COG5185 305 IDIKKATESLEE-------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQ------ESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1123 ERASRNKAEKQkrdlgEELEALKTELEDTLDSTAAQQELRSKREQEvsiLKKTLEDEAKTHEAQIQEMRQkhsqaveela 1202
Cdd:COG5185 366 IVGEVELSKSS-----EELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQR---------- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1203 dQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQlQELQVKFSEGERVRTELADKVTKLQVEL 1282
Cdd:COG5185 428 -QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVR-SKKEDLNEELTQIESRVSTLKATLEKLR 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1283 DSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLK-----QMEDEKNSFREQL 1345
Cdd:COG5185 506 AKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNaktdgQAANLRTAVIDEL 573
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1130 |
3.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDqiiMEDQNCKLAKEKKLLEDRVAEF-----TTNL 1008
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1009 MEEEEKSKSLA----------KLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG3883 105 LDVLLGSESFSdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1079 AKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKA 1130
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1432-1800 |
3.36e-06 |
|
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: 52.05 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1432 QRQSVSNLEKKQKKFDqllaeektisaKYAEERDRAEAEAREKEtkalslaraleeaMEQKAELERLNKQFRTEMEDlms 1511
Cdd:pfam17380 279 QHQKAVSERQQQEKFE-----------KMEQERLRQEKEEKARE-------------VERRRKLEEAEKARQAEMDR--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1512 skddvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnlqAMKAQFERDLQgRDEQSEEKKKQLVRQv 1591
Cdd:pfam17380 332 ------QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-------AMEISRMRELE-RLQMERQQKNERVRQ- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1592 remeaELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1671
Cdd:pfam17380 397 -----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1672 EKKLKSmeaemiqlqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRR-LEARIAQLEEELEEEQGNTELIND 1750
Cdd:pfam17380 472 RKRKKL----------ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1751 RLKKANL----QIDQINTDLNLERSHAQKNENARQQLeRQNKELKAKLQEMESA 1800
Cdd:pfam17380 542 RRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1044-1362 |
4.54e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1044 QELEKTRRKLegdstdlsDQIAELQAQIAELKMQLAKKEEELQ------AALARVEEEAAQKNMALKKIRELETQISELQ 1117
Cdd:PRK11281 63 QDLEQTLALL--------DKIDRQKEETEQLKQQLAQAPAKLRqaqaelEALKDDNDEETRETLSTLSLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1118 EDLESERASRNKAEKQkrdlgeeLEALKTELEDtldstaAQQEL--RSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHS 1195
Cdd:PRK11281 135 DQLQNAQNDLAEYNSQ-------LVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1196 QAVEELADQLEQTKRVKATLekakQTLENERGELANEVKALLQgkgdsehkrkkveAQLQELQVKFSEGERVRTElaDKV 1275
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTARIQRLE-------------HQLQLLQEAINSKRLTLSE--KTV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1276 TKLQveldsvtgllsqsdsksskltkdfSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSF-------REQLEEE 1348
Cdd:PRK11281 263 QEAQ------------------------SQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLtqqnlrvKNWLDRL 318
|
330
....*....|....
gi 74180985 1349 EEAKRNLEKQIATL 1362
Cdd:PRK11281 319 TQSERNIKEQISVL 332
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1137-1524 |
4.80e-06 |
|
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: 51.43 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1137 LGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATle 1216
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1217 kakqtleneRGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKL-------QVELDSVTGLL 1289
Cdd:pfam07888 110 ---------SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1290 SQSDSKSSKLTKDFSALESQL--QDTQEL-LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQV 1366
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLaqRDTQVLqLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1367 TDMKKKMEDGVgcletAEEAKRRLQkdLEGLSQRLEEKVAAydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKF 1446
Cdd:pfam07888 261 SSMAAQRDRTQ-----AELHQARLQ--AAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRL 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1447 DQLLAEEKTisakyaeERDRAEAE-AREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELE 1524
Cdd:pfam07888 331 EERLQEERM-------EREKLEVElGREKDCNRVQLSESRRELQELKASLRVAQK----EKEQLQAEKQELLEYIRQLE 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1314 |
4.88e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1088 ALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQ 1167
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1168 evsiLKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKR 1247
Cdd:COG3883 88 ----LGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1248 KKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQ 1314
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1224 |
4.94e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 864 AENRLTEMETMQSQLMAEKLQLQEQLQAETElcaeaEELRARLTAKKQELEEICHDL---EARVEEEEERCQYLQAEKKK 940
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDWN-----KELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 941 MQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAK 1020
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1021 LKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQaALARVEEEAAQKN 1100
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-KLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1101 MALKK---------------IRELETQISELQEDLES--ERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRS 1163
Cdd:TIGR04523 513 KDLTKkisslkekiekleseKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1164 KREQEVSILKKTLEdeakTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLEN 1224
Cdd:TIGR04523 593 QKEKEKKDLIKEIE----EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1251-1918 |
5.33e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.75 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1251 EAQLQELQvkfSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQklsLSTK 1330
Cdd:pfam10174 2 QAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQH---LQLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1331 LKQMEDEKnsfreqleeeeEAKRNLEKqiaTLHAQVTDMKKKMEDGVGCLETAEEAKRRLQ-------KDLEGLSQRLEE 1403
Cdd:pfam10174 76 IQALQDEL-----------RAQRDLNQ---LLQQDFTTSPVDGEDKFSTPELTEENFRRLQseherqaKELFLLRKTLEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1404 K-----------VAAYDKLEKTKTRLQQELDDLLVDLDHQ--RQSVSNLEKKQKKFDQLLAEEKTISAKYAEE-RDRAEA 1469
Cdd:pfam10174 142 MelrietqkqtlGARDESIKKLLEMLQSKGLPKKSGEEDWerTRRIAEAEMQLGHLEVLLDQKEKENIHLREElHRRNQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1470 EAREKETKALslaRALEEAMEQK-AELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDEL 1548
Cdd:pfam10174 222 QPDPAKTKAL---QTVIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1549 QATEDAKLRLEVNLQAMKAQFERDLQGRD--EQSEEKKKQ-----------LVRQVREMEAELEDERKQRSMAMAARKKL 1615
Cdd:pfam10174 299 SKKESELLALQTKLETLTNQNSDCKQHIEvlKESLTAKEQraailqtevdaLRLRLEEKESFLNKKTKQLQDLTEEKSTL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1616 EMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAemiQLQEELAAAERA 1695
Cdd:pfam10174 379 AGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE---ALSEKERIIERL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1696 KRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQK 1775
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1776 NENARQqlerqnkelKAKLQEMESAVKSKYKASIAALEAKIAQLEEqldnetkERQAASKQVRRtekkLKDVLLQVEDER 1855
Cdd:pfam10174 536 LENQLK---------KAHNAEEAVRTNPEINDRIRLLEQEVARYKE-------ESGKAQAEVER----LLGILREVENEK 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1856 RNAEqfKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1918
Cdd:pfam10174 596 NDKD--KKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1462-1704 |
5.38e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1462 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1542 EELEDELQATEDAKLRLEvNLQAMKAQFERDLQGRDeQSEEKKKQLVRQVREMEAELEDERKQRsmamaarkKLEMDLKD 1621
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKAL--------EKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1622 LEAHIDTANKNREEAIKQLRKLQ-------AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL----- 1689
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELrelrk 244
|
250 260
....*....|....*....|....
gi 74180985 1690 ---------AAAERAKRQAQQERD 1704
Cdd:COG1340 245 elkklrkkqRALKREKEKEELEEK 268
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1466-1874 |
6.01e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1466 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1521
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDleqdyqaasdhlnlvqtalrqqekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1587
Cdd:COG3096 355 DLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQYQQAvQALEKARALcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1588 -VRQVREMEAELEDERKQrsmAMAARKKLEMDLKDLEAHidtanKNR-EEAIKQLRKLQAQMkdcmrELDDTRASREEIL 1665
Cdd:COG3096 435 tPENAEDYLAAFRAKEQQ---ATEEVLELEQKLSVADAA-----RRQfEKAYELVCKIAGEV-----ERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1666 AQAKEnekkLKSMEAEMIQLQEELAAAERAKRQaQQERDELADEIANSSGK---GALALEE-KRRLEARIAqleeeleee 1741
Cdd:COG3096 502 RRYRS----QQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQqldAAEELEElLAELEAQLE--------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1742 qgntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKAKLQEMEsavkSKYKASIAALEAkIAQLEE 1821
Cdd:COG3096 568 -----------------------ELEEQAAEAVEQ---RSELRQQLEQLRARIKELA----ARAPAWLAAQDA-LERLRE 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1822 QLDNETKERQAASKQVRRTEKKLKdvllQVEDERRNAEQFKDQADKASTRLKQ 1874
Cdd:COG3096 617 QSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQALESQIERLSQ 665
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1433-1755 |
6.14e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.84 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1433 RQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLN---KQFRTEMEDL 1509
Cdd:pfam19220 44 PQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielRDKTAQAEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1510 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER------DLQGRDEQSEEK 1583
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1584 KKQLVRQVREMEAELEDERKQRSMAMAA-----------RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMR 1652
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1653 ELDDTRASReeilaqaKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIA 1732
Cdd:pfam19220 284 RLKEASIER-------DTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIA 356
|
330 340
....*....|....*....|...
gi 74180985 1733 QLEEELEEEQGNTELINDRLKKA 1755
Cdd:pfam19220 357 ELTKRFEVERAALEQANRRLKEE 379
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1456-1657 |
6.21e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1456 ISAKYAEERDRAEAEAREkeTKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksvhELEKSKRALEQQVE 1535
Cdd:COG2433 355 VEKKVPPDVDRDEVKARV--IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELT---------EEEEEIRRLEEQVE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1536 EMKTQLEELEDELQATEDAKLRLEvnlqaMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmamaARKKL 1615
Cdd:COG2433 424 RLEAEVEELEAELEEKDERIERLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERE-------RIEEL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74180985 1616 EMDLKDLEAHIDTANKNREEAIKQLRKLQaqmKDCMRELDDT 1657
Cdd:COG2433 492 KRKLERLKELWKLEHSGELVPVKVVEKFT---KEAIRRLEEE 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1010-1225 |
6.34e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1010 EEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:COG3883 17 QIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1090 ARVEE------------------EAAQKNMALKKIRELETQ-ISELQEDLESERASRNKAEKQKrdlgEELEALKTELED 1150
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKL----AELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1151 TLDSTAAQQElrskreqEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENE 1225
Cdd:COG3883 169 AKAELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1522-1683 |
6.76e-06 |
|
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: 49.54 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDlqgrDEQSEEKKKQlvRQVREMEAELEDE 1601
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY----EEQLGNVRNN--KEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1602 RKQRSmamaarkklemdlkDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAE 1681
Cdd:COG1579 102 KRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
..
gi 74180985 1682 MI 1683
Cdd:COG1579 168 LA 169
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1578-1733 |
6.85e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.05 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQ-----LRKLQAQMKDCMR 1652
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1653 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSSGKGALALEEkrRLEARIA 1732
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL-KARAKAAKAQEKVNEALSGIDSDDATSALE--RMEEKIE 175
|
.
gi 74180985 1733 Q 1733
Cdd:COG1842 176 E 176
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1618-1712 |
7.13e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 50.84 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1618 DLKDLEAHIDT-----ANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEI---LAQAKENEKKLKSMEAEMIQLQEEL 1689
Cdd:PRK05431 3 DIKLIRENPEAvkealAKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 74180985 1690 AAAERAKRQAQQERDELADEIAN 1712
Cdd:PRK05431 83 KALEAELDELEAELEELLLRIPN 105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
846-1375 |
7.36e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 846 ELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAEtelCAEAEELRARLTAKKQELEEichdlearve 925
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE---LENLEERLKALTGKHQDVTA---------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 926 eeeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEED-QIIMEDQNCKLAKEKKLLEDRVAEF 1004
Cdd:pfam12128 376 ------KYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1005 TTNLMEEEEKSKSLAKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ-------IAELQAQIAELKMQ 1077
Cdd:pfam12128 450 KLRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQASEAlrqasrrLEERQSALDELELQ 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1078 LAKKEEELQAALAR---------------------------VEEEAAQK------NMALKKI---------RELETQISE 1115
Cdd:pfam12128 529 LFPQAGTLLHFLRKeapdweqsigkvispellhrtdldpevWDGSVGGElnlygvKLDLKRIdvpewaaseEELRERLDK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1116 LQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL----DSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMR 1191
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1192 QKHSQAVEELADQLEQTKRVKATLEKAKQTLENE-RGELANEVKALLQGKGDSEHKRKkveAQLQELQVKFSEGERVRTE 1270
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVvEGALDAQLALLKAAIAARRSGAK---AELKALETWYKRDLASLGV 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1271 LADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQL----QDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLE 1346
Cdd:pfam12128 766 DPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE 845
|
570 580
....*....|....*....|....*....
gi 74180985 1347 EEEEAKRNLEKQIATLHAQVTDMKKKMED 1375
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
993-1218 |
7.64e-06 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 51.47 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 993 EKKLLEDRvaeftTNLMEEEEKSKSLAklknkhEAMITDLEERLRREEKQRQELEKTRR-----------KLEGDSTDLs 1061
Cdd:PLN03188 1046 EKKLEQER-----LRWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1062 DQIAELQaqiaELKMQLAKKEEELQAALARVEEEAAQ---KNMALKKIRELETQISELQedleSERasrnkaEKQKRDLG 1138
Cdd:PLN03188 1114 EQYADLE----EKHIQLLARHRRIQEGIDDVKKAAARagvRGAESKFINALAAEISALK----VER------EKERRYLR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1139 EELEALKTELEDTLDSTAAQQEL--RSKREQEVSIL--KKTLEDEAKTHEA--QIQEMRQKHSQAVEELADQLEQTKRVK 1212
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEALTVaqKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPK 1259
|
....*.
gi 74180985 1213 ATLEKA 1218
Cdd:PLN03188 1260 EAIRPA 1265
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1009-1275 |
9.39e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1009 MEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1089 LARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELedtldsTAAQQELRSKREQE 1168
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------AEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1169 VSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRK 1248
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260
....*....|....*....|....*..
gi 74180985 1249 KVEAQLQELQVKFSEGERVRTELADKV 1275
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELA 266
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1026-1709 |
1.21e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.59 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1026 EAMITDLEERLRREEKQRQE-LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakKEEELQAALARvEEEAAQKNMALK 1104
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL--REETERAIAAR-QAEAAEELTRLH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1105 KirELETQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE------------------------ 1160
Cdd:NF041483 582 T--EAEERLTAAEEAL---ADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaaadasaaraegenv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1161 ---LRSKREQEVSILKKTLEDEAKTHEAQIQEMRQK-HSQAVEELADQLEQTKR----VKATLEKAKQTLENERGELANE 1232
Cdd:NF041483 657 avrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvGTEAAEALAAAQEEAARrrreAEETLGSARAEADQERERAREQ 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1233 VKALLQGkgdsehKRKKVEAQLQELQVKFSEGERVRTEL--ADKVTKLQVElDSVTGLLSQSDSKSSKLTkdfSALESQL 1310
Cdd:NF041483 737 SEELLAS------ARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQVR-DSVAGLQEQAEEEIAGLR---SAAEHAA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1311 QDTQELLQEE-NRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIAT--------LHAQVTDMKKKME-DGVGCL 1380
Cdd:NF041483 807 ERTRTEAQEEaDRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSeaiaeaerLRSDASEYAQRVRtEASDTL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAY-DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAK 1459
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRSDAAAQaDRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1460 YAE-ERDRAEAeareketkALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVheLEKSKRALEQQVEEMK 1538
Cdd:NF041483 967 TGEaERLRAEA--------AETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRT--LDEARKDANKRRSEAA 1036
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1539 TQLEELEDElQATEDAKLRLEVNLQAMKAQFERDLQGrDEQSEEKKKQLVRQVREMEAE----LEDERKQ--------RS 1606
Cdd:NF041483 1037 EQADTLITE-AAAEADQLTAKAQEEALRTTTEAEAQA-DTMVGAARKEAERIVAEATVEgnslVEKARTDadellvgaRR 1114
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1607 MAMAARKKLEMDLKDLEAHIDTAN-KNREEAIKQLR----KLQAQMKDCMRELDDTRASREEILAQA------------K 1669
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHeRARRESAEQMKsageRCDALVKAAEEQLAEAEAKAKELVSDAnseaskvriaavK 1194
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 74180985 1670 ENEKKLKSMEAEMIQLQEElaaAERAKRQAQQERDELADE 1709
Cdd:NF041483 1195 KAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEE 1231
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1025-1176 |
1.33e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 49.37 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1025 HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalk 1104
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA------- 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1105 kirELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ--EVSILKKTL 1176
Cdd:pfam09787 115 ---ELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQltETLIQKQTM 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1304-1494 |
1.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1304 SALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMED-------- 1375
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1376 --GVGCLETAEEAK---------RRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQK 1444
Cdd:COG3883 99 ggSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1445 KFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAE 1494
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1056-1167 |
1.51e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.28 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1056 DSTDLSDQIAELQAQIAELKMQLAKKE---------EELQAALARVEEEAAQKNMALKKIRELETQ--ISelQEDLESER 1124
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 74180985 1125 ASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ 1167
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1522-1706 |
1.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQVEEMKTQLEELEDELQA----------TEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVR 1589
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQqlSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1590 QVREMEAELEDE-----RKQRSMAMAARKKLEM-------DLKDLEAHIDTANKN-REEAIKQLRKLQAQMkdcmRELDD 1656
Cdd:COG3206 252 GPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQlQQEAQRILASLEAEL----EALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1657 TRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1706
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1155-1921 |
1.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1155 TAAQQELRSKREQEVSILKKTLE--DEAKTHEAQIQEMRQKHSQAVEELA------DQLEQTKRVKATLEKAkqtleNER 1226
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEmaRELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEEL-----EER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1227 GELANEVKALLQGKGDsEHKRKKVEAQLqelqvkfsEGERVRTELADKVTKLQVE-------------LDSVTGLLSQSD 1293
Cdd:PRK04863 364 LEEQNEVVEEADEQQE-ENEARAEAAEE--------EVDELKSQLADYQQALDVQqtraiqyqqavqaLERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1294 SKSSKLTKDFSALESQLQD-TQELLQEEnrQKLSLSTKLKQM-----------------EDEKNSFREQLeeeeeakRNL 1355
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEaTEELLSLE--QKLSVAQAAHSQfeqayqlvrkiagevsrSEAWDVARELL-------RRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1356 EKQIAtLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQS 1435
Cdd:PRK04863 506 REQRH-LAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAeAREKETKALSLARALEEAMEQKAELERlnkQFRTEMEdlmsskdd 1515
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLLERER---ELTVERD-------- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1516 vgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ-----------AMKAQFERDLQGrd 1577
Cdd:PRK04863 649 ------ELAARKQALDEEIERLSqpggsedPRLNALAERFGGVLLSEIYDDVSLEdapyfsalygpARHAIVVPDLSD-- 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1578 eqseekkkqlvrqVREMEAELEDerkqrsmamaarkkLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDcmRELddt 1657
Cdd:PRK04863 721 -------------AAEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQW--- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1658 RASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgALALE-----EKRRLEAR 1730
Cdd:PRK04863 769 RYSRfpEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL---AVAFEadpeaELRQLNRR 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1731 IAQLEEELEEEQGNTELINDRLKKANLQIDQIN-----TDLNLERSHAQKNENARQQLERqnkelkakLQEMESAVKsKY 1805
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAKEGLSALNrllprLNLLADETLADRVEEIREQLDE--------AEEAKRFVQ-QH 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1806 KASIAALEAKIAQL---EEQLDNETKERQAASKQVRRTEKK---LKDVL-----LQVEDERRNAEQFKDQADKASTRLKQ 1874
Cdd:PRK04863 917 GNALAQLEPIVSVLqsdPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVqrrahFSYEDAAEMLAKNSDLNEKLRQRLEQ 996
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 74180985 1875 LKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
857-1593 |
2.11e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 857 VREKHLAAEnrlTEMETMQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEIchdlearveEEEERCQYLQ 935
Cdd:PRK10246 189 VFEQHKSAR---TELEKLQAQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL---------NWLTRLDELQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 936 AEKKKMQQniQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQiimEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKS 1015
Cdd:PRK10246 257 QEASRRQQ--ALQQALAAEEKAQPQLAALSLAQPARQLRPHWERI---QEQSAALAHTRQQIEEVNTRLQSTMALRARIR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1016 KSLAKLKNKHEAMITDLEERLRREEKQR---QELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEelqAALARV 1092
Cdd:PRK10246 332 HHAAKQSAELQAQQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLT 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1093 EEEAAQKNMALKKIRELETQISELQEDLeserasrnkAEKQKRdlgeelealKTELEDTLDSTAAQQELRskreqevsil 1172
Cdd:PRK10246 408 ADEVAAALAQHAEQRPLRQRLVALHGQI---------VPQQKR---------LAQLQVAIQNVTQEQTQR---------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1173 kktledeakthEAQIQEMRQKHSQAVEELADQ---LEQTKRVKatlekakqTLENERGELANEVKALLQGKgdSEHKrkk 1249
Cdd:PRK10246 460 -----------NAALNEMRQRYKEKTQQLADVktiCEQEARIK--------DLEAQRAQLQAGQPCPLCGS--TSHP--- 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1250 VEAQLQELQVkfSEGERVRTELADKVTKLQVELDSVTGllsQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLST 1329
Cdd:PRK10246 516 AVEAYQALEP--GVNQSRLDALEKEVKKLGEEGAALRG---QLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNI 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1330 KLKQMED-----EKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEdgvgcletaeEAKRRLQKDLEGLSQRLEEk 1404
Cdd:PRK10246 591 TLQPQDDiqpwlDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE----------QRQQQLLTALAGYALTLPQ- 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1405 vaaydklEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARA 1484
Cdd:PRK10246 660 -------EDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQ 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1485 LEEAMEQKA-ELERLNK---QFRTEMED---------LMSSKDDvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQAt 1551
Cdd:PRK10246 733 LQTLQQQDVlEAQRLQKaqaQFDTALQAsvfddqqafLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQ- 809
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 74180985 1552 edaklrlevNLQAMKAQFerDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:PRK10246 810 ---------HQQHRPDGL--DLTVTVEQIQQELAQLAQQLRE 840
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
851-1131 |
2.29e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 851 EAELTKVREKHLAAENRLTEMETMQSQLmAEKLQLQEQ----LQAETElcAEAEELrARLTAKKQELEEICHDLEARVEE 926
Cdd:pfam19220 138 EEENKALREEAQAAEKALQRAEGELATA-RERLALLEQenrrLQALSE--EQAAEL-AELTRRLAELETQLDATRARLRA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 927 EEERCQYLQAEKKKMQQNIQELEEQLEEEESArQKLQLEKVTTEAklkkLEEDQIIMEDQNcklakekkLLEDRVAEFTt 1006
Cdd:pfam19220 214 LEGQLAAEQAERERAEAQLEEAVEAHRAERAS-LRMKLEALTARA----AATEQLLAEARN--------QLRDRDEAIR- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1007 nlmEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQ 1086
Cdd:pfam19220 280 ---AAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIA 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 74180985 1087 AALARVEEEAAqknmalkkirELETQISELQEDLESERASRNKAE 1131
Cdd:pfam19220 357 ELTKRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
872-1238 |
2.54e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 872 ETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQ 951
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 952 LEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLaklknkhEAMITD 1031
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1032 LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNMALKKIRELET 1111
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALLEELRSLQERLNASERKVEGLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1112 QISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE--LRSKREQEVSILKktLEDEAKTHEAQIQE 1189
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQEREtlQQSAEADKDRIEK--LSAELQRLEERLQE 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1190 MRQKHSQAVEELA-------DQLEQTKRVKATLEKAKQTLENERGELANEVKALLQ 1238
Cdd:pfam07888 337 ERMEREKLEVELGrekdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1051-1339 |
3.25e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.08 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1051 RKLEGDSTDlsdqIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKirELETQISE------LQEDLESER 1124
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1125 ASRNKAEKQK----RDLGEELEALKTELEDTLDSTAAQQELRSKRE--QEVSILKKTLEDEAKTheaqiQEMRQKHSQAV 1198
Cdd:PLN03229 493 EEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKA-----EKLKAEINKKF 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1199 EELADQLEQTKRVKATLEKAKQTLENERGELANEVK-ALLQGKGDSEHKRKKVEAQLqELQVKFSEGERVRT-------E 1270
Cdd:PLN03229 568 KEVMDRPEIKEKMEALKAEVASSGASSGDELDDDLKeKVEKMKKEIELELAGVLKSM-GLEVIGVTKKNKDTaeqtpppN 646
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1271 LADKVTKLQVELDS-------VTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL---STKLKQMEDEKN 1339
Cdd:PLN03229 647 LQEKIESLNEEINKkiervirSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEalnSSELKEKFEELE 725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1421 |
3.76e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1184 EAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELAnevkallqgkgDSEHKRKKVEAQLQELQVKFse 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEAEAEI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1264 gERVRTELADKVTKLQVELDSVTGLLSQSDSKS-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFR 1342
Cdd:COG3883 82 -EERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1343 EQLEEEEEAKRNLEKQIATLHAQVTDMKKKmedgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQE 1421
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAE-------EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1381-1664 |
4.06e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 48.48 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTR----LQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLA--EEK 1454
Cdd:pfam05667 215 ELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRiaeqLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTtdTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK--AELERLNKQFrtemEDLMSSKDDVGKSVHELEKSKRALEQ 1532
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQreEELEELQEQL----EDLESSIQELEKEIKKLESSIKQVEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1533 QVEEMKTQLEELEDELQATEDAKLRL---EVNLQAMKAQFE---RDLQGRDEQSEEKKKQLV---RQVREMEAELEDERK 1603
Cdd:pfam05667 371 ELEELKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIeeyRALKEAKSNKEDESQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1604 Q------------RSMAMAARKKLEMdLKDLEAHIDTANK--NRE-------EAIKQLRKlqaQMKDCMRELDDTRASRE 1662
Cdd:pfam05667 451 RkleeikelrekiKEVAEEAKQKEEL-YKQLVAEYERLPKdvSRSaytrrilEIVKNIKK---QKEEITKILSDTKSLQK 526
|
..
gi 74180985 1663 EI 1664
Cdd:pfam05667 527 EI 528
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
829-1803 |
4.18e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 829 RLFTKVKPLLNSIrHEDELLAKEAELTK-VREKHLAAENRLTEMETMQSQLMAE--KLQLQEQLQAETELCA----EAEE 901
Cdd:TIGR01612 656 KIYSTIKSELSKI-YEDDIDALYNELSSiVKENAIDNTEDKAKLDDLKSKIDKEydKIQNMETATVELHLSNienkKNEL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 902 LRARLTAKKQELEEICHDLEARVEEeeercqyLQAEKKKMQQNIQELeeqleeeesARQKLQLEKVTTE-AKLKKLEEDQ 980
Cdd:TIGR01612 735 LDIIVEIKKHIHGEINKDLNKILED-------FKNKEKELSNKINDY---------AKEKDELNKYKSKiSEIKNHYNDQ 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 981 IIMEDQNCKLAKEKKlleDRVAEFTTNL-MEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTD 1059
Cdd:TIGR01612 799 INIDNIKDEDAKQNY---DKSKEYIKTIsIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNK 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1060 LSDQIAELQAQIAELKMQLAKkeeELQAALARVEEEAAQKNMALKKIRELetqISELQEDLESERASRNKAEKQKRDLGE 1139
Cdd:TIGR01612 876 IKAEISDDKLNDYEKKFNDSK---SLINEINKSIEEEYQNINTLKKVDEY---IKICENTKESIEKFHNKQNILKEILNK 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1140 ELEALKteledtlDSTAAQQELRSKREQevSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADqleqtkrVKATLEKAK 1219
Cdd:TIGR01612 950 NIDTIK-------ESNLIEKSYKDKFDN--TLIDKINELDKAFKDASLNDYEAKNNELIKYFND-------LKANLGKNK 1013
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1220 Q-TLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEgeRVRTELADKVTKLQVELdsvtglLSQSDSKSSK 1298
Cdd:TIGR01612 1014 EnMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIID--EIEKEIGKNIELLNKEI------LEEAEINITN 1085
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1299 LTKDFSALesQLQDTQELLQEENrqkLSLSTKLKQMEDEKNSFREQLEEEEEA----KRNLEKQIATLHAQVTDMKKKME 1374
Cdd:TIGR01612 1086 FNEIKEKL--KHYNFDDFGKEEN---IKYADEINKIKDDIKNLDQKIDHHIKAleeiKKKSENYIDEIKAQINDLEDVAD 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1375 DGVgcletAEEAKRRLQKDLEGLSQRLEEKVAAYD----------KLEKTKTRLQQEL---------------DDLLVDL 1429
Cdd:TIGR01612 1161 KAI-----SNDDPEEIEKKIENIVTKIDKKKNIYDeikkllneiaEIEKDKTSLEEVKginlsygknlgklflEKIDEEK 1235
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1430 DHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERD-RAEAEA--------------REKETKALSLAR----ALEEAME 1490
Cdd:TIGR01612 1236 KKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDiKAEMETfnishdddkdhhiiSKKHDENISDIRekslKIIEDFS 1315
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1491 QKAELERLNKQFRTEMEDLMSSKDDVGKSVHE---------LEKSKRALEQqVEEMKTQLEE----LEDELQATED--AK 1555
Cdd:TIGR01612 1316 EESDINDIKKELQKNLLDAQKHNSDINLYLNEianiynilkLNKIKKIIDE-VKEYTKEIEEnnknIKDELDKSEKliKK 1394
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1556 LRLEVNLQAMKAQFERDLQGRD-EQSEEKKKQLVRQVREMEA-----------------------ELEDERKQRSMAMA- 1610
Cdd:TIGR01612 1395 IKDDINLEECKSKIESTLDDKDiDECIKKIKELKNHILSEESnidtyfknadennenvlllfkniEMADNKSQHILKIKk 1474
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1611 --ARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQA------QMKDCMREL-------------DDTRASREEILAQAK 1669
Cdd:TIGR01612 1475 dnATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkelfeQYKKDVTELlnkysalaiknkfAKTKKDSEIIIKEIK 1554
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1670 ENEKKLkSMEAEmiqlqeelaAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA------RIAQLEEELEEEQG 1743
Cdd:TIGR01612 1555 DAHKKF-ILEAE---------KSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLK 1624
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1744 NTELINDRLkkANLQIDQINTDLNLERSHAQKNENARQQLERQNKEL---KAKLQEMESAVKS 1803
Cdd:TIGR01612 1625 ETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIedkKKELDELDSEIEK 1685
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
983-1151 |
4.28e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 983 MEDQNCKLAKEKKLLEDRVAEFTTNL-MEEEEKSKSLAKLKNKHEAMITDLEeRLRREEKQRQElektrrklEGDSTDLS 1061
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLvMDIEDPSAALNKLNTAAAKIKSKIE-QFQKVIKMYEK--------GGVCPTCT 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1062 DQIAELQAQIAELK---MQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEK------ 1132
Cdd:PHA02562 292 QQISEGPDRITKIKdklKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAaieelq 371
|
170 180
....*....|....*....|
gi 74180985 1133 -QKRDLGEELEALKTELEDT 1151
Cdd:PHA02562 372 aEFVDNAEELAKLQDELDKI 391
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
650-674 |
4.32e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.80 E-value: 4.32e-05
10 20
....*....|....*....|....*
gi 74180985 650 YKEQLAKLMATLRNTNPNFVRCIIP 674
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1019-1153 |
4.52e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.54 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1019 AKLKNKHEAM---ITDLEERLRREEKQRQELEKtrrklegdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKK-------------EQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1096 aaqknmalkkiRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
965-1503 |
4.52e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 965 EKVTTEAKLKKLEEDQIIMEDQNcklAKEKKLLEDRVAEFTTNLMEEEEKSKSLaklknkhEAMITDLEERL-RREEKQR 1043
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRESDRNQEL-------QKRIRLLEKREaEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1044 QELEKTRRKLEGDST-------------DLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELE 1110
Cdd:pfam05557 73 EQAELNRLKKKYLEAlnkklnekesqlaDAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1111 tqisELQEDLESERASRNKAEKQKRDLGEELEalkTELEDTLDSTAAQQELRSKREQEvSILKKTLEdeaktHEAQIQEM 1190
Cdd:pfam05557 153 ----QLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARIPELE-KELERLRE-----HNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1191 RQKHSQAVEELAD------QLEQTKRVKATLEKAKQTLENERGE-----------------LANEVKALLQGKGDSEHKR 1247
Cdd:pfam05557 220 IENKLLLKEEVEDlkrkleREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlrspedLSRRIEQLQQREIVLKEEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1248 KKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQD-TQELLQEENRQKLS 1326
Cdd:pfam05557 300 SSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESyDKELTMSNYSPQLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1327 LSTK-----LKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKK--MEDGVGCLETAEEAKRRLQkDLEGLSQ 1399
Cdd:pfam05557 380 ERIEeaedmTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQesLADPSYSKEEVDSLRRKLE-TLELERQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1400 RLEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKK--FDQLLAEEKTISAKYAEERDRAEAEAREKETk 1477
Cdd:pfam05557 459 RLREQKNELE-MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKnqLEKLQAEIERLKRLLKKLEDDLEQVLRLPET- 536
|
570 580
....*....|....*....|....*.
gi 74180985 1478 alSLARALEEAMEQKAELERLNKQFR 1503
Cdd:pfam05557 537 --TSTMNFKEVLDLRKELESAELKNQ 560
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1335-1536 |
4.93e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1335 EDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLekt 1414
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1415 kTRLQQELDDLLVDLDH--QRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK 1492
Cdd:COG3883 92 -ARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74180985 1493 AELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 1536
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1450-1605 |
5.26e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1450 LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEM-----------EDLMSSKDDVGK 1518
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELqklekrllqkeENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1519 SVHELEKSKRALEQQVEEMKTQLEELEdELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVrEMEAEL 1598
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELE-ELIEEQLQELERISGLTAEEAK-EILLEKVEEEARHEAAVLIKEI-EEEAKE 184
|
....*..
gi 74180985 1599 EDERKQR 1605
Cdd:PRK12704 185 EADKKAK 191
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1462-1704 |
5.74e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.56 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1462 EERDRAEAEAREKETKalsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTql 1541
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1542 eeLEDELQATEDAKLRLEVNLQAMKaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDL-- 1619
Cdd:pfam00261 83 --LENRALKDEEKMEILEAQLKEAK--------EIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1620 -----KDLEAHIDTANKNREEAIKQLRKLQAQMKdcmrelddtrasreEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:pfam00261 153 vgnnlKSLEASEEKASEREDKYEEQIRFLTEKLK--------------EAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|
gi 74180985 1695 AKRQAQQERD 1704
Cdd:pfam00261 219 KYKAISEELD 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
905-1469 |
6.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 905 RLTAKKQELEEICHDLEARVEEEeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIME 984
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 985 D---QNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDL----EERLRREEKQRQELEKTRRKLEGDS 1057
Cdd:PRK01156 239 SalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1058 TDLSD------QIAELQAQIAE-LKMQlaKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKA 1130
Cdd:PRK01156 319 AEINKyhaiikKLSVLQKDYNDyIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1131 EKQKRDLGEELEALKTELEDTLDSTAA-----QQELRSKREQEVSILKKT--LEDEAK-----TH--EAQIQEMRQKHSQ 1196
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSkvsslNQRIRALRENLDELSRNMemLNGQSVcpvcgTTlgEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1197 AVEELADQLEQTKR-VKATLEKAKQTLENE---RGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELA 1272
Cdd:PRK01156 477 KKSRLEEKIREIEIeVKDIDEKIVDLKKRKeylESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1273 D-KVTKLQVELDSVTGLLSQSDSKS-SKLTKDFSALESQLQD----TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLE 1346
Cdd:PRK01156 557 SlKLEDLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDlesrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1347 EEEEAKRnlekQIATLHAQVTDMKKKMEDgvgcletaeeaKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLL 1426
Cdd:PRK01156 637 EIQENKI----LIEKLRGKIDNYKKQIAE-----------IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLE 701
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 74180985 1427 VDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEA 1469
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREA 744
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1460-1640 |
7.59e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.40 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1460 YAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:PRK12705 26 KKRQRLAKEAERILQE------AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1540 qLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVrqVREMEAELEDERKQRSMAMAARKKLEMDL 1619
Cdd:PRK12705 100 -LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAELEEEKAQRVKKIEEEADLEAER 176
|
170 180
....*....|....*....|.
gi 74180985 1620 KDLEAHIDTANKNREEAIKQL 1640
Cdd:PRK12705 177 KAQNILAQAMQRIASETASDL 197
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1071-1221 |
9.02e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1071 IAELKMQLAKKEEELQAALARVEEEAAQKnmalKKIRELETQISELQEDLESE-RASRNKAEKQKRDLGEELEALKTELE 1149
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKK----EALLEAKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1150 DTLDSTA---AQQELRSKREQEVSILKKTLEdeaKTHEAQIQEMRQ----KHSQAVEELADQLEQ------TKRVKATLE 1216
Cdd:PRK12704 104 LLEKREEeleKKEKELEQKQQELEKKEEELE---ELIEEQLQELERisglTAEEAKEILLEKVEEearheaAVLIKEIEE 180
|
....*
gi 74180985 1217 KAKQT 1221
Cdd:PRK12704 181 EAKEE 185
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1026-1270 |
9.17e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1106 IRELETQISELQEDLESERASR-NKAEKQKR--------------------------DLGEELEALKTELEDTLDSTAAQ 1158
Cdd:COG1340 87 LNELREELDELRKELAELNKAGgSIDKLRKEierlewrqqtevlspeeekelvekikELEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1159 QELRSKREQEVSILKK--TLEDEAKTHEAQIQEMRQKH---SQAVEELADQLEQTKRVKATLEKAKQTLENERGELANEV 1233
Cdd:COG1340 167 AELKELRKEAEEIHKKikELAEEAQELHEEMIELYKEAdelRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 74180985 1234 KALLQGKGDSEHKRKK--VEAQLQELQVKFSEGERVRTE 1270
Cdd:COG1340 247 KKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTE 285
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1480-1587 |
1.01e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 44.61 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1480 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 1559
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90 100
....*....|....*....|....*...
gi 74180985 1560 VNLQAMKAQFERDLQGRDEQSEEKKKQL 1587
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1033-1212 |
1.14e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1033 EERLRREEKQRQ-ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlAKKEEELQAALARVEEEAAQKNMalkkirELET 1111
Cdd:COG2268 211 ETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERRE-AETARAEAEAAYEIAEANAEREV------QRQL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1112 QISELQEDLESERASRNKAEKQ-KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVsiLKKTLEDEAKTHEAQIQEM 1190
Cdd:COG2268 284 EIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG--KRALAEAWNKLGDAAILLM 361
|
170 180
....*....|....*....|...
gi 74180985 1191 R-QKHSQAVEELADQLEQTKRVK 1212
Cdd:COG2268 362 LiEKLPEIAEAAAKPLEKIDKIT 384
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1631-1913 |
1.16e-04 |
|
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: 47.04 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1631 KNREEAIKQLRKLQAQMKDCMRELDDTRASRE-EILAQAK---ENEKKLKSMEAEMIQLQEElaaaERAKRQAQQERDEL 1706
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELERIRQEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1707 ADEIANSSGKGALALEEKRRLEaRIAQLEEELEEEQGNTELINDRLKKANLQIDQINTdlnlERSHAQKNENARQQLERQ 1786
Cdd:pfam17380 371 AMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA----EQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1787 NKELKAKLQEMEsavKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRT-EKKLKDVLLQ-VEDERRNAEQFKDQ 1864
Cdd:pfam17380 446 REMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRKLLEKEM 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1865 ADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA---DAMNRE 1913
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMERE 574
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
842-1260 |
1.30e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 842 RHEDELLAKEAELTKVREKHLAAENRLTEM----------ETMQSQLMAEKLQLQEQL-QAETELCAEAEELRARLTAKK 910
Cdd:pfam05557 45 RESDRNQELQKRIRLLEKREAEAEEALREQaelnrlkkkyLEALNKKLNEKESQLADArEVISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 911 QELEEICHDLEArveeEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvTTEAKLKKLEEDQIIMEDQNCKL 990
Cdd:pfam05557 125 LELQSTNSELEE----LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 991 AkekklledRVAEFTTNLMEEEEKSKSLAKLKNKHEAM---ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAEL 1067
Cdd:pfam05557 197 A--------RIPELEKELERLREHNKHLNENIENKLLLkeeVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1068 QAQIAELK--MQLAKKEEELQAA-LARVEEEAAQKNMAL---KKIRELETQISELQEDLESERASRNKAEKQKRDLGEEL 1141
Cdd:pfam05557 269 QDTGLNLRspEDLSRRIEQLQQReIVLKEENSSLTSSARqleKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1142 EALKTELE------DTLDSTAAQQELRSKREQEVsilkKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATL 1215
Cdd:pfam05557 349 LLLTKERDgyrailESYDKELTMSNYSPQLLERI----EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 74180985 1216 EKAK-QTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVK 1260
Cdd:pfam05557 425 QALRqQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME 470
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
850-1192 |
1.35e-04 |
|
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: 46.81 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 850 KEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEeee 929
Cdd:pfam07888 57 REKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRE--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 930 rcqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLM 1009
Cdd:pfam07888 134 ----LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD-------QIAEL---QAQIAELKMQLA 1079
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrTQAELhqaRLQAAQLTLQLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1080 KKEEELQAALAR--VEEEAAQKNMALKK--IRELETQISELQEDLESERASRNKaekqkrdlgeeleaLKTELEDTLDST 1155
Cdd:pfam07888 290 DASLALREGRARwaQERETLQQSAEADKdrIEKLSAELQRLEERLQEERMEREK--------------LEVELGREKDCN 355
|
330 340 350
....*....|....*....|....*....|....*..
gi 74180985 1156 AAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQ 1192
Cdd:pfam07888 356 RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1041-1276 |
1.35e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAEL-KMQLAKKE-EELQAA---LARVEEEAAQKNMALKKIRELE----T 1111
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEErrrLSNAEKLREALQEALEALSGGEggalD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1112 QISELQEDLesERASRnkAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevsilkktLE-DEAKTHE-----A 1185
Cdd:COG0497 245 LLGQALRAL--ERLAE--YDPSLAELAERLESALIELEE------AASELRRYLDS--------LEfDPERLEEveerlA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1186 QIQEMRQKHSQAVEEL-------ADQLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkgdSEhKRKK--------V 1250
Cdd:COG0497 307 LLRRLARKYGVTVEELlayaeelRAELAELENSDERLEELEAELAEAEAELLEAAEKL------SA-ARKKaakklekaV 379
|
250 260 270
....*....|....*....|....*....|...
gi 74180985 1251 EAQLQEL-------QVKFSEGERVRTELADKVT 1276
Cdd:COG0497 380 TAELADLgmpnarfEVEVTPLEEPGPNGADQVE 412
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
962-1181 |
1.46e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 962 LQLEKVTTEAKLKKLEEDQI---IMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEE--KSKSLAkLKNKHEAM------IT 1030
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1031 DLEERLRREEKQRQELEKTRRKLEgdSTDLSDQiaELQAQIAELKMQ-LAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PLN02939 254 ETEERVFKLEKERSLLDASLRELE--SKFIVAQ--EDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1110 ETQISELQEDLESERASRNKAEKQKRdLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAK 1181
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1653-1892 |
1.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1653 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalALEEK-RRLEARI 1731
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------EAEAEiEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1732 AQLEEELEEEQGNTELINDRLKKANLQ--IDQINTDLNLERSHAQKNE---NARQQLERQNKELKAKLQEMESAvkskyk 1806
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFSdfLDRLSALSKIADADADLLEelkADKAELEAKKAELEAKLAELEAL------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1807 asIAALEAKIAQLEEQLDnetkERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEA 1886
Cdd:COG3883 163 --KAELEAAKAELEAQQA----EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 74180985 1887 QRANAS 1892
Cdd:COG3883 237 AAAAAA 242
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
999-1270 |
1.67e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 999 DRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1077
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKReERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1078 LAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRD--LGEELEALKTELEDTLDST 1155
Cdd:pfam02029 114 SWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEnfAKEEVKDEKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1156 AAQQELRSKREQEVsilkKTLEDEAKTHEAQIQEMRQKHSQAVEElADQLEQTKRVKAtlEKAKQTLENERGELANEVKA 1235
Cdd:pfam02029 194 SKVFLDQKRGHPEV----KSQNGEEEVTKLKVTTKRRQGGLSQSQ-EREEEAEVFLEA--EQKLEELRRRRQEKESEEFE 266
|
250 260 270
....*....|....*....|....*....|....*
gi 74180985 1236 LLQgkgdseHKRKKVEAQLQELQVKFSEGERVRTE 1270
Cdd:pfam02029 267 KLR------QKQQEAELELEELKKKREERRKLLEE 295
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1467-1715 |
1.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1467 AEAEAREKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1546
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1547 EL-------QATEDAKLRLEVNLQA-------MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmAMAAR 1612
Cdd:COG3883 87 ELgeraralYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1613 KKLEMDLKDLEAHIDTAnknrEEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1692
Cdd:COG3883 164 AELEAAKAELEAQQAEQ----EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260
....*....|....*....|...
gi 74180985 1693 ERAKRQAQQERDELADEIANSSG 1715
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSA 262
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
990-1115 |
1.80e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 990 LAKEKKL-LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLrreekqrQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQ-------KNMAL-KKIRELETQISE 1115
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrLNVALaQRVQELNRYRSE 198
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1036-1167 |
1.85e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1036 LRRE-EKQRQELEKTRRKLegdsTDLSDQIA-------ELQAQIAELKMQLAKKEEE---LQAALARVEEEAAqknmalk 1104
Cdd:PRK09039 44 LSREiSGKDSALDRLNSQI----AELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1105 kirELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDstAAQQELRSKREQ 1167
Cdd:PRK09039 113 ---AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALD--ASEKRDRESQAK 173
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1056-1240 |
1.89e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.88 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1056 DSTDLSDQIAELQAQIAelkmqlakkeeELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEkqkr 1135
Cdd:pfam00529 52 DPTDYQAALDSAEAQLA-----------KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQ---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1136 dlgEELEALKTELEDTlDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTK-RVKAT 1214
Cdd:pfam00529 117 ---AQLAQAQIDLARR-RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsGAQLQ 192
|
170 180
....*....|....*....|....*..
gi 74180985 1215 LEKAKQTLENERGELAN-EVKALLQGK 1240
Cdd:pfam00529 193 IAEAEAELKLAKLDLERtEIRAPVDGT 219
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1375-1632 |
1.99e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.75 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1375 DGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKL------EKTKTRLQQELDDllvdldhQRQSVSNLEKKQKKFDQ 1448
Cdd:NF012221 1525 DGLGYILDNVVATSESSQQADAVSKHAKQDDAAQNALadkeraEADRQRLEQEKQQ-------QLAAISGSQSQLESTDQ 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1449 LLAEEKTISakyaeERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMssKDDVGKSvheLEKSKR 1528
Cdd:NF012221 1598 NALETNGQA-----QRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQEQ---LDDAKK 1667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1529 ALEQQVEEMKTQleeLEDELQATEDAKLRLEVNL-QAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAElEDERKQRSM 1607
Cdd:NF012221 1668 ISGKQLADAKQR---HVDNQQKVKDAVAKSEAGVaQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQ-QAESDANAA 1743
|
250 260
....*....|....*....|....*
gi 74180985 1608 AMAARKKLEMDLKDLEAHIDTANKN 1632
Cdd:NF012221 1744 ANDAQSRGEQDASAAENKANQAQAD 1768
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1382-1611 |
2.02e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1382 TAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDllvdldhQRQSVSNLEKKQKKFDQLLAE-EKTISAKY 1460
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKLQAEIAEaEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1461 AEERDRAEAEAREKET----KALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDdvgksvhELEKSKRALEQQVEE 1536
Cdd:COG3883 86 EELGERARALYRSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA-------ELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1537 MKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAA 1611
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1184-1420 |
2.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1184 EAQIQEMRQKHSQAVEELADQLEQtkrVKATLEKAKQTLENERGElanevkallQGKGDSEHKRKKVEAQLQELQVKFSE 1263
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1264 gerVRTELADkvtkLQVELDSVTGLLSQSDSKSSKLTKD--FSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSF 1341
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1342 REQLEEE-EEAKRNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKtktRLQQ 1420
Cdd:COG3206 304 RAQLQQEaQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARELYESLLQ---RLEE 376
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1386-1622 |
2.50e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1386 AKRRLQKDLeglsqrLEEKV-AAYDKLEKTKTR-LQQELDDLLVDLDHQRQSV---------------SNLEKKQKKFDQ 1448
Cdd:PHA02562 151 ARRKLVEDL------LDISVlSEMDKLNKDKIReLNQQIQTLDMKIDHIQQQIktynknieeqrkkngENIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1449 LLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtemEDLMSSKDDV----GKSVHELE 1524
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK------VIKMYEKGGVcptcTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1525 KSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQ 1604
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
250
....*....|....*...
gi 74180985 1605 RSMAMAARKKLEMDLKDL 1622
Cdd:PHA02562 374 FVDNAEELAKLQDELDKI 391
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1024-1364 |
3.10e-04 |
|
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: 45.66 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1024 KHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEA------- 1096
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEekykels 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1097 --------------AQKNMALKKIRELETQISELQE-------DLESERASRNKAEKQKRDLGEELEALKTELEdtldst 1155
Cdd:pfam07888 108 asseelseekdallAQRAAHEARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQ------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1156 AAQQELR--SKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQA---VEELADQLEQTKRVKATLEKAKQTLENERGELA 1230
Cdd:pfam07888 182 QTEEELRslSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1231 NEVKAllQGKGDSEHKRKKVEA-----QLQELQVKFSEGervRTELADKVTKLQveldsvtgllsqsdsKSSKLTKDFSA 1305
Cdd:pfam07888 262 SMAAQ--RDRTQAELHQARLQAaqltlQLADASLALREG---RARWAQERETLQ---------------QSAEADKDRIE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1306 -LESQLQDTQELLQEENRQKLSLSTKLKQmedEKNSFREQLeeeEEAKRNLEKQIATLHA 1364
Cdd:pfam07888 322 kLSAELQRLEERLQEERMEREKLEVELGR---EKDCNRVQL---SESRRELQELKASLRV 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1102-1275 |
3.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1102 ALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqqelrsKREQevsilkKTLEDEAK 1181
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL------------EKEI------KRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1182 THEAQIQEMRQKHSQA-----VEELADQLEQTKRVKATLEK----AKQTLENERGELANEVKALLQGKGDSEHKRKKVEA 1252
Cdd:COG1579 70 EVEARIKKYEEQLGNVrnnkeYEALQKEIESLKRRISDLEDeileLMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|...
gi 74180985 1253 QLQELQVKFSEGERVRTELADKV 1275
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1618-1712 |
3.16e-04 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 45.38 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1618 DLKDLEAHIDT-----ANKNREEAIKQLRKLQAQMKDCMRELDDTRASR----EEIlAQAKENEKKLKSMEAEMIQLQEE 1688
Cdd:COG0172 3 DIKLIRENPEAvkealAKRGFDLDVDELLELDEERRELQTEVEELRAERnalsKEI-GKAKKKGEEAEALIAEVKELKEE 81
|
90 100
....*....|....*....|....
gi 74180985 1689 LAAAERAKRQAQQERDELADEIAN 1712
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPN 105
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1679-1846 |
3.26e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.11 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1679 EAEMIQLQEELAAAERAKRQAQQERDELadeianssgkgalaleekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQ 1758
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1759 IDQINTDLNLERSHAQKN-------ENARQQLERQNKELKAKLQEMESAvkskYKASIAALEAKIAQLEEQLDNETKERQ 1831
Cdd:pfam00529 119 LAQAQIDLARRRVLAPIGgisreslVTAGALVAQAQANLLATVAQLDQI----YVQITQSAAENQAEVRSELSGAQLQIA 194
|
170
....*....|....*
gi 74180985 1832 AASKQVRRTEKKLKD 1846
Cdd:pfam00529 195 EAEAELKLAKLDLER 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
863-1128 |
3.53e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 863 AAENRLTEMETMQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEichdlearveeeeercqyLQAEKKKMQ 942
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK------------------LQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 943 QNIQELEEQLEEEESARQKlqlekvtTEAKLKKLEedqIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEeeksksLAKLK 1022
Cdd:COG3883 79 AEIEERREELGERARALYR-------SGGSVSYLD---VLLGSESFSDFLDRLSALSKIADADADLLEE------LKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1023 NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMA 1102
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
250 260
....*....|....*....|....*.
gi 74180985 1103 LKKIRELETQISELQEDLESERASRN 1128
Cdd:COG3883 223 AAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1858 |
3.67e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssgkgalaleekRRLEARIAQleeeleeeq 1742
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------------KRLELEIEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1743 gntelINDRLKKANLQIDQINT-----DLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIA 1817
Cdd:COG1579 71 -----VEARIKKYEEQLGNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74180985 1818 QLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNA 1858
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKR 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1616-1822 |
3.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1616 EMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAaaERA 1695
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1696 KRQAQQER-----------DELADEIANSSGKGALA----------LEEKRRLEARIAQLEEELEEEQGNTELINDRLKK 1754
Cdd:COG3883 93 RALYRSGGsvsyldvllgsESFSDFLDRLSALSKIAdadadlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1755 ANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQ 1822
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1455-1909 |
3.82e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV 1534
Cdd:COG5278 72 TGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1535 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKK 1614
Cdd:COG5278 152 DEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1615 LEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1695 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQ 1774
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1775 KNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDE 1854
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1855 RRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1075-1221 |
3.98e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1075 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEdleserasrnkaekQKRDLGEELEALK---TELEDT 1151
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDeriERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1152 LDSTAAQQELRSKREQEVSILKKtledEAKTHEAQIQEMRQKhsqaVEELADQLEQTKRVKATLEKAKQT 1221
Cdd:COG2433 450 LSEARSEERREIRKDREISRLDR----EIERLERELEEERER----IEELKRKLERLKELWKLEHSGELV 511
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1384-1591 |
4.34e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1384 EEAKRRLQKDleglSQRLEEKVAaydKLEKTKTRLQQElddllvdldhqRQSVSNLEKKQKKFDQLLAEEKtisAKYAEE 1463
Cdd:PRK00409 505 EEAKKLIGED----KEKLNELIA---SLEELERELEQK-----------AEEAEALLKEAEKLKEELEEKK---EKLQEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1464 RDRAEAEAREKETKALSLARalEEAMEQKAELERLNKQFRTEMEDlmsskddvgksvHELEKSKRALEQQVEEMKTQL-- 1541
Cdd:PRK00409 564 EDKLLEEAEKEAQQAIKEAK--KEADEIIKELRQLQKGGYASVKA------------HELIEARKRLNKANEKKEKKKkk 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1542 -EELEDELQATEDAKLR--------------LEVNLQA----MKAQfERDLQGRDEQSEEKKKQLVRQV 1591
Cdd:PRK00409 630 qKEKQEELKVGDEVKYLslgqkgevlsipddKEAIVQAgimkMKVP-LSDLEKIQKPKKKKKKKPKTVK 697
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1520-1907 |
4.39e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1520 VHELEKSKRAleqqVEEMKTQLEELE-DELQATED---AKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1595
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVEEMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1596 AELEDERKQRSMAMAARkklemdlkdleahiDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREeiLAQAKENEKKL 1675
Cdd:pfam05701 145 EELESLRKEYASLVSER--------------DIAIKRAEEAVSASKEIEKTVEELTIELIATKESLE--SAHAAHLEAEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1676 KSMEAEMIQLQEELAAaERAKRQAQQERDELADEIANS-------SGKGALALEEKRRLEARIAQLEEELEEEQGNTELI 1748
Cdd:pfam05701 209 HRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAkdlksklETASALLLDLKAELAAYMESKLKEEADGEGNEKKT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1749 NDRLKKA-----------NLQIDQINTDLNLERSHAqknENARQQLERQNKELkAKLQEMESavkskyKASIAaleakIA 1817
Cdd:pfam05701 288 STSIQAAlasakkeleevKANIEKAKDEVNCLRVAA---ASLRSELEKEKAEL-ASLRQREG------MASIA-----VS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1818 QLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQ 1897
Cdd:pfam05701 353 SLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVL 432
|
410
....*....|
gi 74180985 1898 RELEDATETA 1907
Cdd:pfam05701 433 KEIEAAKASE 442
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1656-1927 |
5.41e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1656 DTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGKgaLALEEKRRLEAriaQLE 1735
Cdd:NF012221 1532 DNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET---NGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1736 EELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAK 1815
Cdd:NF012221 1606 AQRDAILEESRAVTKELTTLAQGLDALDSQAT------YAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1816 IAQLEEQLDNETKERQAAskqVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAeeeaqrANASRRK 1895
Cdd:NF012221 1680 HVDNQQKVKDAVAKSEAG---VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA------ANDAQSR 1750
|
250 260 270
....*....|....*....|....*....|..
gi 74180985 1896 LQRELEDATETADAMNREVSSLknKLRRGDLP 1927
Cdd:NF012221 1751 GEQDASAAENKANQAQADAKGA--KQDESDKP 1780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1727-1926 |
5.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1727 LEARIAQLEEELEEEQGNTELIN-DRLKKANLQIDQI---NTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVK 1802
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeekEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1803 -SKYKASIAALEAKIAQLEEQLDnETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKAstRLKQLKRQLee 1881
Cdd:COG4717 127 lLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEEL-- 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74180985 1882 aeeeaQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDL 1926
Cdd:COG4717 202 -----EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1057-1236 |
5.69e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1057 STDLSDQIAELQAQIAELKMQLA--KKEEELQAALARVEEEAAQKNMALKKIRELETQIS--ELQEDLESERASRNKAEK 1132
Cdd:pfam09731 282 NDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRES 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1133 QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvSILKKTLEDEAKTHEAQIQEMRQK---HSQAVEELADQLEQTK 1209
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENR 440
|
170 180 190
....*....|....*....|....*....|....*..
gi 74180985 1210 R----------VKATLEKAKQTLenERGELANEVKAL 1236
Cdd:pfam09731 441 KaqqlwlaveaLRSTLEDGSADS--RPRPLVRELKAL 475
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1611-1924 |
5.72e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1611 ARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELa 1690
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1691 aaeRAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLNLER 1770
Cdd:COG1340 81 ---DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-----------------------LEWRQQTEVLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1771 shaqknenaRQQLERQNKELKAKLQEMESAVKSKYKasIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQ 1850
Cdd:COG1340 135 ---------EKELVEKIKELEKELEKAKKALEKNEK--LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1851 VEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA--TETADAMNREVSSLKNKLRRG 1924
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkrEKEKEELEEKAEEIFEKLKKG 279
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1035-1167 |
5.97e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.34 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1035 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKkeeeLQAALARVEEEAAQKNMALKKIRELETQIS 1114
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ----AQIDLARRRVLAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1115 ELQEDLESERASRNKAEKQKRDLGEELEAL--KTELEDTLDSTAAQQELRSKREQ 1167
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELKLAKLD 206
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
995-1272 |
6.45e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 995 KLLEDRVAEFTtnlmeeeEKSKSLAKLKNKHEAMITDLEERLRREEKQRQEL-EKTRRklegdstDLSDQIAELQAQIAE 1073
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIE-------DLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1074 LKMQLAKKEEELQAALARVEEEAAQKnmalkkiRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELED--- 1150
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1151 -------------------TLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRV 1211
Cdd:pfam00038 146 elqaqvsdtqvnvemdaarKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRT 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1212 KATLEkakQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvkfSEGERVRTELA 1272
Cdd:pfam00038 226 IQSLE---IELQSLKKQKASLERQLAETEERYELQLADYQELISELE---AELQETRQEMA 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1564-1731 |
6.67e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1564 AMKAQFER--DLQGRDEQSEEKKKQLvrqvREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLR 1641
Cdd:COG1579 1 AMPEDLRAllDLQELDSELDRLEHRL----KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1642 KLQAQM---------KDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1712
Cdd:COG1579 77 KYEEQLgnvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*....
gi 74180985 1713 ssgKGALALEEKRRLEARI 1731
Cdd:COG1579 157 ---ELEELEAEREELAAKI 172
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1450-1923 |
6.75e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1450 LAEEKTISAKYAEERDRAEAEAREKE---TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD------------ 1514
Cdd:TIGR00606 233 LESSREIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlndlyhnhqr 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1515 ----------DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK 1584
Cdd:TIGR00606 313 tvrekerelvDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1585 K---QLVRQVREMEAEL---------EDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREE---AIKQLRKLQAQMKD 1649
Cdd:TIGR00606 393 KnfhTLVIERQEDEAKTaaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1650 CMrELDDTRASREEILAQAKENeKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANS------SGKGALALEE 1723
Cdd:TIGR00606 473 IL-ELDQELRKAERELSKAEKN-SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQ 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1724 KRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKS 1803
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1804 KykASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKdvllQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAE 1883
Cdd:TIGR00606 631 V--CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFIT----QLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL 704
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1884 EEAQRANASRRKLQRELEDATETA-----------DAMNREVSSLKNKLRR 1923
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMlglapgrqsiiDLKEKEIPELRNKLQK 755
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1496-1854 |
7.29e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1496 ERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE----- 1570
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEqleee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1571 -RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKD 1649
Cdd:COG4372 82 lEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1650 CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1729
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1730 RIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASI 1809
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 74180985 1810 AALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDE 1854
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1527-1699 |
7.64e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1527 KRALEQQVEEMKTQ----LEELEDELQATEDAKLrLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELED 1600
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1601 ERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDcmrelddtrASREEILAQAKEnekKLKSMEA 1680
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEILLEKVEE---EARHEAA 172
|
170
....*....|....*....
gi 74180985 1681 EMIQLQEELAAAErAKRQA 1699
Cdd:PRK12704 173 VLIKEIEEEAKEE-ADKKA 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
844-1219 |
7.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 844 EDELLAKEAELTKVREKHLAAENRLTEMETmQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEI---CHDL 920
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLdasSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 921 EArveeeeercqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEkkLLEDR 1000
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1001 VAefttnlmeEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQIAELkmqla 1079
Cdd:COG4913 755 FA--------AALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALL----- 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1080 kkeEELQA-ALARVEEEAAqknmalkkiRELETQISELQEDLESE-RASRNKAEKQKRDLGEELEALKTELEDTLdstaa 1157
Cdd:COG4913 822 ---DRLEEdGLPEYEERFK---------ELLNENSIEFVADLLSKlRRAIREIKERIDPLNDSLKRIPFGPGRYL----- 884
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1158 QQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAK 1219
Cdd:COG4913 885 RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1567-1923 |
1.02e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1567 AQFERDLQGRDEQSEEKKKQLVRQVREM------EAELEDE------RKQRSM-AMAARKKLEM---DLKDLEAHIDTAN 1630
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLVEMARELeelsarESDLEQDyqaasdHLNLVQtALRQQEKIERyqeDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1631 KNREEAIKQLRKLQAQMKDCMRELDdtrasreEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQER---DELA 1707
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVD-------SLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLPDltpENAE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1708 DEIANSSGKGALALEEKRRLEARIAqleeeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLER-- 1785
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLS---------------VADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRyr 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1786 -------QNKELKAKLQEMESAVKSKYKAsiaalEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNA 1858
Cdd:COG3096 506 sqqalaqRLQQLRAQLAELEQRLRQQQNA-----ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1859 EQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMN------REVSSLKNKLRR 1923
Cdd:COG3096 581 SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQqllereREATVERDELAA 651
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1076-1416 |
1.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1076 MQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDST 1155
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1156 AAQQELRSKREQEVSILKK---TLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELANE 1232
Cdd:COG4372 104 ESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1233 VKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQD 1312
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1313 TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQK 1392
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
330 340
....*....|....*....|....
gi 74180985 1393 DLEGLSQRLEEKVAAYDKLEKTKT 1416
Cdd:COG4372 344 QLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1495-1879 |
1.07e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.13 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1495 LERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDElqatedaKLRLEVNLQAMKAQFERDlq 1574
Cdd:pfam15964 302 IERLTK----ERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFE-------KTKALIQCEQLKSELERQ-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1575 gRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMkdCMREL 1654
Cdd:pfam15964 369 -KERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQL--ASQEM 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1655 DDTRASREeilAQAKENEKKLKSMEAEMiQLQEELAAAERAKRQAQQERDELADEIANSSGKgalaLEEKRRLEARIAQL 1734
Cdd:pfam15964 446 DVTKVCGE---MRYQLNQTKMKKDEAEK-EHREYRTKTGRQLEIKDQEIEKLGLELSESKQR----LEQAQQDAARAREE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1735 EEELEEEQGNTE--LINDRLKKANLQidqintdlnleRSHAQKNENARQQLERQNKELKAKLQEMES----------AVK 1802
Cdd:pfam15964 518 CLKLTELLGESEhqLHLTRLEKESIQ-----------QSFSNEAKAQALQAQQREQELTQKMQQMEAqhdktvneqySLL 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1803 SKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQL 1879
Cdd:pfam15964 587 TSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQL 663
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1196-1331 |
1.08e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1196 QAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKAllqgkgdSEHKRKKVEAQLqelqvkfSEGERVRTELADKV 1275
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-------AEAERSRLQALL-------AELAGAGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1276 TKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL-------QEENRQKLSLSTKL 1331
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQAKIADLGRRL 181
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1139-1859 |
1.14e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1139 EELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVKAtLEKA 1218
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQA-LQQA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1219 KQTLENERGELANEVKALlqgkgdsehkrkkVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSK 1298
Cdd:PRK10246 270 LAAEEKAQPQLAALSLAQ-------------PARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1299 ltkDFSALESQLQDTQELLQEENRQKLslstklkqMEDEKNSFREQLEEEEEAKrnleKQIATLHAQVTDMKKKMED--G 1376
Cdd:PRK10246 337 ---QSAELQAQQQSLNTWLAEHDRFRQ--------WNNELAGWRAQFSQQTSDR----EQLRQWQQQLTHAEQKLNAlpA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1377 VGCLETAEE--AKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEK 1454
Cdd:PRK10246 402 ITLTLTADEvaAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1455 TISAKYAEERDRAEAEAREKETKALSLARALEE-AMEQKAELERLNKQFRtemedlmssKDDVGKSVHELEKSKRALEQQ 1533
Cdd:PRK10246 482 TICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHpAVEAYQALEPGVNQSR---------LDALEKEVKKLGEEGAALRGQ 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1534 VEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDE------QSEEKKKQL--VRQVREMEAELEDERKQR 1605
Cdd:PRK10246 553 LDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDiqpwldAQEEHERQLrlLSQRHELQGQIAAHNQQI 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1606 SMAMAA----RKKLEMDLKDLEAHIDTANK------NREEAIK-------QLRKLQAQMKDCMRELDDTRASREEILAQA 1668
Cdd:PRK10246 633 IQYQQQieqrQQQLLTALAGYALTLPQEDEeaswlaTRQQEAQswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1669 KENEKKLKSMEAEMIQLQEELAAAERakrQAQQERDELADEIANSSGkgALALEEKRRLEARIAQleeeleeeqgnteLI 1748
Cdd:PRK10246 713 TVALDNWRQVHEQCLSLHSQLQTLQQ---QDVLEAQRLQKAQAQFDT--ALQASVFDDQQAFLAA-------------LL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1749 NDrlkKANLQIDQINTDLNLERSHAQK-NENARQQLERQNKELKAKLQEmesavkskyKASIAALEAKIAQLEEQLDNET 1827
Cdd:PRK10246 775 DE---ETLTQLEQLKQNLENQRQQAQTlVTQTAQALAQHQQHRPDGLDL---------TVTVEQIQQELAQLAQQLRENT 842
|
730 740 750
....*....|....*....|....*....|....*
gi 74180985 1828 KERQAASKQVRRTE---KKLKDVLLQVEDERRNAE 1859
Cdd:PRK10246 843 TRQGEIRQQLKQDAdnrQQQQALMQQIAQATQQVE 877
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1903 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1603 KQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1683 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDR---------LK 1753
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqaldelLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1754 KANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAA 1833
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1834 SKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1757-1909 |
1.21e-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: 42.60 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1757 LQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQLDNETKERQ----- 1831
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-RLELEIEEVEARIKKYEEQLGNVRNNKEyealq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1832 ----AASKQVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLeeaEEEAQRANASRRKLQRELEDATETA 1907
Cdd:COG1579 96 keieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKI 172
|
..
gi 74180985 1908 DA 1909
Cdd:COG1579 173 PP 174
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1017-1148 |
1.23e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1017 SLAKLKNkheamiTDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEea 1096
Cdd:PRK09039 70 SLERQGN------QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVEL-- 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1097 aqknmalkkireLETQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL 1148
Cdd:PRK09039 142 ------------LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1536-1925 |
1.32e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1536 EMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQ---SEEKKKQLVRQVREMEAELEDERKQRSMAMAAR 1612
Cdd:pfam05622 63 LLQKQLEQLQEENFRLETARDDYRIKCEELEKEVL-ELQHRNEEltsLAEEAQALKDEMDILRESSDKVKKLEATVETYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1613 KKLEmDLKDLEAHIDT----------ANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEilaQAKENEKklksMEAEM 1682
Cdd:pfam05622 142 KKLE-DLGDLRRQVKLleernaeymqRTLQLEEELKKANALRGQLETYKRQVQELHGKLSE---ESKKADK----LEFEY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1683 IQLQEELAAAERAKRQAQQERDELADeianssgkgalaleekrrleariaqleeeleeeqgntelINDRLKKANLQIDQI 1762
Cdd:pfam05622 214 KKLEEKLEALQKEKERLIIERDTLRE---------------------------------------TNEELRCAQLQQAEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1763 NTDLNLERSHAQKNENArqQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEK 1842
Cdd:pfam05622 255 SQADALLSPSSDPGDNL--AAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1843 KLKDVLLQVEDERRNAEQFKDQADKASTrlkqLKRQLEEAEEEAQRANASRRKLQRELEDATETADA-MNREVSSLKNKL 1921
Cdd:pfam05622 333 RILELQQQVEELQKALQEQGSKAEDSSL----LKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSnLAQKIDELQEAL 408
|
....
gi 74180985 1922 RRGD 1925
Cdd:pfam05622 409 RKKD 412
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1018-1420 |
1.34e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKT-------RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEE------ 1084
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyrelRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELtesgdy 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1085 LQAA--LARVEEEAAQKNMALKKIRELETQI-SELQEDLESERASRNKAEKQKRDLGEelealkTELEDTLdstaaqQEL 1161
Cdd:PRK04778 194 VEAReiLDQLEEELAALEQIMEEIPELLKELqTELPDQLQELKAGYRELVEEGYHLDH------LDIEKEI------QDL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1162 RSKREQEVSILKKTLEDEAKTHEAQIQEmrqkhsqAVEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLqgkg 1241
Cdd:PRK04778 262 KEQIDENLALLEELDLDEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELK---- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1242 dsehkrkkveAQLQELQVKF----SEGERVRteladkvtKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL 1317
Cdd:PRK04778 331 ----------EEIDRVKQSYtlneSELESVR--------QLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1318 QEENRQKLSLSTKLKQMEDEKNSFREQLEEeeeakrnlekqiatlhaqvtdMKKKMedgvgcletaEEAKRRLQK-DLEG 1396
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLER---------------------YRNKL----------HEIKRYLEKsNLPG 441
|
410 420
....*....|....*....|....*
gi 74180985 1397 LSQR-LEEKVAAYDKLEKTKTRLQQ 1420
Cdd:PRK04778 442 LPEDyLEMFFEVSDEIEALAEELEE 466
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1050-1297 |
1.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1050 RRKLEGDSTDLS----------DQIAELQAQIAELKMQL----------AKKEEELQA-ALARVEEEAAQKNMALKKIRE 1108
Cdd:PHA02562 152 RRKLVEDLLDISvlsemdklnkDKIRELNQQIQTLDMKIdhiqqqiktyNKNIEEQRKkNGENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1109 LETQISELQEDL-------ESERASRNKAEKQKRDLGEELEALKTEL----EDTLDSTAAQQ-----ELRSKREQEVSIL 1172
Cdd:PHA02562 232 IKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1173 KKTLEDeaktheaqIQEMRQKHSQAVEELADQLEQTKRVKATLEKAKQTLENERGELanevkallqgkgdsehkrKKVEA 1252
Cdd:PHA02562 312 QHSLEK--------LDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA------------------KKVKA 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1253 QLQELQVKF----SEGERVRTELADKVTKLQ------VELDSVTGLLSQSDSKSS 1297
Cdd:PHA02562 366 AIEELQAEFvdnaEELAKLQDELDKIVKTKSelvkekYHRGIVTDLLKDSGIKAS 420
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1619-1873 |
1.40e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1619 LKDLEAHIDTANKNREEAIKQLRKLQAQMKD-------CMRELDDTRASREEIlaqakenEKKLKSMEAEMIQLQeelaa 1691
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQL-------NKQIDELNASIAKLE----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1692 aeraKRQAQQERDeLADEIANSSGKG---ALAL----EEKRRLEaRIaqleeeleeeQGNTELINDRLKKANLQIDQINT 1764
Cdd:PRK11637 117 ----QQQAAQERL-LAAQLDAAFRQGehtGLQLilsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1765 DLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQaaskQVRRTEKKL 1844
Cdd:PRK11637 181 ELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRD----SIARAEREA 256
|
250 260 270
....*....|....*....|....*....|..
gi 74180985 1845 KdvlLQVEDERRNAEQFKD---QADKASTRLK 1873
Cdd:PRK11637 257 K---ARAEREAREAARVRDkqkQAKRKGSTYK 285
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1662-1806 |
1.53e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1662 EEILAQAKEN--EKKLK------SMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalALEEKRRLEARIAQ 1733
Cdd:PRK00409 501 ENIIEEAKKLigEDKEKlneliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKE--------KLQEEEDKLLEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1734 LEeeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQnKELKAKLQEMESAVKSKYK 1806
Cdd:PRK00409 573 KE------------AQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKE 632
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1029-1173 |
1.54e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.29 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1029 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK-KIR 1107
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1108 ELETQISELQEDLES-------ERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILK 1173
Cdd:pfam12795 160 ALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
994-1145 |
1.63e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 994 KKLLEDRVAEFTTNLM----EEEEKSKSLAKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTD-LSDQIAELQ 1068
Cdd:smart00787 139 MKLLEGLKEGLDENLEglkeDYKLLMKELELLNSIKPK-LRDRKDALEEELRQLKQLEDELEDCDPTELDrAKEKLKKLL 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkirELETQISELQEDLESERASRNKAEKQKRDLGEELEALK 1145
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1610-1852 |
1.67e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1610 AARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEilaqakenEKKLKSMEAEMIQLQEEL 1689
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQL--------ESRLAQTLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1690 AAA-----------ERAKRQ---AQQERDELADEIANSS-GKGALALEEKRRLEARI----AQLEEELEEEQGNTELI-- 1748
Cdd:PRK11281 145 AEYnsqlvslqtqpERAQAAlyaNSQRLQQIRNLLKGGKvGGKALRPSQRVLLQAEQallnAQNDLQRKSLEGNTQLQdl 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1749 -NDRLKKANLQIDQINTDLNLERSHAqkNENARQQLERQNKElkakLQEMESAVKSKYKASIAALEAKIAQLEEQLDNET 1827
Cdd:PRK11281 225 lQKQRDYLTARIQRLEHQLQLLQEAI--NSKRLTLSEKTVQE----AQSQDEAARIQANPLVAQELEINLQLSQRLLKAT 298
|
250 260
....*....|....*....|....*
gi 74180985 1828 KERQAASKQVRRTEKKLkDVLLQVE 1852
Cdd:PRK11281 299 EKLNTLTQQNLRVKNWL-DRLTQSE 322
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1032-1160 |
1.73e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.92 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1032 LEERLRREEKQR--QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlakKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PRK00247 288 AEQRAQYREKQKekKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKT---RTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1110 ETQisELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:PRK00247 365 ARQ--ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQV 413
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1588-1860 |
1.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1588 VRQVREMEAELEDERKQRSMAMAA----RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREE 1663
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1664 ILAQAKENEKKLKSMEAEMiqlqEELAAAERAKRQAQQERDELADEIANSSgkgaLALEEKRRLEARIAQLEEELEEEQg 1743
Cdd:COG1340 83 LNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLEWRQQTEV----LSPEEEKELVEKIKELEKELEKAK- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1744 ntelindRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQL 1823
Cdd:COG1340 154 -------KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKA 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 74180985 1824 DNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQ 1860
Cdd:COG1340 226 DELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1638-1796 |
1.80e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1638 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1718 ALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLerSHAQKNenarQQLERQNKELKAKLQE 1796
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV--ALAQRV----QELNRYRSEFFGRLRE 205
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
971-1160 |
1.81e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 971 AKLKKLEEDQIIME----DQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR-QE 1045
Cdd:pfam04012 15 EGLDKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEkKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1046 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARveEEAAQKNMALKK----------IRELEtQISE 1115
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTslgslstssaTDSFE-RIEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74180985 1116 LQEDLESERASRNKAEkQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam04012 172 KIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1058-1135 |
1.88e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKR 1135
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1012-1901 |
2.16e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK----KEEELQ 1086
Cdd:NF041483 360 EDTAAQLAKAARTAEEVLTKASEDAKATTRAaAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKeyraKTVELQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1087 AALARVEEEAAQ----------------KNMALKKIRELETQISEL-----QEDLESERASRNKAEKQKRDLGEELEALK 1145
Cdd:NF041483 440 EEARRLRGEAEQlraeavaegerirgeaRREAVQQIEEAARTAEELltkakADADELRSTATAESERVRTEAIERATTLR 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1146 TELEDTLDSTAAQQE-LRSKREQEVSILKKTLEDEAK-THEAQIQEMRQKHSQAVEELAD-QLEQTKRVKA---TLEKAK 1219
Cdd:NF041483 520 RQAEETLERTRAEAErLRAEAEEQAEEVRAAAERAAReLREETERAIAARQAEAAEELTRlHTEAEERLTAaeeALADAR 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1220 QTLENERGELANEVKAL----------LQGKGDSEHKRKKVEAQLQELQVKfSEGE----RVRTELADKVTKLQVEL-DS 1284
Cdd:NF041483 600 AEAERIRREAAEETERLrteaaerirtLQAQAEQEAERLRTEAAADASAAR-AEGEnvavRLRSEAAAEAERLKSEAqES 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1285 VTGLLSQSDSKSSKLTKDfsALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRN-LEKQIATLH 1363
Cdd:NF041483 679 ADRVRAEAAAAAERVGTE--AAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKrVEEAQAEAQ 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1364 AQVTDMKKKMEDGVGcleTAEEAKRRLQKDLEGLSQRLEEKV-----AAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSN 1438
Cdd:NF041483 757 RLVEEADRRATELVS---AAEQTAQQVRDSVAGLQEQAEEEIaglrsAAEHAAERTRTEAQEEADRVRSDAYAERERASE 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1439 LEKKQKKfdqlLAEEKTISAKYAEERDRAEA--EAREKETKALSLA-RALEEAMEQKAELERLNKQFRTEM-EDLMSSKD 1514
Cdd:NF041483 834 DANRLRR----EAQEETEAAKALAERTVSEAiaEAERLRSDASEYAqRVRTEASDTLASAEQDAARTRADArEDANRIRS 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1515 DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK------AQFER------DLQGRDEQSEE 1582
Cdd:NF041483 910 DAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQliaeatGEAERlraeaaETVGSAQQHAE 989
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1583 KKKQLVRQVREmEAELEDERKQRSMAMAARKKLEMDLKDleahidtANKNREEAIKQLRKLQAQMKDCMRELddTRASRE 1662
Cdd:NF041483 990 RIRTEAERVKA-EAAAEAERLRTEAREEADRTLDEARKD-------ANKRRSEAAEQADTLITEAAAEADQL--TAKAQE 1059
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL-ADEIANSSGKGALALEEKrrleariaqleeeleee 1741
Cdd:NF041483 1060 EALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTdADELLVGARRDATAIRER----------------- 1122
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1742 qgnTELINDRLKKanlQIDQINtdlnlERSHAQKNENARQQLERQNKELKAKLQEMESAvkskykasiaalEAKIAQLEE 1821
Cdd:NF041483 1123 ---AEELRDRITG---EIEELH-----ERARRESAEQMKSAGERCDALVKAAEEQLAEA------------EAKAKELVS 1179
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1822 QLDNE-TKERQAAskqVRRTEKKLKDVLLQVEDERRNAEQFKDQADKASTRL-KQLKRQLEEAEEEAQRANASRRKLQRE 1899
Cdd:NF041483 1180 DANSEaSKVRIAA---VKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQDV 1256
|
..
gi 74180985 1900 LE 1901
Cdd:NF041483 1257 LE 1258
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1453-1603 |
2.50e-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: 42.18 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1453 EKTISAKYAEERDRAEAEAREKETKAL-SLARALEEAMEQ------------KAELERLNKQFRTEM----------EDL 1509
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRCQALLqELSAPLEEKISQgsysvpggyqlyLEDREKLVEKYRQVPrkgvkaeevlQEF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1510 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL-QGRDEQSEEKKKQLV 1588
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrQLKEKMEEERENLLK 255
|
170
....*....|....*
gi 74180985 1589 RQVREMEAELEDERK 1603
Cdd:cd16269 256 EQERALESKLKEQEA 270
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1578 |
2.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1247 RKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1327 LSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVA 1406
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1407 AydKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALE 1486
Cdd:COG4372 179 A--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1487 EAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1566
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|..
gi 74180985 1567 AQFERDLQGRDE 1578
Cdd:COG4372 337 AELADLLQLLLV 348
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
957-1182 |
2.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 957 SARQKL--QLEKVTTEAKLKKLEEDQIIMEDQNCK-LAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKlknKHEAMITDLE 1033
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIRELNQQIQtLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1034 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA--KKEEE--------------LQAALARVEEEAA 1097
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKmyekggvcptctqqISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1098 QKNMALKKIRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR---EQEVSILKK 1174
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQD 386
|
....*...
gi 74180985 1175 TLEDEAKT 1182
Cdd:PHA02562 387 ELDKIVKT 394
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
964-1115 |
2.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 964 LEKVTTEAKLKKLEE--DQIIMEDQN-CKLAKEKKLLE--DRVAEFTTNLMEE-EEKSKSLAKLKNK---HEAMITDLEE 1034
Cdd:PRK12704 24 VRKKIAEAKIKEAEEeaKRILEEAKKeAEAIKKEALLEakEEIHKLRNEFEKElRERRNELQKLEKRllqKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1035 RLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK-----KEEELQAALARVEEEAAQKNMALkkIREL 1109
Cdd:PRK12704 104 LLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltAEEAKEILLEKVEEEARHEAAVL--IKEI 178
|
....*.
gi 74180985 1110 ETQISE 1115
Cdd:PRK12704 179 EEEAKE 184
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1631-1913 |
2.71e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1631 KNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1711 ANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKEL 1790
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1791 KAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEKKLKDvllqvEDERRNAEQFKDQADKAST 1870
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-----AKLKEEELELKSEEEKEAQ 408
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 74180985 1871 RLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1718-1923 |
2.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1718 ALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLnlERSHAQKnENARQQLERQNKELKAKLQEM 1797
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--EALQAEI-DKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1798 ESAVKSKYKASIAA------LEAKiaQLEEQLDnetkeRQAASKQVRRTEKKLkdvLLQVEDERRNAEQFKDQADKASTR 1871
Cdd:COG3883 89 GERARALYRSGGSVsyldvlLGSE--SFSDFLD-----RLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1872 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1578-1714 |
2.73e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNRE------------EAIKQLRKLQA 1645
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaaltkgneelarEALAEKKSLEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1646 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSS 1714
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLGSLSTSSATDS 165
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
851-1201 |
2.76e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 851 EAELTKVREKHLAAENRLTEMETMQSQLMAEKLQlqEQLQAETELCAEAEELRARLTAKKQELeeichdleARVEEEEER 930
Cdd:PLN03229 435 EGEVEKLKEQILKAKESSSKPSELALNEMIEKLK--KEIDLEYTEAVIAMGLQERLENLREEF--------SKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 931 CQYLQAEK-KKMQQNIQELEEQLEEEESARQKLQlekvtteaKLKKLEEDQIIMEdQNCKLAKEKKLLEDRVAEfTTNLM 1009
Cdd:PLN03229 505 MHPVLMEKiEKLKDEFNKRLSRAPNYLSLKYKLD--------MLNEFSRAKALSE-KKSKAEKLKAEINKKFKE-VMDRP 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1010 EEEEKSKSL-AKLKNKHEAMITDLEERLRRE-EKQRQELEKTRRKLEgDSTDLsdQIAELQAQIAELKMQLAkkEEELQA 1087
Cdd:PLN03229 575 EIKEKMEALkAEVASSGASSGDELDDDLKEKvEKMKKEIELELAGVL-KSMGL--EVIGVTKKNKDTAEQTP--PPNLQE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1088 ALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTL----DSTAAQQELRS 1163
Cdd:PLN03229 650 KIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIaealNSSELKEKFEE 723
|
330 340 350
....*....|....*....|....*....|....*...
gi 74180985 1164 KREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:PLN03229 724 LEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRVEV 761
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1154-1403 |
2.84e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1154 STAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEeladqleQTKRVKATLEK-AKQTLENERGELANE 1232
Cdd:pfam05667 155 GSRALRPFHTQTLVLPGRKGKTLKNSKELKEFYSEYLPPVTAQPSS-------RASVVPSLLERnAAELAAAQEWEEEWN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1233 VKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTK----------- 1301
Cdd:pfam05667 228 SQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKgsrfthteklq 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1302 ---DFSALESQL---QDTQELLQEENRQKLS--------LSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVt 1367
Cdd:pfam05667 308 ftnEAPAATSSPptkVETEEELQQQREEELEelqeqledLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY- 386
|
250 260 270
....*....|....*....|....*....|....*.
gi 74180985 1368 DMKKKMedgVGCLETAEEAKRRLQKDLEGLSQRLEE 1403
Cdd:pfam05667 387 KVKKKT---LDLLPDAEENIAKLQALVDASAQRLVE 419
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1533-1921 |
3.04e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1533 QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLvRQVREMEAELEDE-RKQRSMAMAA 1611
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEAlREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1612 RKKLEMDLKDLEAHIDTANKNRE--EAIKQ-LRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEaemiQLQEE 1688
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREviSCLKNeLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1689 LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLeARIAQLEEELeeeqgntelinDRLKKANLQIDQINTDLNL 1768
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKEL-----------ERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1769 ershaqknenarqqLERQNKELKAKLQEMEsavksKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTEK-KLKDV 1847
Cdd:pfam05557 226 --------------LKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1848 LLQVEDERRNAEQFKDQADKASTR---------LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1918
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEkarreleqeLAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYD 366
|
...
gi 74180985 1919 NKL 1921
Cdd:pfam05557 367 KEL 369
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1635-1836 |
3.31e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1635 EAIKQLRKLQAQMKDCMRELDDTRASREEI-LAQAKENEkklksmEAEMIQLQEELAAAERAKRQAQQERDELADE---I 1710
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELeAAALQPGE------EEELEEERRRLSNAEKLREALQEALEALSGGeggA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1711 ANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLE-RQN-- 1787
Cdd:COG0497 243 LDLLGQALRALERLAEYDPSLAE--------------LAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAll 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74180985 1788 ------------------KELKAKLQEMESAvkskyKASIAALEAKIAQLEEQLDNE----TKERQAASKQ 1836
Cdd:COG0497 309 rrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAaeklSAARKKAAKK 374
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1002-1142 |
3.54e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 41.77 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1002 AEFTTNLME--EEEKSKSlAKLKNKHEAMITDLEERLRRE--------EKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1071
Cdd:pfam03148 203 EKFTQDNIEraEKERAAS-AQLRELIDSILEQTANDLRAQadavnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1072 AELKMQLAKKEEELQAALARVEEEAAQKNMAL----------KKIRELETQISELQEDLESERASRNKAEKQKRDLGEEL 1141
Cdd:pfam03148 282 EALEKAIRDKEAPLKLAQTRLENRTYRPNVELcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDI 361
|
.
gi 74180985 1142 E 1142
Cdd:pfam03148 362 A 362
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
844-1088 |
3.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 844 EDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEICHDLEAR 923
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 924 VEEeeercqylqaekkkMQQNIQELEEQLEEEES-----ARQKLQLEKVTTEAKLKKLEEdqiIMEDQNcKLAKEKKLLE 998
Cdd:COG3883 92 ARA--------------LYRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEE---LKADKA-ELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 999 DRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250
....*....|
gi 74180985 1079 AKKEEELQAA 1088
Cdd:COG3883 234 AAAAAAAAAA 243
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1289-1559 |
3.58e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1289 LSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQklslSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTD 1368
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1369 MKKkmedgVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDL----DHQRQSVSNLEKKQK 1444
Cdd:pfam15905 134 LTR-----VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqknlEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1445 KFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELE 1524
Cdd:pfam15905 209 STEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE 288
|
250 260 270
....*....|....*....|....*....|....*
gi 74180985 1525 KSKralEQQVEEMKTQLEELEDELQATEDaKLRLE 1559
Cdd:pfam15905 289 SEK---EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1523-1727 |
3.64e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1523 LEKSK-RALEQQVEEMKTQLEELEDELQATEDaklrLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1601
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1602 RKQRSMAMAARKKLEMDLKDLEAHIDTANK----------------NREEAIKQLRKLQAQMKDC---MRELDDTRASRE 1662
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELqhsLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74180985 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRL 1727
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1131-1223 |
3.70e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1131 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvsilKKTLEDEAKTHEAQIQEMRQKHSQ-AVEELADQLEQTK 1209
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQE----LVALEGLAAELEEKQQELEAQLEQlQEKAAETSQERKQ 216
|
90
....*....|....
gi 74180985 1210 RVKATLEKAKQTLE 1223
Cdd:PRK11448 217 KRKEITDQAAKRLE 230
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1047-1241 |
4.06e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1047 EKTRRKLEgDSTDLSDQIA----ELQAQ-IAELKMQLAKKEEELQAALARVEEEAAQknmalKKIRELETQiselQEDLE 1121
Cdd:PTZ00491 643 ERTRDSLQ-KSVQLAIEITtksqEAAARhQAELLEQEARGRLERQKMHDKAKAEEQR-----TKLLELQAE----SAAVE 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1122 SERASRNKAEKqkrdlgeELEALKTELEDTLDstaaQQELRSKREQevsILKKT-LEDEAKTHEAQIQEMRQKHSQAVE- 1199
Cdd:PTZ00491 713 SSGQSRAEALA-------EAEARLIEAEAEVE----QAELRAKALR---IEAEAeLEKLRKRQELELEYEQAQNELEIAk 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1200 --ELADqLEQTK--RVKATLekAKQTLEnergELAN---EVKA-LLQGKG 1241
Cdd:PTZ00491 779 akELAD-IEATKfeRIVEAL--GRETLI----AIARagpELQAkLLGGLG 821
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1052-1206 |
4.13e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.32 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1052 KLEGDSTDLSDQIAELQAQIA----ELKMQLAKKEEELQAALARVEEEAAQK---------NMALKKIRELETQISELQE 1118
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKlepyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1119 DLEsERASRnKAEKQKRDLGEELEALKTELEDTLDSTAAQ-----QELRSKREQEVSILKKTLEDEAKTHEAQ----IQE 1189
Cdd:pfam01442 81 ELR-KRLNA-DAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQE 158
|
170
....*....|....*..
gi 74180985 1190 MRQKHSQAVEELADQLE 1206
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1467-1733 |
4.32e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1467 AEAEAREKETKALSLARALEEA----MEQKaELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1542
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEArqarLERE-KAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1543 EledelqatedaklrlevNLQAMKAQFERDLQGRDEQSEEKkkqlvrqvremEAELEDERK---QRSMAMAARKKLEMDL 1619
Cdd:PRK05035 515 D-----------------NSAVIAAREARKAQARARQAEKQ-----------AAAAADPKKaavAAAIARAKAKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1620 KDLEAHIDTANK----NREEAIKQLRKLQAQMKD-----CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:PRK05035 567 ANAEAEEEVDPKkaavAAAIARAKAKKAAQQAASaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 74180985 1691 AAE----RAK-RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQ 1733
Cdd:PRK05035 647 AVAaaiaRAKaRKAAQQQANAEPEEAEDPKKAAVA-AAIARAKAKKAA 693
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1608-1830 |
4.33e-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: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1608 AMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQE 1687
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1688 ELAAAERAKrqaqqERDELADEIANssgkgalaleekrrLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLn 1767
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIES--------------LKRRI--------------SDLEDEILELMERIEELEEEL- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1768 lershaqknENARQQLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQLDNETKER 1830
Cdd:COG1579 127 ---------AELEAELAELEAELEEKKAELDEELA-ELEAELEELEAEREELAAKIPPELLAL 179
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1110-1447 |
4.37e-03 |
|
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: 42.03 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1110 ETQISELQEDLESERASRNKAEK-----QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvsiLKKTLEDEAKTHE 1184
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1185 AQIQEmrqkhsqavEELADQLEQTKRVKATLEKAKQTLENERGELANEVKALLQgkgDSEHKRKKVEAQLQELQVKFSEG 1264
Cdd:pfam17380 363 ERIRQ---------EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1265 ERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDfsaLESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQ 1344
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1345 LEEEEEAKRNLEKQIATLHAQVTDMKKKMEdgvgcletAEEaKRRLQKDLEGlSQRLEEKVAaydKLEKTKTRLQqeldD 1424
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRRE--------AEE-ERRKQQEMEE-RRRIQEQMR---KATEERSRLE----A 570
|
330 340
....*....|....*....|...
gi 74180985 1425 LLVDLDHQRQSVSNlEKKQKKFD 1447
Cdd:pfam17380 571 MEREREMMRQIVES-EKARAEYE 592
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1047-1277 |
4.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1047 EKTRRKLEGDSTDLSDQIAELQAQiaelKMQLAKKEEELQAALARVEEeaaqknmalkkireletqiseLQEDLEseras 1126
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAEK---------------------LKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1127 rnkaeKQKRDLGEELEALKTELEDtldstAAQQELRSKREQEVSILKKTLEDEAKTHEA----QIQEMRQKHSQAVEELa 1202
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASvkahELIEARKRLNKANEKK- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1203 dqleqtkrVKATLEKAKQTLENERGElanEVKAL-LQGKGDSEHKRKKVEAQLQE----LQVKFSEGERVRTELADKVTK 1277
Cdd:PRK00409 624 --------EKKKKKQKEKQEELKVGD---EVKYLsLGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1432-1728 |
4.85e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1432 QRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSlaRALEEAMEQKAELERLN-KQFRTEMEDLM 1510
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS--DKLEKLVEQNTDLRLEKlGENAESSKRLN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1511 SSKDDVGKSVHELEKSKRALEQQVEeMKTQLEELEDELQATE------DAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK 1584
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSID-IKKATESLEEQLAAAEaeqeleESKRETETGIQNLTAEIEQGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1585 KQL-----VRQVREMEAELEDERKQRS--------MAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCM 1651
Cdd:COG5185 361 EEIenivgEVELSKSSEELDSFKDTIEstkesldeIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1652 RELDDTRASREEILAQAKENEKKLKSMEAEMIQ--LQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLE 1728
Cdd:COG5185 441 KLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1513-1648 |
4.85e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1513 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdeQSEEKKKQLVRQVR 1592
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLE----EAEKEAQQAIKEAK 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1593 -EMEAELEDERKQRSMAMAARKklEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMK 1648
Cdd:PRK00409 584 kEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1436-1598 |
4.87e-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: 40.68 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKaELERLNKQfrtemedlmsskdd 1515
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKE-------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1516 vgksVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1595
Cdd:COG1579 98 ----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
...
gi 74180985 1596 AEL 1598
Cdd:COG1579 174 PEL 176
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1408-1841 |
5.08e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1408 YDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLaeEKTISAKYAEERDRAEAEAREKETKALS---LARA 1484
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKALMdeiRARL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1485 LEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQA 1564
Cdd:COG5278 159 LLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAAL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1565 MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQ 1644
Cdd:COG5278 239 ALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1645 AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1724
Cdd:COG5278 319 AAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1725 RRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSK 1804
Cdd:COG5278 399 AAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALA 478
|
410 420 430
....*....|....*....|....*....|....*..
gi 74180985 1805 YKASIAALEAKIAQLEEQLDNETKERQAASKQVRRTE 1841
Cdd:COG5278 479 AAAAALAEAEAAAALAAAAALSLALALAALLLAAAEA 515
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1773-1923 |
5.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1773 AQKNENARQQLERQNKELKAKLQEMESAVKSKYKasiaaleakiaQLEEQLDNETKERQaasKQVRRTEKKLKDVLLQVE 1852
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH-----------KLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74180985 1853 DERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRAnasRRKLQRELEDATE-TAD-AMNREVSSLKNKLRR 1923
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL---IEEQLQELERISGlTAEeAKEILLEKVEEEARH 169
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1442-1605 |
5.27e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1442 KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH 1521
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1522 ELEKSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREmEAELEDE 1601
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EADLEAE 175
|
....
gi 74180985 1602 RKQR 1605
Cdd:PRK12705 176 RKAQ 179
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1384-1670 |
5.66e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1384 EEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTktrlqqELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEE 1463
Cdd:COG5185 281 NENANNLIKQFENTKEKIAEYTKSIDIKKAT------ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1464 RDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSvheLEKSKRALEQQVEEMKTQLEE 1543
Cdd:COG5185 355 NLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---LEDTLKAADRQIEELQRQIEQ 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1544 LEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDERKQrsmamaARKKLEMDLKDLE 1623
Cdd:COG5185 432 ATSSNEEVSKLLNELISELNKVMREADEESQ---SRLEEAYDEINRSVRSKKEDLNEELTQ------IESRVSTLKATLE 502
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 74180985 1624 AHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE 1670
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1437-1730 |
5.72e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1437 SNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFrtemEDLMSSKDDV 1516
Cdd:PRK04778 119 EDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF----VELTESGDYV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1517 GKSVH--ELEKSKRALEQQVEEMKTQLEELEDELQA------------TED----AKLRLEVNLQAMKAQFERDL----Q 1574
Cdd:PRK04778 195 EAREIldQLEEELAALEQIMEEIPELLKELQTELPDqlqelkagyrelVEEgyhlDHLDIEKEIQDLKEQIDENLalleE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1575 GRDEQSEEKKKQLVRQVREMEAELEDErkqrsmaMAARKKLEMDLKDLEAHIDTANKNR-----------------EEAI 1637
Cdd:PRK04778 275 LDLDEAEEKNEEIQERIDQLYDILERE-------VKARKYVEKNSDTLPDFLEHAKEQNkelkeeidrvkqsytlnESEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1638 KQLRKLQAQMKDCMRELDDTRASRE-------EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:PRK04778 348 ESVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
330 340
....*....|....*....|
gi 74180985 1711 ANSsgkgalaleeKRRLEAR 1730
Cdd:PRK04778 428 HEI----------KRYLEKS 437
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
1105-1548 |
5.80e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 41.77 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1105 KIRELETQISELQEDLESERASRNKAEKQKrdlgEELEALKTELEDTLDSTAAQQ-----ELRSKREQEVSILK--KTLE 1177
Cdd:pfam09730 28 KEAYYAQRILELQNELKQARAVLSNTQAEN----ERLASLSQELKEECECVELQRgrmrdEIKEYKVREARLLQdySELE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1178 DEAKTHEAQIQEMRQ--------KH-----SQAVEELADQLEQTKRVKA----TLEKAKQTLENERgELANEVKALLQGK 1240
Cdd:pfam09730 104 EENISLQKQVSVLKQnqvefeglKHeitrkEEETELLNSQLEEAIRLREiaerQLDEALETLKTER-EQKNSLRKELSHY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1241 GDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVTKLQVELDSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:pfam09730 183 MTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRKSEVFPPAPSLVSDLLSEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1321 NrqkLSLSTKLKQmedeknsfreQLEEeeeakrnLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLsQR 1400
Cdd:pfam09730 263 N---ISEIQKLKQ----------QLIQ-------VEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM-RG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1401 LEEKVAAYDKLEKTKTRLQQELDD--------LLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAr 1472
Cdd:pfam09730 322 LQASKERQDALDSEKDRDSHEDGDyyevdingPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAEA- 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74180985 1473 eketkalslaralEEAMEQKAELERLNKQFRTEMEdlmsskddvgksvhELEKSKRALEQQVEEMKTQLEELEDEL 1548
Cdd:pfam09730 401 -------------QDLAEKIRQLEKASHQDQERIA--------------HLEKELGKTRKVAGESEGSLSVAQDEL 449
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1765-1923 |
5.89e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1765 DLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQ------LEEQLDNETKERQAAS---- 1834
Cdd:COG3206 102 KLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEISYTSPDPELAAAVANalaeayLEQNLELRREEARKALefle 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1835 KQVRRTEKKLKDVLLQVED--ERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAM-- 1910
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlq 261
|
170
....*....|...
gi 74180985 1911 NREVSSLKNKLRR 1923
Cdd:COG3206 262 SPVIQQLRAQLAE 274
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1001-1226 |
5.98e-03 |
|
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: 41.48 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1001 VAEFTTNLMEEEEKSKSLAKlknkhEAMITDLEE--------RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1072
Cdd:pfam15709 302 TFVVTGNMESEEERSEEDPS-----KALLEKREQekasrdrlRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1073 ELKMQLAKKEEELQAALARVEEEAAQknmalkkiRELETQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:pfam15709 377 ELELEQQRRFEEIRLRKQRLEEERQR--------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1153 DSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELADQLEQTKRVkATLEKAKQTLENER 1226
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL-ALEEAMKQAQEQAR 521
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
865-1154 |
6.11e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 865 ENRLTEMETMQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQYLQAEKKKMQQN 944
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELK---ELAEKRDELNAQVKELREEAQE----LREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 945 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLedrvaefttnlmeeeEKSKSLAKLKNK 1024
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELV---------------EKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1025 HEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK 1104
Cdd:COG1340 152 AKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1105 KIRELETQISELQEDLESERASRNKAEKQKRDlgEELEALKTELEDTLDS 1154
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKK 278
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
880-1716 |
6.25e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 880 AEKLQLQEQLQAEtELCAEAEELRARLTAK----KQELEEICHDLEARVEEEEERCQYLQAEKKKmqqnIQELEEQLEEE 955
Cdd:NF041483 220 AERLLNAASTQAQ-EATDHAEQLRSSTAAEsdqaRRQAAELSRAAEQRMQEAEEALREARAEAEK----VVAEAKEAAAK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 956 ESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKS---------LAKLKNKHE 1026
Cdd:NF041483 295 QLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTvaaedtaaqLAKAARTAE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1027 AMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQiaeLKMQLAKKEEELQAALARVEEEAaqknmalkk 1105
Cdd:NF041483 375 EVLTKASEDAKATTRAaAEEAERIRREAEAEADRLRGEAADQAEQ---LKGAAKDDTKEYRAKTVELQEEA--------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1106 iRELETQISELQEDLESErASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEA 1185
Cdd:NF041483 443 -RRLRGEAEQLRAEAVAE-GERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1186 QIQEMRQKHSQAVEEL-ADQLEQTKRVKATLEKAKQTL--ENERGELANEVKA---LLQGKGDSEHKRKKVEAQLQELQv 1259
Cdd:NF041483 521 QAEETLERTRAEAERLrAEAEEQAEEVRAAAERAARELreETERAIAARQAEAaeeLTRLHTEAEERLTAAEEALADAR- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1260 kfSEGERVRTELADKVTKLQVEL-DSVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEK 1338
Cdd:NF041483 600 --AEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1339 NSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETA--------EEAKRRLQKDLEGLSQRLEEKVAAYDK 1410
Cdd:NF041483 678 SADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSAraeadqerERAREQSEELLASARKRVEEAQAEAQR 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1411 LEKTKTRLQQELDDLLVDLDHQ-RQSVSNLEKKqkkfdqllAEEKTISAKYAEER--DRAEAEAREKETKALSLARALEE 1487
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQvRDSVAGLQEQ--------AEEEIAGLRSAAEHaaERTRTEAQEEADRVRSDAYAERE 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1488 AMEQKAELERLNKQFRTEMEDLMSSKdDVGKSVHELEKSKRALEQQVEEMKTqleELEDELQATEDAKLRlevnlqaMKA 1567
Cdd:NF041483 830 RASEDANRLRREAQEETEAAKALAER-TVSEAIAEAERLRSDASEYAQRVRT---EASDTLASAEQDAAR-------TRA 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1568 QFERDLQGRDEQSEEKKKQLVrqvreMEAELEDERKQRSMAMAARKKLEMDLKDleahidtANKNREEAIKQLRKLQAqm 1647
Cdd:NF041483 899 DAREDANRIRSDAAAQADRLI-----GEATSEAERLTAEARAEAERLRDEARAE-------AERVRADAAAQAEQLIA-- 964
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1648 kDCMRELDDTRASREEILAQAKENEKKLKSmEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGK 1716
Cdd:NF041483 965 -EATGEAERLRAEAAETVGSAQQHAERIRT-EAERVKAEAA-AEAERLRTEAREEADRTLDEARKDANK 1030
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1526-1721 |
7.08e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1526 SKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLvrqvremeaELEDERKQR 1605
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQL---------ATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1606 SMAMAARKKLEMDlkdleahidtanKNREEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSMEAEM 1682
Cdd:pfam09787 112 AEAELERLQEELR------------YLEEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74180985 1683 IQLQEELAA--AERAKRQAQQERDELADEIANSSGKGALAL 1721
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGTSI 220
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1500-1710 |
7.12e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATED-AKLRLEVNLQAMKAQFERD-----L 1573
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEErLAEALEKLEEAEKAADESErgrkvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1574 QGRDEQSEEKKKQLVRQVRemEAELEDERKQRSMAMAARKklemdLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRE 1653
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLK--EAKEIAEEADRKYEEVARK-----LVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74180985 1654 LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1438-1647 |
7.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1438 NLEKKQKKFDQLLAEEKTISAkyAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvg 1517
Cdd:COG3206 190 ELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1518 kSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG3206 264 -VIQQLRAQLAELEAELAELSARYTPNHPDVIA-----------LRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74180985 1598 LEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQM 1647
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1658-1909 |
7.31e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1658 RASREEILAQAKENEK----KLKsMEAEMIQL-QEELAAAERAKRQAQQERDELADEIAnssgkGALAleekrRLEARIA 1732
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKaeeaKAR-FEARQARLeREKAAREARHKKAAEARAAKDKDAVA-----AALA-----RVKAKKA 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1733 QLEEELEEEQG----NTELINDR----LKKANLQIDQINTDLNLERSHAQKNENARQQLERQnkELKAKLQEMESAVKSK 1804
Cdd:PRK05035 501 AATQPIVIKAGarpdNSAVIAARearkAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKA--AQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1805 yKASIAA--LEAKIAQLEEQLDNETKERQAASKQvrrtEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKqlKRQLEEA 1882
Cdd:PRK05035 579 -KAAVAAaiARAKAKKAAQQAASAEPEEQVAEVD----PKKAAVAAAIARAKAKKAEQQANAEPEEPVDPR--KAAVAAA 651
|
250 260
....*....|....*....|....*..
gi 74180985 1883 EEeaqRANASRRKLQRELEDATETADA 1909
Cdd:PRK05035 652 IA---RAKARKAAQQQANAEPEEAEDP 675
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1610-1711 |
7.77e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1610 AARKKLEMD-----LKDLEAHIDTANKNREEAIK--------QLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEK 1673
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasfeRLAELRDELAELEEELEALKArweAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 74180985 1674 KLKSMEAEMIQLQEELAAAERAKRQAQQ-ERDEL-ADEIA 1711
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPlLREEVtEEDIA 518
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1189 |
8.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 967 VTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEfttnLMEE-EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQE 1045
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEE----LNEEyNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1046 LEKTRRKL--EG----------DSTDLSDQIAELQA--QIAELKMQLAKKEEELQAALARVEEEA-AQKNMALKKIRELE 1110
Cdd:COG3883 88 LGERARALyrSGgsvsyldvllGSESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1111 TQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQE 1189
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1490-1625 |
8.97e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1490 EQKAELERLNKQfrtEMEDLMSSKDDVgksVHELEKSKRALEQ---QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1566
Cdd:pfam05911 677 DLKTEENKRLKE---EFEQLKSEKENL---EVELASCTENLEStksQLQESEQLIAELRSELASLKESNSLAETQLKCMA 750
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 74180985 1567 AQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAMAARKKLEMDLKDLEAH 1625
Cdd:pfam05911 751 ESYE-DLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1063-1158 |
9.07e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.03 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalkkIRELETQISELQEDLESERASRNKAEKQkrDLGEELE 1142
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAA--------TAALEARLAALRAALAAAREAVAAAAAA--ALEARLA 70
|
90
....*....|....*.
gi 74180985 1143 ALKTELEDTLDSTAAQ 1158
Cdd:COG4223 71 ALEAKAAAPEAEAAAA 86
|
|
| RUN_RUNDC1 |
cd17683 |
RUN domain found in RUN domain-containing protein 1 (RUNDC1) and similar proteins; RUN ... |
1531-1625 |
9.22e-03 |
|
RUN domain found in RUN domain-containing protein 1 (RUNDC1) and similar proteins; RUN domain-containing protein 1 (RUNDC1) is thought to a role as p53/TP53 inhibitor and as such may have oncogenic activity. This model contains the RUN domain.
Pssm-ID: 439045 Cd Length: 248 Bit Score: 39.91 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1531 EQQVEEMKTQLEELE---DELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEkkkqlvrqvREMEAELEDERKQRSM 1607
Cdd:cd17683 2 EQLVDQLKTQISDLErfiNFLQHWGDLRARLEIAVNRVIELAETQQRLDEEDSSS---------YTDSSDDPVVRSEDEL 72
|
90
....*....|....*...
gi 74180985 1608 AMAARKKLEMDLKDLEAH 1625
Cdd:cd17683 73 TTAVRKELAPALRDLLQH 90
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1056-1133 |
9.31e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 9.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74180985 1056 DSTDLSDQIAELQAQIAELKMQLakkeEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERASRNKAEKQ 1133
Cdd:COG0845 55 DPPDLQAALAQAQAQLAAAQAQL----ELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARAN 128
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1520-1789 |
9.66e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1520 VHELEKSKRALEQQVEEMK---------------TQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKK 1584
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRqkkgaepsrlyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAE-DFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1585 kqlvrqvREMEAELEDERKQRSMAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKlQAQMKDCMRELDDTR-----A 1659
Cdd:pfam00038 99 -------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQA-QVSDTQVNVEMDAARkldltS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1660 SREEILAQAKENEKKLKsMEAEM---IQLQEELAAAERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEE 1736
Cdd:pfam00038 171 ALAEIRAQYEEIAAKNR-EEAEEwyqSKLEELQQAAARNGDALRSAKEEIT--------------ELRRTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 74180985 1737 ELEEEQGNTELINDRLKKANLQIDQINTDL-NLERSHAQknenARQQLERQNKE 1789
Cdd:pfam00038 236 LKKQKASLERQLAETEERYELQLADYQELIsELEAELQE----TRQEMARQLRE 285
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1245-1527 |
9.95e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1245 HKRKKVEaQLQELQVkFSEgervrtelADKVTKlqvelDSVTGLLSQSDSKSSKLtkdfSALESQLqDTQELLQEEnrqk 1324
Cdd:PHA02562 151 ARRKLVE-DLLDISV-LSE--------MDKLNK-----DKIRELNQQIQTLDMKI----DHIQQQI-KTYNKNIEE---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1325 lsLSTKLKQMEDEKNSFREQLEEEEeakRNLEKQIATLHAQVTDMKKKMEDGVGCLetaeeakrrlqKDLEGLSQRLEEK 1404
Cdd:PHA02562 207 --QRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAAL-----------NKLNTAAAKIKSK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74180985 1405 VAAYDKLEKTKTRLQ------QELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKA 1478
Cdd:PHA02562 271 IEQFQKVIKMYEKGGvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNK 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74180985 1479 LSLARALEEAMEQKAELERLNKQF---RTEMEDLMSSKDDVGKSVHELEKSK 1527
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| |
