|
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 ... |
838-1918 |
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: 1408.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 838 TRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDM 917
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 918 ESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDR 997
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 998 IAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLAN 1077
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1078 KEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQE 1157
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1158 LRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSK 1237
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1238 SDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEE 1317
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1318 TRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQ 1397
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1398 LEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALT 1477
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1478 LARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEV 1557
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1558 NMQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQL 1637
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1638 KKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSML 1717
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1718 QDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELEST 1797
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1798 IKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLE 1877
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 768942001 1878 EAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSKL 1918
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-761 |
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: 1381.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQ-------GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 245
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 246 YIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFH 325
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 326 IMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQ 405
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 406 EQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 485
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 486 EQEEYQREGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVD 565
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 566 FCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSDSTYGAFKTRKGMFRTVGQ 645
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 646 LYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNA 725
Cdd:cd14932 561 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 768942001 726 IPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14932 641 IPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
93-761 |
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: 1308.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKD----QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 248
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 249 GANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYR-FLSNGNMTIPGLQDKELFAETMEAFHIM 327
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 SIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQ 407
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 408 AEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFGLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK-FQKPKKLKDDVDF 566
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 567 CIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhivgldkvagMSDSTYGAFKTRKGMFRTVGQL 646
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYE----------ESGGGGGKKKKKGGSFRTVSQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 647 YKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAI 726
Cdd:cd01377 548 HKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAI 627
|
650 660 670
....*....|....*....|....*....|....*
gi 768942001 727 PKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd01377 628 PKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 1289.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKD---QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSI 329
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 330 PEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 489
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 490 YQREGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFCII 569
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 570 HYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSDSTYGA-FKTRKGMFRTVGQLYK 648
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSaYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 649 EQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPK 728
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 768942001 729 GFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-761 |
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: 1233.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQ-------GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 245
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 246 YIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFH 325
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 326 IMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQ 405
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 406 EQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 485
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 486 EQEEYQREGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVD 565
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 566 FCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSDsTYGAFKTRKGMFRTVGQ 645
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE-MPGAFKTRKGMFRTVGQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 646 LYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNA 725
Cdd:cd15896 560 LYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 768942001 726 IPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd15896 640 IPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 1212.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSIPEE 332
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 333 ERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAV 412
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 413 EALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 492
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 493 EGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFCIIHYA 572
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 573 GKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSDSTY-GAFKTRKGMFRTVGQLYKEQL 651
Cdd:cd14919 481 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpGAFKTRKGMFRTVGQLYKEQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 652 GNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKGFM 731
Cdd:cd14919 561 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 768942001 732 DGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14919 641 DGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
93-761 |
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: 1148.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQ---GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSI 329
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 330 PEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 489
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 490 YQREGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFCII 569
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 570 HYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSDSTY-GAFKTRKGMFRTVGQLYK 648
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLpSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 649 EQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPK 728
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 768942001 729 GFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
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 ... |
93-761 |
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: 1137.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSfKSKKD-------------QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 239
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 240 NFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAE 319
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 320 TMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYV 399
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 400 QKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 479
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 480 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKpKK 559
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 560 LKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhIVGLDKVAgMSDSTYGAfKTRKGM 639
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA-RTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 640 FRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 719
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 768942001 720 ILTPNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 1095.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQG---ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGlQDKELFAETMEAFHIMSI 329
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 330 PEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 489
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 490 YQREGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFCII 569
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 570 HYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSDSTYGAfKTRKGMFRTVGQLYKE 649
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG-RPRRGMFRTVGQLYKE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 650 QLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKG 729
Cdd:cd14930 559 SLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG 638
|
650 660 670
....*....|....*....|....*....|..
gi 768942001 730 FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14930 639 FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
81-761 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1085.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 81 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMM 160
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 161 QDREDQSILCTGESGAGKTENTKKVIQYLAYIASSfKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 240
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGS-GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 241 FDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELFAE 319
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 320 TMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYV 399
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 400 QKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 479
Cdd:pfam00063 320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 480 HTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkK 559
Cdd:pfam00063 400 HHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP-R 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 560 LKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGmsdSTYGAFKTRKGM 639
Cdd:pfam00063 476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANES---GKSTPKRTKKKR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 640 FRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 719
Cdd:pfam00063 553 FITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 768942001 720 ILTPNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:pfam00063 633 ILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
74-773 |
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: 1007.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 74 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITD 153
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 154 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYIASSFKSKkdqGELEKQLLQANPILEAFGNAKTVKNDNSSRF 233
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 234 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQ 312
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVDGID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 313 DKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDT-AAQKVCHLLSVNVTDFTRAILSPR 391
Cdd:smart00242 238 DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 392 IKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 471
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 472 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTH 551
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 552 PKFQKPKKlKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDmdhivgldkvagmsdstYG 631
Cdd:smart00242 474 PHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS-----------------GV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 632 AFKTRKGMFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVF 711
Cdd:smart00242 536 SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPF 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 712 QEFRQRYEILTPNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFRAGVLAHLEEERD 773
Cdd:smart00242 616 DEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
27-1145 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 884.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 27 KKLVWIPSEKLGFEPGSVKEELGDEcmveltdSGRKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 104
Cdd:COG5022 19 KGWIWAEIIKEAFNKGKVTEEGKKE-------DGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 105 SGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 184
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 185 VIQYLAYIASSfkSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIR 264
Cdd:COG5022 172 IMQYLASVTSS--STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 265 QAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMT-IPGLQDKELFAETMEAFHIMSIPEEERIGFLKVVSA 343
Cdd:COG5022 250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 344 VLQLGNMTFKKERhSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERM 423
Cdd:COG5022 330 ILHIGNIEFKEDR-NGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 424 FRWLVFRINKALDKTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFg 503
Cdd:COG5022 409 FDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 504 LDLQPCIELIDKpAGPPGILALLDEECWFPKATDKSFVEKVVQ--EQGTHPKFQKPKklKDDVDFCIIHYAGKVDYKADE 581
Cdd:COG5022 487 FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSR--FRDNKFVVKHYAGDVEYDVEG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 582 WLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVgldkvagmsdstygafktRKGMFRTVGQLYKEQLGNLMTTLRNT 661
Cdd:COG5022 564 FLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE------------------SKGRFPTLGSRFKESLNSLMSTLNST 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 662 NPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNA----IPKGFMDGKQAC 737
Cdd:COG5022 626 QPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAV 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 738 VLMIKALELDPNLYRIGQSKVFFRAGVLAHLEEERDMKITDVIITFQAWCRGYVARKAFTKRQQQLTAMKVIQRNCAAYL 817
Cdd:COG5022 706 KSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRR 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 818 KLRNWQWWRLFTKVKPLLQVTRQEEEMLAKeDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAE 897
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSY-LACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLL 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 898 EMRARLVNRKQELEEIlHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKvttDSKMKALEGNI 977
Cdd:COG5022 865 KKETIYLQSAQRVELA-ERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEL---IARLKKLLNNI 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 978 MVLDDQNNKLNKEKKLLEDRiaEFSSNLSEE-EEKSRSLQKLKNkheaiitdLEDRLRkeeKQRQELEKNRRKLEGDSTD 1056
Cdd:COG5022 941 DLEEGPSIEYVKLPELNKLH--EVESKLKETsEEYEDLLKKSTI--------LVREGN---KANSELKNFKKELAELSKQ 1007
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1057 LhdqiADLQAQIADLRaQLANKEEELQNAlIRIEEEAAANMASQKKIKELEAQILELDEDLERE---KFYRSKNGQRCKE 1133
Cdd:COG5022 1008 Y----GALQESTKQLK-ELPVEVAELQSA-SKIISSESTELSILKPLQKLKGLLLLENNQLQARykaLKLRRENSLLDDK 1081
|
1130
....*....|..
gi 768942001 1134 LEKELEAIKNKL 1145
Cdd:COG5022 1082 QLYQLESTENLL 1093
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
93-761 |
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: 863.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASS--FKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSgsSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFL-----SNGNMTIPGLQDKELFAETMEAF 324
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 325 HIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHS--DQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKA 402
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 403 QTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 481
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 482 MFILEQEEYQREGIEWSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLK 561
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 562 DDVdFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDkftaelwrdmdhivgldkvagmsdstygafktrkgmfr 641
Cdd:cd00124 478 KLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 642 tvgqlYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 721
Cdd:cd00124 519 -----FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 768942001 722 TPNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd00124 594 APGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
93-761 |
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: 778.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIAS---------SFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 243
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 244 NGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNMTIPGLQDKELFAETME 322
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 323 AFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKA 402
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 403 QTQEQAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 482
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 483 FILEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP---K 558
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpdK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 559 KLKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWrdmDHIVGLDKVagmSDSTYGAFKTRK- 637
Cdd:cd14927 477 KRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDST---EDPKSGVKEKRKk 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 638 -GMFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 716
Cdd:cd14927 551 aASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 768942001 717 RYEILTPNAIPK-GFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14927 631 RYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
94-761 |
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: 761.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASS--FKSKKD---QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 248
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 249 GANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIM 327
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 SIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQE 406
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 407 QAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 486
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 487 QEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPK--KLKDD 563
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKvvKGRAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 564 VDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhivGLDkvagmSDSTYGAFKTRKG-MFRT 642
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA---TAD-----ADSGKKKVAKKKGsSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 643 VGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 722
Cdd:cd14913 549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 768942001 723 PNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14913 629 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
93-761 |
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: 760.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQ---GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRsELCL--EDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIM 327
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVK-EMCLlsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 SIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQ 407
Cdd:cd14909 240 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 408 AEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd14909 320 VTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKKLKDDVD- 565
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKPGQQa 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 566 --FCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMdhivgldkvAGMSDSTYGAFKTRK---GMF 640
Cdd:cd14909 476 ahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH---------AGQSGGGEQAKGGRGkkgGGF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 641 RTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 720
Cdd:cd14909 547 ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 768942001 721 LTPNAIpKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14909 627 LNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
93-761 |
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: 742.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKD-QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSIP 330
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 331 EEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEF 410
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 411 AVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 490
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 491 QREGIEWSFIDFGLDLQPCIELIDKPAGppgILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKKLKD---DVDF 566
Cdd:cd14934 400 KREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGkgpEAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 567 CIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKvagmsdstygafKTRKGMFRTVGQL 646
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK------------QKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 647 YKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAI 726
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*
gi 768942001 727 PKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14934 625 PQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
93-761 |
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: 719.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSIPEE 332
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 333 ERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAV 412
Cdd:cd14929 241 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 413 EALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 492
Cdd:cd14929 321 GALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 493 EGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPK--KLKDDVDFCII 569
Cdd:cd14929 400 EGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKpdKKKFEAHFELV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 570 HYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDmdhivglDKVAGmSDSTYGAFKTRKGM-FRTVGQLYK 648
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKKRKKGAsFQTVASLHK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 649 EQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPK 728
Cdd:cd14929 549 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPK 628
|
650 660 670
....*....|....*....|....*....|....
gi 768942001 729 G-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14929 629 SkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
94-761 |
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: 703.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSG-LIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSfksKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS---SSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGsPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFA 411
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 412 VEALAKASYERMFRWLVFRINKALDKTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 490
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 491 QREGIEWSFIDFgLDLQPCIELIDkpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK--FQKPKKLKDdvDFCI 568
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNT--AFIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 569 IHYAGKVDYKADEWLMKNMDPLNESVATLLNQStdkftaelwrdmdhivgldkvagmsdstygafKTRKgmfRTVGQLYK 648
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS--------------------------------KNRK---KTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 649 EQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPK 728
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWL 597
|
650 660 670
....*....|....*....|....*....|...
gi 768942001 729 GfMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd01380 598 R-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
94-761 |
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: 698.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIAS-SFKSKKDQ----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 248
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 249 GANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNMTIPGLQDKELFAETMEAFHIM 327
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 SIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQE 406
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 407 QAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 486
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 487 QEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKKLKD--D 563
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGkpE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 564 VDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMdhiVGLDkvagmSDSTYGAFKTRKG-MFRT 642
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGAD-----APIEKGKGKAKKGsSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 643 VGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 722
Cdd:cd14917 549 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 768942001 723 PNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14917 629 PAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
95-761 |
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: 692.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 95 VLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 174
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 175 GAGKTENTKKVIQYLAYIASSFKSKKD-----QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMS 328
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 329 IPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQ 407
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 408 AEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPK--KLKDDV 564
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 565 DFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMdhivgldkVAGMSDSTYGAFKTRKG-MFRTV 643
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGsSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 644 GQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 723
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 768942001 724 NAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
94-761 |
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: 690.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASSFKSKKD-------QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 246
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 247 IVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFH 325
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 326 IMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQT 404
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 405 QEQAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 484
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 485 LEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKKLKDD 563
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 564 VD--FCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRdmdhivGLDKVAGMSDSTYGAFKTRKGMFR 641
Cdd:cd14910 477 VEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFS------GAAAAEAEEGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 642 TVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 721
Cdd:cd14910 551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 768942001 722 TPNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14910 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
94-761 |
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: 687.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASSFKSKKD-------QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 246
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 247 IVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNMTIPGLQDKELFAETMEAFH 325
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 326 IMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQT 404
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 405 QEQAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 484
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 485 LEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPK--KLK 561
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKvvKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 562 DDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGldkvAGMSDSTYGAFKTRKGMFR 641
Cdd:cd14912 477 AEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG----ASAGGGAKKGGKKKGSSFQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 642 TVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 721
Cdd:cd14912 553 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 768942001 722 TPNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14912 633 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-761 |
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: 683.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASSFKSKKD------QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 247
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 248 VGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNMTIPGLQDKELFAETMEAFHI 326
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 327 MSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQ 405
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 406 EQAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 485
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 486 EQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPK--KLKD 562
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKpaKGKA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 563 DVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMdhivgLDKVAGMSDSTYGAFKTRKGMFRT 642
Cdd:cd14923 477 EAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY-----AGAEAGDSGGSKKGGKKKGSSFQT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 643 VGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 722
Cdd:cd14923 552 VSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 768942001 723 PNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14923 632 ASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
94-761 |
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: 682.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIAS-SFKSKKD-----QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 247
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 248 VGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNMTIPGLQDKELFAETMEAFHI 326
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 327 MSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDTA-AQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQ 405
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 406 EQAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 485
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 486 EQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPK--KLKD 562
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRnvKGKQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 563 DVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMdhiVGLDkvAGMSDSTYGAfKTRKGMFRT 642
Cdd:cd14916 477 EAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASAD--TGDSGKGKGG-KKKGSSFQT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 643 VGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 722
Cdd:cd14916 551 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 768942001 723 PNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14916 631 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-761 |
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: 676.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASSFKSKKD-------QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 246
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 247 IVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLrSELCLEDYSKYRF--LSNGNMTIPGLQDKELFAETMEAF 324
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 325 HIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmPDDT-AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQ 403
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 404 TQEQAEFAVEALAKASYERMFRWLVFRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 483
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 484 ILEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPK--KL 560
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKpaKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 561 KDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRdmdhivGLDKVAGMSDSTYGAFKTRKGMF 640
Cdd:cd14915 476 KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS------GGQTAEAEGGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 641 RTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 720
Cdd:cd14915 550 QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 768942001 721 LTPNAIPKG-FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14915 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
94-761 |
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: 660.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASSfkskkdQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 253
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNN------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 254 TYLLEKSRAIRQAKEERSFHIFYYLLTGAG--DKLRSELCLEDYSKYRFLS-NGNMTIPGLQDKELFAETMEAFHIMSIP 330
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 331 EEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQK-VCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 489
Cdd:cd14883 316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 490 YQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFCII 569
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 570 HYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhIVGLDKVAGMSDSTYGAFKTRKGMfRTVGQLYKE 649
Cdd:cd14883 472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKGK-PTVGDTFKH 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 650 QLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKG 729
Cdd:cd14883 550 QLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSAD 629
|
650 660 670
....*....|....*....|....*....|..
gi 768942001 730 FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14883 630 HKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
94-761 |
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: 657.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASsfkskkDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 253
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 254 TYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELFAETMEAFHIMSIPEE 332
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 333 ERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAV 412
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 413 EALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 492
Cdd:cd01383 314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 493 EGIEWSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKpkklKDDVDFCIIHYA 572
Cdd:cd01383 394 DGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ERGGAFTIRHYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 573 GKVDYKADEWLMKNMDPLNESVATLLNQSTDKF---TAELWRDMDHIVGLDKVAGMSDStygafktrkgMFRTVGQLYKE 649
Cdd:cd01383 467 GEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLpqlFASKMLDASRKALPLTKASGSDS----------QKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 650 QLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIpKG 729
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SA 615
|
650 660 670
....*....|....*....|....*....|..
gi 768942001 730 FMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd01383 616 SQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
94-761 |
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: 629.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIassfkSKKDQGELEK---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 250
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 251 NIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSI 329
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 330 PEEERIGFLKVVSAVLQLGNMTFkKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVG---RDYVQKAQTQE 406
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 407 QAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 486
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 487 QEEYQREGIEWSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFP-KATDKSFVEKVVQEQGTHPKFQKPKKLKD--D 563
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 564 VDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDmdhivgldkvagmsdstyGAFKTRKGMFRTV 643
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKKRPPTA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 644 GQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 723
Cdd:cd01378 535 GTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSP 614
|
650 660 670
....*....|....*....|....*....|....*...
gi 768942001 724 NAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd01378 615 KTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
93-761 |
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: 628.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASsfKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELFAETMEAFHIMSIP 330
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGIS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 331 EEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQ--KVC-HLLSVNVTDFTRAILSpRIKVGRD-YVQKAQTQE 406
Cdd:cd01384 239 EEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFhlKAAaELLMCDEKALEDALCK-RVIVTPDgIITKPLDPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 407 QAEFAVEALAKASYERMFRWLVFRINKAL--DKTKRqgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 484
Cdd:cd01384 318 AATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 485 LEQEEYQREGIEWSFIDFgLDLQPCIELIDKpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKklKDDV 564
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 565 DFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhivgldkvagmSDSTYGAFKtrkgmFRTVG 644
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLP-----------REGTSSSSK-----FSSIG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 645 QLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 724
Cdd:cd01384 534 SRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPE 613
|
650 660 670
....*....|....*....|....*....|....*..
gi 768942001 725 AiPKGFMDGKQACVLMIKALELDPnlYRIGQSKVFFR 761
Cdd:cd01384 614 V-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
93-761 |
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: 610.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIaSSFKSKkdqgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAI-SGQHSW-----IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNM-TIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKKERHS--DQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd01381 315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFgLDLQPCIELIdkPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKlKDDVDFC 567
Cdd:cd01381 395 EEYDKEGINWQHIEF-VDNQDVLDLI--ALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS-DLNTSFG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 568 IIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWrdmdhivglDKVAGMSDSTYGAFKTRKGMFRTvgqly 647
Cdd:cd01381 471 INHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF---------NEDISMGSETRKKSPTLSSQFRK----- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 648 keQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIP 727
Cdd:cd01381 537 --SLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPP 614
|
650 660 670
....*....|....*....|....*....|....
gi 768942001 728 KGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd01381 615 AHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
93-761 |
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: 583.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASSfkskkDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS-----GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELcledyskyrflsngnMTIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL---------------LKDPLLDDVGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFkKERHSD--------QASMPDDTAAQKvchLLSVNVTDF-----TRAILSPRIKVGRDY 398
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNIEF-EENGSDsgggcnvkPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKGTV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 399 VQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 478
Cdd:cd01382 297 IKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 479 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIDKPAGppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPK 558
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 559 K--------LKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDmdhivgLDKVAGMSDSTY 630
Cdd:cd01382 452 KsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES------STNNNKDSKQKA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 631 GafktrKGMFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVV 710
Cdd:cd01382 526 G-----KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 768942001 711 FQEFRQRYEILTPNAIPKgfMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
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 ... |
93-761 |
2.70e-179 |
|
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: 558.24 E-value: 2.70e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSfkskkdQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAgdKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDT---AAQKVCHLLSVNVTDFTRAILSPRIKV-GRDYVQKAQTQEQ 407
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVAnrdVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 408 AEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFC 567
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 568 IIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhivgldkvagmsdstyGAFKTRKGmfrTVGQLY 647
Cdd:cd14872 470 VKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----------------GDQKTSKV---TLGGQF 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 648 KEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPNAIP 727
Cdd:cd14872 531 RKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIA 609
|
650 660 670
....*....|....*....|....*....|....*
gi 768942001 728 KGFM-DGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14872 610 KRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
93-761 |
8.82e-179 |
|
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: 557.44 E-value: 8.82e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIAssfksKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 252
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNG-NMTIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd01387 155 SQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKKE--RHS-DQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQA 408
Cdd:cd01387 235 EEQDSIFRILASVLHLGNVYFHKRqlRHGqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 409 EFAVEALAKASYERMFRWLVFRINKALDKTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 488
Cdd:cd01387 315 LDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 489 EYQREGIEWSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKklKDDVDFCI 568
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR--MPLPEFTI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 569 IHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDM--DHIVGLDKVAGmsdstyGAFKTRKGMFRTVGQL 646
Cdd:cd01387 469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHraQTDKAPPRLGK------GRFVTMKPRTPTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 647 YKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAI 726
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 768942001 727 PKGfMDGKQACVLMIKALELDP-NLYRIGQSKVFFR 761
Cdd:cd01387 623 PRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
93-761 |
8.27e-175 |
|
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: 547.07 E-value: 8.27e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 167
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 168 ILCTGESGAGKTENTKKVIQYLAYIASSFKSKKDQ-------------GELEKQLLQANPILEAFGNAKTVKNDNSSRFG 234
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 235 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDK 314
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 315 ELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASmpDDTAAQ---KVCHLLSVNVTDFTRAILSPR 391
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 392 IKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 471
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 472 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELID-KPAGPPGILALLDeECWFPKAT--DKSFVEKVVQEQ 548
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 549 GT-------------HPKFQKPkKLKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTdkftaelwrdmdh 615
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHP-KFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 616 ivgldkvagmsdstygafKTRKGMfrTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVL 695
Cdd:cd14890 542 ------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768942001 696 EGIRICRQGFPNRVVFQEFRQRYEILTPNAipkgfMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
93-761 |
6.15e-171 |
|
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: 536.28 E-value: 6.15e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIAssfkskkdqGELE----KQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 247
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 248 VGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFlSNGNMTIPGLQDKELFAETMEAFHIM 327
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 SIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASM--PDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQ 405
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 406 EQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 485
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 486 EQEEYQREGIEWSFIDFgLDLQPCIELIDkpaGPPGILALLDEECWFPKATDKSFVEKVVqeqGTHPKFQK----PKKLK 561
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 562 ddVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRdmdhiVGLDKVAGMSDSTYGAFKTRKG--- 638
Cdd:cd14903 463 --TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----EKVESPAAASTSLARGARRRRGgal 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 639 MFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 718
Cdd:cd14903 536 TTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 768942001 719 EILTPNAiPKGFMDGKQACVLMIKALELD-PNLYRIGQSKVFFR 761
Cdd:cd14903 616 WLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
93-761 |
4.63e-168 |
|
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: 529.64 E-value: 4.63e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLayiasSFKSKKDQGE-LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd01385 81 ESGSGKTESTNFLLHHL-----TALSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLS-NGNMTIPGLQDKELFAETMEAFHIMSIP 330
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVGFL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 331 EEERIGFLKVVSAVLQLGNMTFKKER-HSDQASMPDDTAAQK-VCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQA 408
Cdd:cd01385 236 PETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 409 EFAVEALAKASYERMFRWLVFRINKAL----DKTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 484
Cdd:cd01385 316 IATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 485 LEQEEYQREGIEWSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDdv 564
Cdd:cd01385 395 LEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEP-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 565 DFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELwrdmdhiVGLDKVA--------------------G 624
Cdd:cd01385 470 AFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrwavlrafframaafreaG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 625 MSDSTYGAFKTRKGMFRTVGQL---------------YKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQL 689
Cdd:cd01385 543 RRRAQRTAGHSLTLHDRTTKSLlhlhkkkkppsvsaqFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQL 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 690 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnaIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd01385 623 RYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
93-759 |
4.50e-166 |
|
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: 523.20 E-value: 4.50e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 164
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 165 --DQSILCTGESGAGKTENTKKVIQYLAYIASsfKSKKDQGELEK-----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 237
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 238 RINFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTI--PGLQDKE 315
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrrDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 316 LFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTF-KKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKV 394
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 395 GRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEK 473
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 474 LQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIELIDkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQG 549
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 550 THPKFQKPKKLKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAElwrdmdhivgldkvagmsdst 629
Cdd:cd14901 472 KHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 630 ygafktrkgmfrTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRV 709
Cdd:cd14901 531 ------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRF 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 768942001 710 VFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKA------LELDPNLYrIGQSKVF 759
Cdd:cd14901 599 PHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
94-761 |
2.85e-165 |
|
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: 519.91 E-value: 2.85e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIassfkSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 253
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 254 TYLLEKSRAIRQAKEERSFHIFYYLLTG-AGDKLRSELCLEDYSKYRFLSNGNMTIPGLQD----KELFAETMEAFHIMS 328
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNnsgnREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 329 IPEEERIGFLKVVSAVLQLGNMTFK---KERHSDQASM-PDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQT 404
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 405 QEQAEFAVEALAKASYERMFRWLVFRINKAL--DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 482
Cdd:cd01379 317 VEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 483 FILEQEEYQREGIEWSFIDFGlDLQPCIE-LIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPkFQKPKklK 561
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK--S 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 562 DDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAElwrdmdhivgldkvagmsdstygafktrkgmfr 641
Cdd:cd01379 470 NALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 642 TVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 721
Cdd:cd01379 517 TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFL 596
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 768942001 722 TPNAIPKGFMDgKQACVLMIKALELDPnlYRIGQSKVFFR 761
Cdd:cd01379 597 AFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
93-761 |
8.80e-163 |
|
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: 513.47 E-value: 8.80e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASSfkskkDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFH----IM 327
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHdltnIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 S---IPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQT 404
Cdd:cd14897 236 KligFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 405 QEQAEFAVEALAKASYERMFRWLVFRINKAL----DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 480
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 481 TMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKkl 560
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASP-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 561 KDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWrdmdhivgldkvagmsdstygafktrkgmf 640
Cdd:cd14897 471 GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 641 rtvGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 720
Cdd:cd14897 521 ---TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 768942001 721 LTPNAiPKGFMDGKQACVLMIKALELDPnlYRIGQSKVFFR 761
Cdd:cd14897 598 ICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
93-761 |
3.89e-160 |
|
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: 506.64 E-value: 3.89e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASS---FKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 248
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQsleLSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 249 GANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLS-NGNMTIPGLQDKELFAETMEAFHIM 327
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 328 SIPEEERIGFLKVVSAVLQLGNMTFKKerhSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQ 407
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 408 AEFAVEALAKASYERMFRWLVFRINKALdkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFgLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKklKDDVDFC 567
Cdd:cd14873 396 LEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPR--VAVNNFG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 568 IIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWrdmDHivglDKVAGMSDSTYGAFKTRKgmfRTVGQLY 647
Cdd:cd14873 470 VKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---EH----VSSRNNQDTLKCGSKHRR---PTVSSQF 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 648 KEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIP 727
Cdd:cd14873 540 KDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLAL 619
|
650 660 670
....*....|....*....|....*....|....
gi 768942001 728 KGFMDGKqaCVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14873 620 PEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
93-761 |
1.69e-159 |
|
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: 505.06 E-value: 1.69e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 165
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 166 QSILCTGESGAGKTENTKKVIQYLAYI----ASSFKSKKDQG---ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 238
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 239 INFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELF 317
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 318 AETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTF----KKERHSDQASMPDDTAaqKVCHLLSVNVTDFTRAILSPRIK 393
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenaDDEDVFAQSADGVNVA--KAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 394 VGRDYV-QKAQTQEQAEFAVEALAKASYERMFRWLVFRINKAldkTKRQG------------ASFIGILDIAGFEIFELN 460
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 461 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFP-KATDKS 539
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 540 FVEKVVQEQ-GTHPKFQKPKKLKDdvDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQStdkftaelwrdmdhivg 618
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 619 ldkvagmsdstygafktRKgmFRTvgqlykeQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGI 698
Cdd:cd14892 534 -----------------SK--FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 699 RICRQGFPNRVVFQEFRQRYEILTPN-AIPKGFMDGKQACVLMIKALE-----LDPNLYRIGQSKVFFR 761
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
93-723 |
1.01e-156 |
|
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: 498.06 E-value: 1.01e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASSFKSKKDQgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD--------- 242
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 243 VNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNG------NMT--------- 307
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakpisiDMSsfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 308 ---------IPGLQDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQ---KVCHL 375
Cdd:cd14888 238 yltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 376 LSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFE 455
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 456 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDkpAGPPGILALLDEECWFPKA 535
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVPGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 536 TDKSFVEKVVQEQGTHPKFQKPKklKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRdmdh 615
Cdd:cd14888 475 KDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS---- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 616 ivgldkvAGMSDSTYGAFKTRKgmFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVL 695
Cdd:cd14888 549 -------AYLRRGTDGNTKKKK--FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660
....*....|....*....|....*...
gi 768942001 696 EGIRICRQGFPNRVVFQEFRQRYEILTP 723
Cdd:cd14888 620 QAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
93-724 |
2.60e-147 |
|
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: 472.21 E-value: 2.60e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 163
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 164 EDQSILCTGESGAGKTENTKKVIQYLAYIASSFKSK--------------KDQGELEKQLLQANPILEAFGNAKTVKNDN 229
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 230 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLS---NG 304
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 305 NMTIPGLQDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQA--SMPDDTAAQKVCHLLSVNVTD 382
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 383 FTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKAL-------DKTKRQGASFIGILDIAGFE 455
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 456 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIELIDKPagPPGILALLDEECWFP 533
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 534 KATDKSFVEKVVQEQGTHPKFQKPKKLKDDVdFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDM 613
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 614 DhivgldkvaGMSDSTYGAFKTRKGMFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNG 693
Cdd:cd14907 557 D---------GSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLG 627
|
650 660 670
....*....|....*....|....*....|.
gi 768942001 694 VLEGIRICRQGFPNRVVFQEFRQRYEILTPN 724
Cdd:cd14907 628 VLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
95-761 |
1.36e-146 |
|
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: 469.77 E-value: 1.36e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 95 VLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 170
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 171 TGESGAGKTENTKKVIQYLAYIAssfkskKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGA 250
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 251 NIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN--GNMTIPGlQDKELFAETMEAFHIMS 328
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREVQ-YWKKKYDEVCNAMDMVG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 329 IPEEERIGFLKVVSAVLQLGNMTFKkerhsdqasmPDDTAAQKV-----------CHLLSVNVTDFTRAILSPRIKVGRD 397
Cdd:cd14889 235 FTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVendsngwlkaaAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 398 YVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 475
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 476 QLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIdkPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQ 555
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 556 KPKklKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDK-----FTAELWRDMDHIVGLDKVAGMSDSty 630
Cdd:cd14889 462 KSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPllsvlFTATRSRTGTLMPRAKLPQAGSDN-- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 631 gAFKTRKgmfRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVV 710
Cdd:cd14889 538 -FNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPS 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 768942001 711 FQEFRQRYEIL--TPNaIPKgfmdGKQACVLMIKALELDPnlYRIGQSKVFFR 761
Cdd:cd14889 614 FAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
94-721 |
3.03e-141 |
|
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: 453.61 E-value: 3.03e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 161
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 162 ----DREDQSILCTGESGAGKTENTKKVIQYLAYI-----ASSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSR 232
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 233 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSelcledyskyrflsngnmtipglq 312
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 313 dKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSD-QASMPDDTAAQKV------CHLLSVNVTDFTR 385
Cdd:cd14900 218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 386 AILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKAL---DKTKRQGAS-FIGILDIAGFEIFELNS 461
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 462 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDkpAGPPGILALLDEECWFPKATDKSFV 541
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 542 EKVVQEQGTHPKFQKPKKLKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATllnqstdkftaelwrdmdhivgldk 621
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVD------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 622 vagmsdstygafktrkgMFRTVGQlYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRIC 701
Cdd:cd14900 509 -----------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
|
650 660
....*....|....*....|
gi 768942001 702 RQGFPNRVVFQEFRQRYEIL 721
Cdd:cd14900 571 RAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
93-744 |
1.69e-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: 452.04 E-value: 1.69e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 162
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 163 REDQSILCTGESGAGKTENTKKVIQYLAYI----ASSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 238
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 239 INFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMT---IPGLQDK- 314
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarKRAVADKy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 315 -ELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAA---QKVCHLLSVNVTDFTRAILSP 390
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 391 RIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALD--------KTKRQGASFIGILDIAGFEIFELNSF 462
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 463 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVE 542
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK--SNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 543 KVVQEQGthPKFQkpkklkddvdFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDkftaelwrDMDHIVGLDKV 622
Cdd:cd14902 478 KFYRYHG--GLGQ----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 623 AGMSDSTYGAFKTRK-GMFRT--VGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 699
Cdd:cd14902 538 RDSPGADNGAAGRRRySMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 768942001 700 ICRQGFPNRVVFQEFRQRYEIL-----TPNAIPK-GFMDGKQA--CVLMIKAL 744
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
93-761 |
2.21e-138 |
|
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: 446.41 E-value: 2.21e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERyySGLI----YTYSGLFCVVVNPYKHLPiysEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 165
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 166 QSILCTGESGAGKTENTKKVIQYL------------AYIASSFKSKKDQG-ELEKQLLQANPILEAFGNAKTVKNDNSSR 232
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttravggkkasgQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 233 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPG 310
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 311 LQDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHS----DQASMPDDTAAQKVCHLLSVNVTDFTRA 386
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSegeaEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 387 ILSPRIkVGRDYVQKAQ-TQEQAEFAVEALAKASYERMFRWLVFRINKALDKtKRQGASFIGILDIAGFEIFEL-NSFEQ 464
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 465 LCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIELIdkPAGPPGILALLDEECWFPKATDKS 539
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLI--ASKPNGILPLLDNEARNPNPSDAK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 540 FVEKVVQEQGTHPKF--QKPKKLKDdvDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQStdkftaelwrdmdhiv 617
Cdd:cd14891 466 LNETLHKTHKRHPCFprPHPKDMRE--MFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS---------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 618 gldkvagmsdstygafktrkgmfrtvgQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEG 697
Cdd:cd14891 528 ---------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQT 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 698 IRICRQGFPNRVVFQEFRqryEILTPNAIPKGF-MDGKQACVL---MIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14891 581 CEVLKVGLPTRVTYAELV---DVYKPVLPPSVTrLFAENDRTLtqaILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
93-761 |
1.06e-136 |
|
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: 441.91 E-value: 1.06e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLayiaSSFKSKKDQGELeKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 252
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNM-TIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKK-ERHSDQ-ASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSsERESQEvAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 488
Cdd:cd14896 315 DARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 489 EYQREGIEWSFIDfGLDLQPCIELIdkPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkKLKDDVdFCI 568
Cdd:cd14896 395 ECQRELLPWVPIP-QPPRESCLDLL--VDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKP-QLPLPV-FTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 569 IHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGmsdstygafktrkgmfrTVGQLYK 648
Cdd:cd14896 470 RHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP-----------------TLASRFQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 649 EQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTpNAIPK 728
Cdd:cd14896 533 QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQE 611
|
650 660 670
....*....|....*....|....*....|...
gi 768942001 729 GFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14896 612 ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
93-761 |
1.84e-135 |
|
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: 438.61 E-value: 1.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAYIASSFKSKKdqgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKT-----IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--SNGNMTIPGLQDKELFAETMEAFHIMSI 329
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 330 PEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQkVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAE 409
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 410 FAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 489
Cdd:cd14904 315 ENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 490 YQREGIEWSFIDFGlDLQPCIELIDkpaGPPGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKPKKLKddVDF 566
Cdd:cd14904 395 YIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKR--TQF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 567 CIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWrdmdhivglDKVAGMSDSTYGAFKTRKGMFRTVGQL 646
Cdd:cd14904 469 IINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---------GSSEAPSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 647 YKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAI 726
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 768942001 727 PKGfmDGKQACVLMIKAL-ELDPNLYRIGQSKVFFR 761
Cdd:cd14904 620 HSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
91-804 |
1.58e-130 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 430.61 E-value: 1.58e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 91 NEASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 169
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 170 CTGESGAGKTENTKKVIQYLAYIASSFKSKKDQgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 249
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQ----NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 250 ANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSI 329
Cdd:PTZ00014 264 GSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 330 PEEERIGFLKVVSAVLQLGNMTF---KKERHSDQASMPDDTAA--QKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQT 404
Cdd:PTZ00014 344 SESQIEDIFSILSGVLLLGNVEIegkEEGGLTDAAAISDESLEvfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 405 QEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 484
Cdd:PTZ00014 424 KDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 485 LEQEEYQREGIEWSFIDFgLDLQPCIELI-DKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFqKPKKLKDD 563
Cdd:PTZ00014 503 RESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKY-KPAKVDSN 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 564 VDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhivgldkvagMSDStygafKTRKGMFrtV 643
Cdd:PTZ00014 578 KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVE----------VEKG-----KLAKGQL--I 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 644 GQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 723
Cdd:PTZ00014 641 GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDL 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 724 NAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR---AGVLAHLEEERDMKITDVIITFQAWCRGYVARKAFTKRQ 800
Cdd:PTZ00014 721 AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNI 800
|
....
gi 768942001 801 QQLT 804
Cdd:PTZ00014 801 KSLV 804
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
93-761 |
1.71e-130 |
|
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: 425.86 E-value: 1.71e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 162
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 163 REDQSILCTGESGAGKTENTKKVIQYLAYIASSFK-SKKDQGELEK-----QLLQANPILEAFGNAKTVKNDNSSRFGKF 236
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 237 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDY--------SKYRFLSNGNM-T 307
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGitgglqlpNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 308 IPGLQDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFK---KERHSDQASMPDDTAAQKVCHLLSVNVTDFT 384
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEskeEDGAAEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 385 RAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGA-SFIGILDIAGFEIFELNSFE 463
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 464 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPagPPGILALLDEECWFP-KATDKSFVE 542
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYAS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 543 KVV--------QEQGTHPKFQKPKKLKDDVDFCIIHYAGKVDYKADEWLM-KNMDPLNesvatllnqstdkftaelwrdm 613
Cdd:cd14908 478 RLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP---------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 614 dhivgldkvagmsdstygafKTRKGMFRTvGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNG 693
Cdd:cd14908 536 --------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 694 VLEGIRICRQGFPNRVVFQEFRQRYEILTPnAIPK----GFMDGKQACVLMIKALELDPNLYR----------------- 752
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipedtmq 673
|
....*....
gi 768942001 753 IGQSKVFFR 761
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
94-761 |
6.66e-129 |
|
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: 422.05 E-value: 6.66e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPiysedivNMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 161
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 162 --DREDQSILCTGESGAGKTENTKKVIQYLAYIASSFK----SKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 235
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTatssSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 236 FIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYS--KYRFLSNGNMTI 308
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 309 --PGLQDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSD---------------QASMPDDTAAQK 371
Cdd:cd14895 235 rnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 372 ---VCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTK--------- 439
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 440 -RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIELIDkpAG 518
Cdd:cd14895 395 nKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE--QR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 519 PPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLL 598
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 599 NQSTDKFTAELWRDMdhivgldKVAGMSDSTYGAFKT--RKGMFRTV--GQLYKEQLGNLMTTLRNTNPNFVRCIIPNHE 674
Cdd:cd14895 552 GKTSDAHLRELFEFF-------KASESAELSLGQPKLrrRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 675 KKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKALELdpnlyriG 754
Cdd:cd14895 625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL-------G 697
|
....*..
gi 768942001 755 QSKVFFR 761
Cdd:cd14895 698 KTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
93-759 |
1.04e-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: 408.22 E-value: 1.04e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAyiasSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMGLTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKKErhsDQASMPDdtAA----------QKVCHLLSVNVTDFTRAILSPRIKVGRDYVQK 401
Cdd:cd14876 237 EQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQEIEG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 402 AQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 481
Cdd:cd14876 312 RWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 482 MFILEQEEYQREGIEWSFIDFGLDLqpciELIDKPAGPPG-ILALLDEECWFPKATDKSFVEKVVQEQGTHPKFqKPKKL 560
Cdd:cd14876 391 VFERESKLYKDEGIPTAELEYTSNA----EVIDVLCGKGKsVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 561 KDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMdhIVGLDKVAgmsdstygafktrKGMF 640
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV--VVEKGKIA-------------KGSL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 641 rtVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 720
Cdd:cd14876 531 --IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKF 608
|
650 660 670
....*....|....*....|....*....|....*....
gi 768942001 721 LTPNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVF 759
Cdd:cd14876 609 LDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
93-761 |
2.03e-121 |
|
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: 400.15 E-value: 2.03e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKSKkdqgeLEKQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 251
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKyrflsNGNMTIPGLQDKEL-------FAETMEAF 324
Cdd:cd01386 156 IQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE-----SNSFGIVPLQKPEDkqkaaaaFSKLQAAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 325 HIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAI------------LSPRI 392
Cdd:cd01386 231 KTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 393 KVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALdKTKRQGASFIGILDIAGFEIFELN------SFEQLC 466
Cdd:cd01386 311 QESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFEDLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 467 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAG------------PPGILALLDEECWFPK 534
Cdd:cd01386 390 HNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEALYPG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 535 ATDKSFVEKVVQEQGT--HPKFQKP-KKLKDDVDFCIIHYAGK--VDYKADEWLMK-NMDPLNESVATLLNQSTDKFtae 608
Cdd:cd01386 470 SSDDTFLERLFSHYGDkeGGKGHSLlRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET--- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 609 lwrdmdhivgldkvagmsdstygAFKTRKGMFRTVgqlyKEQLGNLMTTLRNTNPNFVRCIIPNHE------KKAGKLEP 682
Cdd:cd01386 547 -----------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSSPAAG 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 683 HLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKGF-----MDGKQACVLMIKALELDPNLY 751
Cdd:cd01386 600 DELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSY 679
|
730
....*....|
gi 768942001 752 RIGQSKVFFR 761
Cdd:cd01386 680 RIGLSQVFFR 689
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
93-757 |
1.31e-116 |
|
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: 387.41 E-value: 1.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 170
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 171 TGESGAGKTENTKKVIQYLAYIASSFKSKK-----DQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 244
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 245 GYIVGANIETYLLEKSR-AIRQAKEERSFHIFYYLLTGAGDKLRSELCLE-DYSKYRFL------------------SNG 304
Cdd:cd14906 161 GKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNnDPSKYRYLdarddvissfksqssnknSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 305 NMTIPGLQDKELFAETMEAfhiMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDT---AAQKVCHLLSVNVT 381
Cdd:cd14906 241 NNKTESIESFQLLKQSMES---MSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKvtaSLESVSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 382 DFTRAILSPRIKVGRDYVQKAQTQE--QAEFAVEALAKASYERMFRWLVFRINKALDK----------TKRQGASFIGIL 449
Cdd:cd14906 318 VFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 450 DIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIDKPAGppGILALLDEE 529
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 530 CWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKddVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAEL 609
Cdd:cd14906 475 CIMPKGSEQSLLEKYNKQYHNTNQYYQRTLAK--GTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 610 WRdmdhivglDKVAGMSDSTygafkTRKGMFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQL 689
Cdd:cd14906 553 FQ--------QQITSTTNTT-----KKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 690 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSK 757
Cdd:cd14906 620 RNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
93-759 |
5.44e-115 |
|
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: 380.74 E-value: 5.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 168
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 169 LCTGESGAGKTENTKKVIQYLAYIASS---FKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 245
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASptsWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 246 YIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIpglqDKELFAETMEAFH 325
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 326 IMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKV---CHLLSVNVTDFTRAILSPRIKVGRDYV--Q 400
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 401 KAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 480
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 481 TMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKL 560
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 561 KDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLDKVAGMSdstygafktrKGMF 640
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQS----------RAPV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 641 RTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 720
Cdd:cd14880 544 LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKL 623
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 768942001 721 LTPN--AIPKGFMDGKQAcvlmikalELDPNLYRIGQSKVF 759
Cdd:cd14880 624 LRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
93-761 |
3.13e-114 |
|
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: 378.46 E-value: 3.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 166
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 167 SILCTGESGAGKTENTKKVIQYLAYIASSFKSKkdqgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 246
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 247 IVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-MTIPGLQDKELFAETMEAFH 325
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 326 IMsIPEEERIGFLKVVSAVLQLGNMTFKKERHS---DQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKA 402
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 403 QTQEQAEFAVEALAKASYERMFRWLVFRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 482
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 483 FILEQEEYQREGIEWSFIDFGlDLQPCIELIDKPAgpPGILALLDEECWFPKATDKSFVEKVvqeqgthpkfqkPKKLKD 562
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSSC------------KSKIKN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 563 D---------VDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDHIVGLdkvagmsdstygaf 633
Cdd:cd14886 459 NsfipgkgsqCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 634 ktRKGMFrtVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 713
Cdd:cd14886 525 --MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEE 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 768942001 714 FRQRYEILT--PNAIPKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14886 601 FFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
93-761 |
1.08e-111 |
|
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: 371.45 E-value: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYS-GLIYTYSGLFCVVVNPYKHLPIYSEDIVNMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 169
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 170 CTGESGAGKTENTKKVIQYL---AYIASSFKSKKDQGE-LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 244
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQRSIADkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 245 GYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELC-LEDYSKYRFLSNGNMTI------PGLQDKELF 317
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGgLKTAQDYKCLNGGNTFVrrgvdgKTLDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 318 AETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERhSDQASMPDDTAAQKVCHLLSVNVTDFTRAILsprIKVGRD 397
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQ-NDKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 398 YVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALD-KTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 476
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 477 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDkpAGPPGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQ 555
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 556 KPKKLKDDvDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELwrdmdhivgLDKVAGMSDstygafkt 635
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLAR-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 636 RKgmfRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 715
Cdd:cd14875 536 RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFC 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 768942001 716 QRYEILTPNAIPKGFMDGK--QACVLMIKALE-----LDPNlYRIGQSKVFFR 761
Cdd:cd14875 613 RYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
93-718 |
1.80e-106 |
|
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: 358.25 E-value: 1.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 161
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 162 DREDQSILCTGESGAGKTENTKKVIQYLA------------YIASSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDN 229
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 230 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSE----LCLEDYSKYRFLSNG 304
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEqkqvLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 305 NMTIP---GLQDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERH-------SDQASMPDDTAA----- 369
Cdd:cd14899 241 SLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHkgddtvfADEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 370 QKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKAL-------------- 435
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 436 DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDK 515
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 516 PagPPGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKPKKLKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNE 592
Cdd:cd14899 480 R--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 593 SVATLLNQSTDKFTAELW--RDMDHIVGLDKVAGMSDSTYGAFKTRKGMFrTVGQLYKEQLGNLMTTLRNTNPNFVRCII 670
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 768942001 671 PNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 718
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
93-761 |
1.71e-95 |
|
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: 326.61 E-value: 1.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYS--------GLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 164
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 165 DQSILCTGESGAGKTENTKKVIQYLAYIaSSFKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 244
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV-SDRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 245 GYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAgdklrselcledyskyrFLSNGNMTIPGLQDKELFA--ETME 322
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAA-----------------VAAATQKSSAGEGDPESTDlrRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 323 AFHIMSIPEEERIGFLKVVSAVLQLGNMTF--------KKERHSDQASMPDDTAAQKVCHLLSV-------NVTDFTRAI 387
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFttdqepetSKKRKLTSVSVGCEETAADRSHSSEVkclssglKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 388 LS--------PRIKVGRDYV------------QKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKR------- 440
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 441 ------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG--IEWSFIDFGLDLQPC 509
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFSFPLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 510 IELIDKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEKVVQEQGTHPKFQK--PKKL 560
Cdd:cd14887 463 STLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 561 KDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNqSTDKFTAElwrdmdhiVGLDKVAGMSdstygAFKTRKgmf 640
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLFL-ACSTYTRL--------VGSKKNSGVR-----AISSRR--- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 641 RTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 720
Cdd:cd14887 606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYET 685
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 768942001 721 LTPNAIpKGFMDGKQACVLMIKALELDPNLYRIGQSKVFFR 761
Cdd:cd14887 686 KLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
94-725 |
1.36e-92 |
|
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: 313.37 E-value: 1.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHlpIYSEDIVNMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 173
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIASSFKSkkdqgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGYIVGANIE 253
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 254 TYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSelcleDYSKYRFLSNGNMTIPGLQDK-ELFAETMEAFHIMSIPEE 332
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKN-----DFIDTSSTAGNKESIVQLSEKyKMTCSAMKSLGIANFKSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 333 ErigflKVVSAVLQLGNMTFKKERHSDQASmpdDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAV 412
Cdd:cd14898 225 E-----DCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 413 EALAKASYERMFRWLVFRINKALDKTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 492
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 493 EGIEWSFIDFgLDLQPCIELIDKPAgppGILALLDEECWFPKATDKSFVEKVvqeqgtHPKFQKPKKLKDDVDFCIIHYA 572
Cdd:cd14898 374 EGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI------KKYLNGFINTKARDKIKVSHYA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 573 GKVDYKADEWLMKNmdplnesvatllnqsTDKFTAELWRDMdhivgldkvaGMSDstygafktrKGMFRTVGQLYKEQLG 652
Cdd:cd14898 444 GDVEYDLRDFLDKN---------------REKGQLLIFKNL----------LIND---------EGSKEDLVKYFKDSMN 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 653 NLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNA 725
Cdd:cd14898 490 KLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
93-761 |
1.37e-92 |
|
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: 315.42 E-value: 1.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKhlpIYSEDIvNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQ---VIDVDI-NEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYlaYIASSfkskKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSGV----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSIPEE 332
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 333 ERIGFLkVVSAVLQLGNMTFK---KERHSDQASMPDDT--AAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQ 407
Cdd:cd14937 231 KDDLFL-TLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 408 AEFAVEALAKASYERMFRWLVFRINKALDKTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 487
Cdd:cd14937 310 SVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 488 EEYQREGIEWSFIDFGLDLQpcieLIDKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDvDFC 567
Cdd:cd14937 389 ELYKAEDILIESVKYTTNES----IIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 568 IIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRDMDhivgldkvagMSDSTygafkTRKGMfrtVGQLY 647
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL-----GRKNL---ITFKY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 648 KEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILTPNAIP 727
Cdd:cd14937 526 LKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSK 604
|
650 660 670
....*....|....*....|....*....|....
gi 768942001 728 KGFMDGKQACVLMIKAlELDPNLYRIGQSKVFFR 761
Cdd:cd14937 605 DSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
93-761 |
4.47e-89 |
|
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: 305.59 E-value: 4.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 169
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 170 CTGESGAGKTENTKKVIQYLAYIASSFKSKkdqgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 248
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 249 GANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNG----NMTIPGLQDKELFAETMEAF 324
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 325 HIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAQT 404
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 405 QEQAEFAVEALAKASYERMFRWLVFRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 481
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 482 MFILEQEEYQREGI----------EWSFIDFgldlqpcieLIDKPAgppGILALLDEECWFPKATDKSFVEKV---VQEQ 548
Cdd:cd14878 396 LFLQEQTECVQEGVtmetayspgnQTGVLDF---------FFQKPS---GFLSLLDEESQMIWSVEPNLPKKLqslLESS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 549 GTHPKFQKPKK------LKDD-VDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELwrdmdhivgldk 621
Cdd:cd14878 464 NTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL------------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 622 vagmsdstygaFKTRkgmFRTVGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRIC 701
Cdd:cd14878 532 -----------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIF 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 702 RQGFPNRVVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMIKALELDPnlYRIGQSKVFFR 761
Cdd:cd14878 598 RYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
90-760 |
1.73e-88 |
|
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: 303.70 E-value: 1.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 90 LNEASVLHNLKERYYSGLIYTY---SGLfcVVVNPYKHLPIYSEDIVNMYK-------GKKRHEMPPHIYAITDTAYRSM 159
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 160 MQDREDQSILCTGESGAGKTENTKKVI-QYLAYIASSFKSKKdqgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 238
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK----LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 239 INFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--SNGNMT--IPGLQDK 314
Cdd:cd14879 155 LQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLplGPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 315 ELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSDQASM----PD--DTAAqkvcHLLSVNVTDFtRAIL 388
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAvvknTDvlDIVA----AFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 389 SPRIK-VGRD----YVQKAQTQEQAefavEALAKASYERMFRWLVFRINKALDKTKRQGASFIGILDIAGFEIF---ELN 460
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQR----DELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 461 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIDKPAGppGILALLDEEC-WFPKATDKS 539
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGKPG--GLLGILDDQTrRMPKKTDEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 540 FVEKVVQEQGTHPKFQKPKKLKDDVD---FCIIHYAGKVDYKADEWLMKNMDPLNesvatllnqstdkftaelwrdmdhi 616
Cdd:cd14879 463 MLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVLS------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 617 vgldkvagmsdstyGAFKTrkgMFRTVGQLyKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLE 696
Cdd:cd14879 518 --------------PDFVN---LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPE 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 697 GIRICRQGFPNRVVFQEFRQRYEILTPnaipkgFMDGKQACVLMIKALELDPNLYRIGQSKVFF 760
Cdd:cd14879 580 LAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
93-713 |
8.84e-84 |
|
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: 291.04 E-value: 8.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 164
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 165 DQSILCTGESGAGKTENTKKVIQYLAYIassfKSKKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 242
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 243 -------VNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSE-----------LCLEDYSKYRFLSNG 304
Cdd:cd14884 157 entqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARrnlvrncgvygLLNPDESHQKRSVKG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 305 NMTIPGL----------QDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKerhsdqasmpddtaaqkVCH 374
Cdd:cd14884 237 TLRLGSDsldpseeekaKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA-----------------AAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 375 LLSVNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGA----------- 443
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysine 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 444 SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIDKpagppgIL 523
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------IF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 524 ALLDE-----ECWFPKATDKSFV-----EKVVQEQGTH------PKFQ----KPKKLKDDVdFCIIHYAGKVDYKADEWL 583
Cdd:cd14884 453 RRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDAdgtaKKQNIKKNI-FFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 584 MKNMDPLNESVATLLNQSTDKFTAElwrdmdhivgldkvagmsdstyGAFKTRKGMFRTVGQLYKEQLGNLMTTLRNTNP 663
Cdd:cd14884 532 DKNSDKIETSIETLISCSSNRFLRE----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDM 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 768942001 664 NFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 713
Cdd:cd14884 590 YYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
94-748 |
8.94e-78 |
|
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: 271.60 E-value: 8.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKH----LPIYSEDIVNMYkgkkrhempPHIYAITDTAYRSMMQDREDQSIL 169
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 170 CTGESGAGKTENTKKVIQYLAYIASsfkskkdqGELE----KQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdVNG 245
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 246 YIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYS--KYRFLSNGNMTIPGLQDKELFAETMEA 323
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 324 FHIMSIPeeerigFLKVV---SAVLQLGNMTFKkERHSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQ 400
Cdd:cd14881 224 LGILGIP------FLDVVrvlAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 401 KAQTQEQAEFAVEALAKASYERMFRWLVFRINKaldkTKRQGAS--------FIGILDIAGFEIFELNSFEQLCINYTNE 472
Cdd:cd14881 297 SVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 473 KLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIELIDkpAGPPGILALLDEECwFPKATDKSFVEKVVQEQGTH 551
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 552 PKFQKPKKlKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFtaelwrdmdhivgldkvagmsdstyg 631
Cdd:cd14881 449 PRLFEAKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF-------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 632 AFKTRKGMFRTvgqlykeQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVF 711
Cdd:cd14881 502 GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650 660 670
....*....|....*....|....*....|....*....
gi 768942001 712 QEFRQRYEILTPNAIPKGFMDGKQAC--VLMIKALELDP 748
Cdd:cd14881 575 KAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
94-714 |
5.59e-74 |
|
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: 261.95 E-value: 5.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLP-IYSEDIVNMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSfKSKKdqgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 252
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 253 ETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNMTIPGLQDKELFAETMEAFHIMSIPE 331
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 332 EERIGFLKVVSAVLQLGNMTFKKErhSDQASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDYVQKAqtqeqaefa 411
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 412 vEALAKASYERMFRWLVFRINKALDKTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 491
Cdd:cd14905 304 -DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 492 REGIEW-SFIDFGlDLQPCIELIDKpagppgILALLDEECWFPKATDKSFVEKVVQEQGTHPKF-QKPKKlkddvdFCII 569
Cdd:cd14905 381 TERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 570 HYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAElwrdMDHIVGLDKVAGMSDSTYGAFKTRK-------GMFRT 642
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFS----RDGVFNINATVAELNQMFDAKNTAKksplsivKVLLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 643 VGQLYKEQL-----------------------GNLMTTLRNTNP---------NFVRCIIPNHEKKAGKLEPHLVLDQLR 690
Cdd:cd14905 524 CGSNNPNNVnnpnnnsgggggggnsgggsgsgGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660
....*....|....*....|....*...
gi 768942001 691 CNGVLEGIRICRQGFP----NRVVFQEF 714
Cdd:cd14905 604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
93-726 |
2.24e-68 |
|
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: 244.01 E-value: 2.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 93 ASVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 171
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 172 GESGAGKTENTKKVIQYLAyiaSSFKSKKDQgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNgYIVGAN 251
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTT----KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 252 IE-TYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDKELFAETMEAFHIMSIP 330
Cdd:cd14874 143 LKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 331 EEERIGFLKVVSAVLQLGNMTFKKERHS----DQASMPDDTAAQKVCHLLSVNVTDFTrAILSPRIKVGrdyvqKAQTQE 406
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNPnveqDVVEIGNMSEVKWVAFLLEVDFDQLV-NFLLPKSEDG-----TTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 407 QAEFAVEALAKASYERMFRWLVFRINKALDKTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 486
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 487 QEEYQREGIEwsfIDF----GLDLQPCIELIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKlKD 562
Cdd:cd14874 375 LVDYAKDGIS---VDYkvpnSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 563 DVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWRdmdhivgldkvagmsdsTYGAfkTRKGMFRT 642
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE-----------------SYSS--NTSDMIVS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 643 VGQLYKEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 722
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 768942001 723 PNAI 726
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
96-719 |
1.33e-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: 244.50 E-value: 1.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 96 LHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKR----------HEMPPHIYAITDTAYRSMMQDRED 165
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 166 QSILCTGESGAGKTENTKKVIQYLAYIASSFKSKKD-QGE------LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 238
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDsEGAsgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 239 INFDVNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAG------DKLRSELCLEDYSKYRFLSN--GNMTIpg 310
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdptlrDSLEMNKCVNEFVMLKQADPlaTNFAL-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 311 lqDKELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKE---------------RHSDQASMPDDTAAQKVCHL 375
Cdd:cd14893 242 --DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDpeggksvggansttvSDAQSCALKDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 376 LSVN--VTD---FTRAILSpriKVGRDYVQ--KAQTQEQAEFAVEALAKASYERMFRWLVFRINKAL----DKTKRQG-- 442
Cdd:cd14893 320 LEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNiv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 443 --ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWSFIDFGLDLQPCIE 511
Cdd:cd14893 397 inSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 512 LIDKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKKLKDDVD------------FCIIHYAGKVDYKA 579
Cdd:cd14893 477 LFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 580 DEWLMKNMDPLNESVATLLNQSTDKFTaelwrdmdHIVGLDKVAGMSDSTYGAFKTRKG----MFRTVGQLYKE------ 649
Cdd:cd14893 555 KGLSSKNMLSISSTCAAIMQSSKNAVL--------HAVGAAQMAAASSEKAAKQTEERGstssKFRKSASSAREsknitd 626
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 650 --------QLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 719
Cdd:cd14893 627 saatdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
94-761 |
1.98e-65 |
|
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: 235.79 E-value: 1.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 174 SGAGKTENTKKVIQYLAYIAssfKSKKDQGElekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 253
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---DGNRGATG---RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 254 TYLLEKSRAIRQAKEERSFHIFYYLLTG--AGDKLRsELCLEDYSKYRFLSngnmTIPGLQDKEL-------------FA 318
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR----IPPEVPPSKLkyrrddpegnverYK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 319 ETMEAFHIMSIPEEERIGFLKVVSAVLQLGNMTFKKERHSdqASMPDDTAAQKVCHLLSVNVTDFTRAILSPRIKVGRDY 398
Cdd:cd14882 231 EFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 399 VQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTNEK 473
Cdd:cd14882 309 ERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 474 LQQLFNHTMFI---LEQEEYQREGIEWSFIDFGLDLQpciELIDKPAgppGILALLDEECwfPKATDKSFVEKVVQEQgt 550
Cdd:cd14882 386 MQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYIMDRIKEK-- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 551 HPKFQKPKKlkdDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTDKFTAELWrdmdhivgldkvagmSDSTY 630
Cdd:cd14882 456 HSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF---------------TNSQV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 631 GAFKTRKGMFRTVGQlykEQLGNLMTTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVV 710
Cdd:cd14882 518 RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 768942001 711 FQEFRQRYEILTPNAIPKGFMDgKQACVLMIKALELDPnlYRIGQSKVFFR 761
Cdd:cd14882 595 FQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-246 |
2.35e-58 |
|
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: 199.11 E-value: 2.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 115 FCVVVNPYKHLPIYSEDIV-NMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYIA 193
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 194 SSFKSKKD----------QGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 246
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 ... |
94-759 |
1.86e-53 |
|
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: 201.60 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 94 SVLHNLKERYYSGLIYTYSGLFCVVVNPYKHLPIYSEDIVNMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 173 ESGAGKTENTKKVIQYLAYIASSFKS------------------KKDQGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 234
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 235 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERSFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNMTIPGLQDK 314
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 315 ELFAETMEAFHIMSIPEEERIGFLKVVSAVLQLGN--------------------MTFKKERHSDQASMPDDTAAQK--- 371
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllmgknqcgQNINYETILSELENSEDIGLDEnvk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 372 ----VCHLLSVNVTDFTRAILSPRIkVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVFRINKALDKTKR--QGASF 445
Cdd:cd14938 321 nlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 446 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIDKPAgpPGILAL 525
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 526 LDEECWFPKATDKS-FVEKVVQEQGTHPKFQKPKKLKDDVD-FCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTD 603
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITGNKKtFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 604 KFTAELWRDMDHivglDKVAGMSD-----STYGAFKTRKGMFRTVGQLYKEQLGNLMTTLRN----TNPNFVRCIIPNHE 674
Cdd:cd14938 558 EYMRQFCMFYNY----DNSGNIVEekrrySIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKlqetTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 675 KKA-GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnaipkgfmDGKQACVLMIKALELDPNLYRI 753
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 768942001 754 GQSKVF 759
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
989-1831 |
2.60e-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: 131.33 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 989 KEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQI 1068
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1069 ADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDT 1148
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1149 LdttAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQakrnklsVEKAKQALESEFNELQI 1228
Cdd:TIGR02168 392 E---LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE-------LEEELEELQEELERLEE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1229 ELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEavekiakLQSELENVNSLLNESEGKNTKSS--KDMLSLESH 1306
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN-------LEGFSEGVKALLKNQSGLSGILGvlSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1307 LQDTQELLQEETRQKLAISTrFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKR 1386
Cdd:TIGR02168 535 YEAAIEAALGGRLQAVVVEN-LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1387 LQREFDTVKLQL---EEKEAAYEKLERTKTRLQQ-ELDDLLVNQDGLrqlvnnMERKQRKFDQMLAEEKTISTQYAEERD 1462
Cdd:TIGR02168 614 LRKALSYLLGGVlvvDDLDNALELAKKLRPGYRIvTLDGDLVRPGGV------ITGGSAKTNSSILERRREIEELEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1463 KAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELE 1542
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1543 DELQATEDAKLRLEVNMQamkaqfdrDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVH 1622
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIE--------ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1623 IDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDE 1702
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1703 LQDEINGNNTKNSMLQDEKRRLEARITQLEEELEeeqlnsEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAER 1782
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL------EEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIE 993
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 768942001 1783 KNKELSLKLQELestikSKYKSSLTALEAKVAQLEEQLDTEIKERQQAT 1831
Cdd:TIGR02168 994 EYEELKERYDFL-----TAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1038-1885 |
7.27e-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: 129.79 E-value: 7.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1038 KQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQ--LANKEEELQNALIRIEEEAAANmasqkKIKELEAQILELDE 1115
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQaeKAERYKELKAELRELELALLVL-----RLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1116 DLERekfyrskNGQRCKELEKELEAIKNKLDDTLDttaAQQELRAKRETEVAQLRKAQEEENKM-HESQIAELSKKHLQA 1194
Cdd:TIGR02168 247 ELKE-------AEEELEELTAELQELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1195 FNEM-NEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIA 1273
Cdd:TIGR02168 317 QLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1274 KLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQellqeetrqKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVE 1353
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1354 KQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEK----------------EAAYEK-LErtkTRLQ 1416
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlselisvDEGYEAaIE---AALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1417 QELDDLLV-NQDGLRQLVNNMERKQRKFDQMLAEektiSTQYAEERDKAEAEAREKETRALTLARELET----------- 1484
Cdd:TIGR02168 545 GRLQAVVVeNLNAAKKAIAFLKQNELGRVTFLPL----DSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsy 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1485 -------ITDLKNELERTNKQLKAEM-----EDLVSSK---------------------DDAGKNVHELERSKRATEQQL 1531
Cdd:TIGR02168 621 llggvlvVDDLDNALELAKKLRPGYRivtldGDLVRPGgvitggsaktnssilerrreiEELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1532 EEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKK 1611
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1612 LELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAER 1691
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1692 LKRQMQAERDELQDEINGnntknsmLQDEKRRLEARItqleeeleeeqlnsEMANDRNKRTTLQVDQLTAELSAERSAAQ 1771
Cdd:TIGR02168 860 EIEELEELIEELESELEA-------LLNERASLEEAL--------------ALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1772 RLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKVAQLEEqldteikERQQATRMVRRTEKKMKEL---VLQV 1848
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED-------DEEEARRRLKRLENKIKELgpvNLAA 991
|
890 900 910
....*....|....*....|....*....|....*..
gi 768942001 1849 EDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTR 1885
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1161-1920 |
1.73e-29 |
|
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: 128.64 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1161 KRETEvAQLRKAQEEENKMhESQIAELSK--KHLQAFNEMNEQLeQAKRNKLSvEKAKQALESEFNELQIELKTLGQSKS 1238
Cdd:TIGR02168 174 RKETE-RKLERTRENLDRL-EDILNELERqlKSLERQAEKAERY-KELKAELR-ELELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1239 DSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEET 1318
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1319 RQKLAISTRFRQMEEEQNSLRemleeeeeakknveKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQL 1398
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELK--------------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1399 EEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQlvnNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTL 1478
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLK---KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1479 ARELetITDLKNELERTNKQLKAeMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAklrLEVN 1558
Cdd:TIGR02168 473 AEQA--LDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1559 MQAMkaqFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGR-------- 1630
Cdd:TIGR02168 547 LQAV---VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllg 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1631 --------DEALKQLKKLQVQF----KD---------MMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATA 1689
Cdd:TIGR02168 624 gvlvvddlDNALELAKKLRPGYrivtLDgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1690 ERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARItqleeeleeeqlnsEMANDRNKRTTLQVDQLTAELSAERSA 1769
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV--------------EQLEERIAQLSKELTELEAEIEELEER 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1770 AQRLEGARSQAERKNKELSLKLQELESTIKSkYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVE 1849
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1850 DERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSKLRR 1920
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
885-1613 |
3.18e-29 |
|
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: 127.87 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 885 QLQAET-----ELCAEAEEMRARL-VNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQK 958
Cdd:TIGR02168 206 ERQAEKaerykELKAELRELELALlVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 959 LQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEK 1038
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1039 QRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEE-----EAAANMASQKKIKELEAQILEL 1113
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1114 DEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEE--ENKMHESQIAELsKKH 1191
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGI-LGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1192 LQAFNEMNEQLEQAKRNKL----------SVEKAKQALES-EFNELQ----IELKTLGQSKSDSEHRRKKAES------- 1249
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALggrlqavvveNLNAAKKAIAFlKQNELGrvtfLPLDSIKGTEIQGNDREILKNIegflgva 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1250 ----------------------------QVQELQVKYGDCER-----------------QRQEAVEKIAKLQSELENVNS 1284
Cdd:TIGR02168 605 kdlvkfdpklrkalsyllggvlvvddldNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1285 LLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLG 1364
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1365 DMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLlvnQDGLRQLVNNMERKQRKFD 1444
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL---RERLESLERRIAATERRLE 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1445 QMLAEEKTIStqyaEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSK 1524
Cdd:TIGR02168 842 DLEEQIEELS----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1525 RATEQQLEEIKTQLEELEDELQATEDaKLRLEVNMQAMKA-QFDRDLQARDEQGEERRKQLVKQVHEL---------EAE 1594
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYE 996
|
810 820
....*....|....*....|....
gi 768942001 1595 LEDERR-----QRSQAVSAKKKLE 1613
Cdd:TIGR02168 997 ELKERYdfltaQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
835-1688 |
9.88e-29 |
|
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: 126.34 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 835 LQVTRQEEEMLAKEDELSKVKEKqLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEIL 914
Cdd:TIGR02169 200 LERLRREREKAERYQALLKEKRE-YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 915 HDMESRLEEEEERVNQMLN----ERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKE 990
Cdd:TIGR02169 279 KKIKDLGEEEQLRVKEKIGeleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 991 KKLLEDRIAEFSSNLSEEEEKSRSL-QKLKnkheaiitDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIA 1069
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETrDELK--------DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1070 DLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKnklDDTL 1149
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE---ERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1150 DTTAAQQELRAKRE---TEVAQLRKAQEEenkmHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNEL 1226
Cdd:TIGR02169 508 GGRAVEEVLKASIQgvhGTVAQLGSVGER----YATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1227 QIELKTLGQSKSDSehrrkkaesqVQELQVKYGDCERQRQEAVEKIakLQSELEnVNSLlneSEGKNTKSSKDMLSLESH 1306
Cdd:TIGR02169 584 RDERRDLSILSEDG----------VIGFAVDLVEFDPKYEPAFKYV--FGDTLV-VEDI---EAARRLMGKYRMVTLEGE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1307 LQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKR 1386
Cdd:TIGR02169 648 LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1387 LQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTisTQYAEERDKAEA 1466
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1467 EAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQ 1546
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1547 ATEDAKLRLEVNMQAMKAQFDrDLQARDEQGEERRKQLVKQVHELE---AELEDERRQRSQAVSAK---KKLELDLGELE 1620
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEIPEEElslEDVQAELQRVE 964
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1621 VHIDA-------ANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAinsakETEKK---VKTMEADAAQFQEDLAT 1688
Cdd:TIGR02169 965 EEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-----EKKKRevfMEAFEAINENFNEIFAE 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1534 |
9.22e-28 |
|
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: 123.24 E-value: 9.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILH 915
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 916 DMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKM--KALEGNIMVLDDQNNKLNKEKKL 993
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 994 LEDRIAEFSSNLSEEEEKSRSLQKLKNKHE------AIITDLEDRLRKEEKQRQELEKNRRKLEGdstdLHDQIADLQAQ 1067
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAqlqarlDSLERLQENLEGFSEGVKALLKNQSGLSG----ILGVLSELISV 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1068 IADLRAQLANK-EEELQNALIRIEEEAAANMASQKKIKELEAQILELDE----DLEREKFYRSKNGQRCKELEKELEAIK 1142
Cdd:TIGR02168 532 DEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1143 NKLD-------------DTLDTTAAQQELRAKRETEV-----------AQLRKAQEEENKM--HESQIAELSKKhlqaFN 1196
Cdd:TIGR02168 612 PKLRkalsyllggvlvvDDLDNALELAKKLRPGYRIVtldgdlvrpggVITGGSAKTNSSIleRRREIEELEEK----IE 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1197 EMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQ 1276
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1277 SELENVNSLLNESEGKntksskdMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQI 1356
Cdd:TIGR02168 768 ERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1357 SVLQGQLGDMKKKMDQEVSSLESAEESRKRLQRE-------FDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGL 1429
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1430 RQLVNNMERKQRKFDQMLAE-EKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVS 1508
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE 1000
|
730 740
....*....|....*....|....*.
gi 768942001 1509 SKDDAGKNVHELERSKRATEQQLEEI 1534
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
989-1848 |
2.98e-26 |
|
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: 118.25 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 989 KEKKLLEDRIA---EFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEK----NRRKLEGDSTDLHDQI 1061
Cdd:TIGR02169 153 VERRKIIDEIAgvaEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1062 ADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILEL--DEDLEREKFYRSKNGQRCKeLEKELE 1139
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGELEAEIAS-LERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1140 AIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKhlqafnemnEQLEQAKRNKL-SVEKAKQA 1218
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL---------KEELEDLRAELeEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1219 LESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSK 1298
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1299 DMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLE 1378
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1379 SAeeSRKRLQreFDTVKLQLEEKEAAyEKLERTK---------TRLQQELDDL--------------LVNQD-------- 1427
Cdd:TIGR02169 543 VA--AGNRLN--NVVVEDDAVAKEAI-ELLKRRKagratflplNKMRDERRDLsilsedgvigfavdLVEFDpkyepafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1428 ---GLRQLVNNMERKQRKFDQM--------LAEEKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTN 1496
Cdd:TIGR02169 618 yvfGDTLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1497 KQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQamkaqfdrDLQARDEQ 1576
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK--------ELEARIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1577 GEERRKQLVKQVHELEAELEDERRQRSQAvsAKKKLELDLGELEVHIDAANKgrdealkQLKKLQVQFKDMMRESEDLRL 1656
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQA--ELSKLEEEVSRIEARLREIEQ-------KLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1657 SRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELE 1736
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1737 EEQLNSEMANDRNKrttlQVDQLTAELSAERSAAQRLEGARSQAERKNKELSlKLQELESTIKSKYKSSLTALEakvaQL 1816
Cdd:TIGR02169 921 ELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLD----EL 991
|
890 900 910
....*....|....*....|....*....|..
gi 768942001 1817 EEQLDTEIKERQQATRMVRRTEKKMKELVLQV 1848
Cdd:TIGR02169 992 KEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1091-1902 |
1.36e-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: 115.92 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1091 EEAAANMASQKKIKELEAQILELDEDLER------------EKFYR-SKNGQRCKELEKELEAIKNKLDdTLDTTAAQQE 1157
Cdd:TIGR02168 162 EEAAGISKYKERRKETERKLERTRENLDRledilnelerqlKSLERqAEKAERYKELKAELRELELALL-VLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1158 LRAKREtevaQLRKAQEEENKmHESQIAELSkkhlqafnemnEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSK 1237
Cdd:TIGR02168 241 LEELQE----ELKEAEEELEE-LTAELQELE-----------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1238 SDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQ-- 1315
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtl 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1316 -----EETRQKLAISTRFRQMEEEQNSL-----REMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRK 1385
Cdd:TIGR02168 385 rskvaQLELQIASLNNEIERLEARLERLedrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1386 RLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQmLAE--------EKTIST-- 1455
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSElisvdegyEAAIEAal 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1456 ----QYAEERDKAEAE------AREKETRALTLARELETITDLKNELERTNKQLKAEM---EDLVSSKDDAGKNVHELER 1522
Cdd:TIGR02168 544 ggrlQAVVVENLNAAKkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLgvaKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1523 SKRATEQQLEEIKTQLEELEDELQATEDAKL----------RLEVNMQAM-KAQFDRDLQARDEQGEERRKQLVKQVHEL 1591
Cdd:TIGR02168 624 GVLVVDDLDNALELAKKLRPGYRIVTLDGDLvrpggvitggSAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1592 EAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKK 1671
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1672 VKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANdrnkr 1751
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA----- 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1752 ttLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKsKYKSSLTALEAKVAQLEEQLdTEIKERQQAT 1831
Cdd:TIGR02168 859 --AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-ELESKRSELRRELEELREKL-AQLELRLEGL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1832 RMVRRT--EKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEE-------AEEEVTRANAYRRKLQRELEDANE 1902
Cdd:TIGR02168 935 EVRIDNlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
209-702 |
5.75e-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: 113.68 E-value: 5.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 209 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KEERSFHIFYY 277
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 278 LLTGAG-----DKLRSELCLE--DYSKYRFLSNGNMTIPGL--------QDKELFAETMEAFHIMSIPEEERIGFLKVVS 342
Cdd:cd14894 329 MVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 343 AVLQLGNMTFKKERHSDQASMPDD---TAAQKVCHLLSV-NVTDFTRAILSPRIKVGRDYVQKAQTQE--QAEFAVEALA 416
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 417 KASYERMFRWLVFRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQqlfnh 480
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 481 tmfileQEEYQREGIEWSFIDFGLDLQPCIELIDKPAGPPGILALLDEECWFPKAT----------DKSFVEKVVQEQGT 550
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 551 H----PKFQKPKK-----LKDDVDFCIIHYAGKVDYKADEWLMKNMDPLNESVATLLNQSTdkfTAELWRDMDHIVGLDK 621
Cdd:cd14894 638 RlpepPRVLSNAKrhtpvLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSN---SSHFCRMLNESSQLGW 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 622 VAGMSDSTYGAFKTR-KGMFRTVGQLYKEQlgNLMTTLRNTN-PNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 699
Cdd:cd14894 715 SPNTNRSMLGSAESRlSGTKSFVGQFRSHV--NVLTSQDDKNmPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 768942001 700 ICR 702
Cdd:cd14894 793 ICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1023-1660 |
5.86e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1023 EAIITDLEDRLRKEEKQR------QELEKNRRKLEGDStdlhdqiadLQAQIADLRAQLANKEEELQNALIRIEEEAAAN 1096
Cdd:COG1196 192 EDILGELERQLEPLERQAekaeryRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1097 MASQKKIKELEAQILELDEDLERekfyrskNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEE 1176
Cdd:COG1196 263 AELEAELEELRLELEELELELEE-------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1177 nkmhESQIAELSKKHLQAfnemNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELqv 1256
Cdd:COG1196 336 ----EEELEELEEELEEA----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1257 kygdcERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQN 1336
Cdd:COG1196 406 -----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1337 SLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQ 1416
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1417 QELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAE-ERDKAEAEAREKETRALTLARELETITD-----LKN 1490
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLvASDLREADARYYVLGDTLLGRTLVAARLeaalrRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1491 ELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdL 1570
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE----R 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1571 QARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDE-------ALKQLKKLQVQ 1643
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEER 796
|
650
....*....|....*..
gi 768942001 1644 FKDMMRESEDLRLSRDE 1660
Cdd:COG1196 797 YDFLSEQREDLEEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1243-1899 |
2.95e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1243 RRKKAESQ--------------VQELQVKYGDCERQRQEAvEKIAKLQSELENVnsllnesegKNTKSSKDMLSLESHLQ 1308
Cdd:COG1196 173 RKEEAERKleateenlerlediLGELERQLEPLERQAEKA-ERYRELKEELKEL---------EAELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1309 DTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEakknvekQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQ 1388
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1389 REFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEA 1468
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1469 REKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQAT 1548
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1549 EDAKLRLEVNMQAMKAQFDRDLQARDEQGEE----RRKQLVKQVHELEAELEDERRQRSQAVSAkkkLELDLGELEVHI- 1623
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVEAAYEAA---LEAALAAALQNIv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1624 ---DAANKGRDEALKQLKKLQVQFkdmmresedLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAER 1700
Cdd:COG1196 553 vedDEVAAAAIEYLKAAKAGRATF---------LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1701 DELQDEINGNNTKNSMLQDEKRRLEARITQleeeleeeqlnsEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQA 1780
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEG------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1781 ERKNKELSLKLQELEStikskykssltALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKD 1860
Cdd:COG1196 692 ELELEEALLAEEEEER-----------ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 768942001 1861 QADKLNSRTRQLKRQLEE-------AEEEVTRANAYRRKLQRELED 1899
Cdd:COG1196 761 DLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1264-1919 |
2.99e-23 |
|
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: 108.22 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1264 QRQEAVEKIAKLQSELENVNSLLNEsegknTKSSKDMLSLESHL-QDTQELLQEETRQKLAIST-RFRQMEEEQNSLREM 1341
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNE-----LERQLKSLERQAEKaERYKELKAELRELELALLVlRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1342 LEEEEEAKKNVEKQISVLQGQL-------GDMKKKMD------QEVSSLESAEESRKRLQRE-FDTVKLQLEEKEAAYEK 1407
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLeelrlevSELEEEIEelqkelYALANEISRLEQQKQILRErLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1408 LERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETITD 1487
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1488 LKNELERTNKQLKAEMEDLVSSKDDAgkNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFD 1567
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1568 RdLQARDEqGEERRKQLVKQVHELEAELEDERRQR-------SQAVSAKKKLEL--------DLGELEVHIDAANKGRDE 1632
Cdd:TIGR02168 486 Q-LQARLD-SLERLQENLEGFSEGVKALLKNQSGLsgilgvlSELISVDEGYEAaieaalggRLQAVVVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1633 ALKQLKKLQVQFKDMMRESE-DLRLSRDEAINSAKETEKKVKTMEADAAQFQ-------------EDLATAERLKRQM-- 1696
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLrp 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1697 --------------------------------QAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEM 1744
Cdd:TIGR02168 644 gyrivtldgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1745 ANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKyKSSLTALEAKVAQLEEQLDTEI 1824
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1825 KERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQ 1904
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730
....*....|....*
gi 768942001 1905 DTMNREVNILKSKLR 1919
Cdd:TIGR02168 883 ASLEEALALLRSELE 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
853-1422 |
1.50e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 853 KVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEIlhdmESRLEEEEERVNQML 932
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 933 NERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKS 1012
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1013 RSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEE 1092
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1093 AAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRckeLEKELEAIKNKLDDTLDTTAAQQELRAKR-ETEVAQLRK 1171
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR---LLLLLEAEADYEGFLEGVKAALLLAGLRGlAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1172 AQEEEnkmhESQIAELSKKHLQAFNEMNEQLEQAKRNKLsveKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQV 1251
Cdd:COG1196 532 VEAAY----EAALEAALAAALQNIVVEDDEVAAAAIEYL---KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1252 QELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQM 1331
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1332 EEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREF----DTVKLQLEEKEAAYEK 1407
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEeellEEEALEELPEPPDLEE 764
|
570
....*....|....*
gi 768942001 1408 LERTKTRLQQELDDL 1422
Cdd:COG1196 765 LERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
815-1443 |
1.82e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 815 AYLKLRNWQWWRLftkvkpllQVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCA 894
Cdd:COG1196 227 AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 895 EAEEMRARLVNRKQELEEilhdmesRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALE 974
Cdd:COG1196 299 RLEQDIARLEERRRELEE-------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 975 GNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDS 1054
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1055 TDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAanmasqkKIKELEAQILELDEDLEREKFYRSKNGQRCKEL 1134
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1135 EKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAfnemnEQLEQAKRNKLSVEK 1214
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-----RAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1215 AKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNT 1294
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1295 KSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEV 1374
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1375 SSLESAEESRKRLQREfdtvklqLEEKEA----AYEKLERTKTR---LQQELDDLLVNQDGLRQLVNNMER-KQRKF 1443
Cdd:COG1196 760 PDLEELERELERLERE-------IEALGPvnllAIEEYEELEERydfLSEQREDLEEARETLEEAIEEIDReTRERF 829
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1294-1920 |
2.67e-21 |
|
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: 101.79 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1294 TKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQ-------LGDM 1366
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARkqeleeiLHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1367 KKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQEL----DDLLVNQDGLRQLVNN---MERK 1439
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIkkleEDILLLEDQNSKLSKErklLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1440 QRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRaltLARELETitdlKNELERTNKQLKAEMEDLVSSKDDagknvhe 1519
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEER---LKKEEKG----RQELEKAKRKLEGESTDLQEQIAE------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1520 lerskraTEQQLEEIKTQLEELEDELQAtedAKLRLEvnmqamkaqfdrDLQARDEQGEERRKQLVKQVHELEAELEDER 1599
Cdd:pfam01576 227 -------LQAQIAELRAQLAKKEEELQA---ALARLE------------EETAQKNNALKKIRELEAQISELQEDLESER 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1600 RQRSQAVSAKKKLELDL----GELEVHIDAAN------KGRDEALKQLKK-LQVQFKDMMRESEDLRLSRDEAINSAKEt 1668
Cdd:pfam01576 285 AARNKAEKQRRDLGEELealkTELEDTLDTTAaqqelrSKREQEVTELKKaLEEETRSHEAQLQEMRQKHTQALEELTE- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1669 ekkvktmeaDAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDR 1748
Cdd:pfam01576 364 ---------QLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1749 NKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQElESTIKSKYKSSLTALEAKVAQLEEQLDTEIKERQ 1828
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1829 QATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMN 1908
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQR 593
|
650
....*....|..
gi 768942001 1909 REVNILKSKLRR 1920
Cdd:pfam01576 594 QLVSNLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
846-1707 |
2.73e-20 |
|
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: 98.51 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 846 AKEDELSKVKEKQLQ-AEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLEEE 924
Cdd:pfam02463 170 KKKEALKKLIEETENlAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 925 EERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSN 1004
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1005 LSEEEEKSRSLQKLKNKHEAIITDLEDRlRKEEKQRQELEknRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQN 1084
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEE-EEELEKLQEKL--EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1085 ALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEaIKNKLDDTLDTTAAQQELRAKRET 1164
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL-KDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1165 EVAQLRKAQEEENKMHESQIAELSKKHL---QAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSE 1241
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLaliKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1242 HRRKKAESQVQELQVKYGDceRQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQK 1321
Cdd:pfam02463 566 LVRALTELPLGARKLRLLI--PKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1322 LAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQgqlGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEK 1401
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQ---EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1402 EAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARE 1481
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1482 LEtitdlKNELERTNKQLKAEMEdlvssKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDElqatedAKLRLEVNMQA 1561
Cdd:pfam02463 801 EE-----LRALEEELKEEAELLE-----EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE------EELERLEEEIT 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1562 MKAQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQ 1641
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1642 VQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQ-MQAERDELQDEI 1707
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKErLEEEKKKLIRAI 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1399-1922 |
5.48e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1399 EEKEAAYEKLERTKTRLqQELDDLlvnqdgLRQLVNNME------RKQRKFDQMLAEEKTISTQ-YAEERDKAEAEAREK 1471
Cdd:COG1196 172 ERKEEAERKLEATEENL-ERLEDI------LGELERQLEplerqaEKAERYRELKEELKELEAElLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1472 ETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDA 1551
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1552 KLRLEvnmqamkaQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRD 1631
Cdd:COG1196 325 LAELE--------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1632 EALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNN 1711
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1712 TKNSMLQDEKRRLEARITQLEEELEEEQLNSE-----MANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQaeRKNKE 1786
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ--NIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1787 LSLKLQELESTIKSKYKSSLTAL------EAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQyKD 1860
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLpldkirARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR-LE 633
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1861 QADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSKLRRDL 1922
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
911-1567 |
1.06e-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: 96.24 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 911 EEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKE 990
Cdd:TIGR04523 53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 991 KKLLEDRIAEFssnLSEEEEKSRSLQKLKNKHEAIItdledrlrkeeKQRQELEKNRRKLEgdstdlhDQIADLQAQIAD 1070
Cdd:TIGR04523 133 KKENKKNIDKF---LTEIKKKEKELEKLNNKYNDLK-----------KQKEELENELNLLE-------KEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1071 LRAQLANKEEELQNalirIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLD 1150
Cdd:TIGR04523 192 IKNKLLKLELLLSN----LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1151 TTAAQQELRAKRETEVAQLrkaqEEENKMHESQIAELSKKHLQAFN-EMNEQLEQAKRNKLSVEKAKQALESEFNELQIE 1229
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKEL----EKQLNQLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1230 LKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENvnsllnesegkntksskdmlsLESHLQD 1309
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND---------------------LESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1310 TQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQR 1389
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1390 EFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLA--EEKTISTQYAEERDKAEAE 1467
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdlEDELNKDDFELKKENLEKE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1468 AREKEtraltlaRELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQA 1547
Cdd:TIGR04523 563 IDEKN-------KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650 660
....*....|....*....|
gi 768942001 1548 TEDAKLRLEVNMQAMKAQFD 1567
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIK 655
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
834-1416 |
1.85e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.41 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 834 LLQVTRQEE-------EMLAKEDELSKVKEKQLQAEEMIKEFESKQ--QQLNAEKMALQEqLQAETELCaeaEEMRARLV 904
Cdd:PRK02224 158 LLQLGKLEEyrerasdARLGVERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAE-LDEEIERY---EEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 905 NRKQELEEILHDMESRleeeeervnqmlnerkkmQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQN 984
Cdd:PRK02224 234 ETRDEADEVLEEHEER------------------REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 985 NKLNKEKKL-------LEDRIAEFSSNLSEE----EEKSRSLQKLKNKHEAI---ITDLEDRLRKEEKQRQELEKNRRKL 1050
Cdd:PRK02224 296 DDLLAEAGLddadaeaVEARREELEDRDEELrdrlEECRVAAQAHNEEAESLredADDLEERAEELREEAAELESELEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1051 EGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNgqR 1130
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAG--K 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1131 CKELEKELEAiknklDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESqiaelskkhLQAFNEMNEQLEQAKRNKL 1210
Cdd:PRK02224 454 CPECGQPVEG-----SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER---------AEDLVEAEDRIERLEERRE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1211 SVEKAKQALESEFNELQIELKTLGQSKSD-----SEHRRK--KAESQVQELQVKYGDCERQRQ------EAVEKIAKLQS 1277
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAEleaeaEEKREAaaEAEEEAEEAREEVAELNSKLAelkeriESLERIRTLLA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1278 ELENVNSllnesegkntksskDMLSLESHLQDTQElLQEETRQKLA-ISTRFRQMEEEQNSLRemleeeeeakknvekqI 1356
Cdd:PRK02224 600 AIADAED--------------EIERLREKREALAE-LNDERRERLAeKRERKRELEAEFDEAR----------------I 648
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1357 SVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQ 1416
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
906-1621 |
2.37e-18 |
|
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: 92.10 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 906 RKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDE--EEADRQKLQMEKVTTDSKMKALEGNIMVLDDQ 983
Cdd:pfam15921 104 QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNtvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 984 nNKLNKEKKLLEDriAEFSSNLSEEEEKSRSLQKLKNKHEAIitdledrlrkeekqrqelEKNRRKLEGDSTDLHDQIAD 1063
Cdd:pfam15921 184 -GVLQEIRSILVD--FEEASGKKIYEHDSMSTMHFRSLGSAI------------------SKILRELDTEISYLKGRIFP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1064 LQAQIADLRAQLANKEE-ELQNALIRIEEeaaanmasqkKIKELEAQILELDEDlerekfyRSKNGQRCKELEKELEAIK 1142
Cdd:pfam15921 243 VEDQLEALKSESQNKIElLLQQHQDRIEQ----------LISEHEVEITGLTEK-------ASSARSQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1143 nklDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQleQAKRNKLSVEKAK-----Q 1217
Cdd:pfam15921 306 ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEA--RTERDQFSQESGNlddqlQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1218 ALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGD--CERQRQEAVEKIAK--LQSELENVNSLLnesEGKN 1293
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnMEVQRLEALLKAMKseCQGQMERQMAAI---QGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1294 tKSSKDMLSLESHLQDTQELL----QEETRQKLAISTRFRQMEEEQNSLREMLEEeeeakknvekqISVLQGQLGDMKKK 1369
Cdd:pfam15921 458 -ESLEKVSSLTAQLESTKEMLrkvvEELTAKKMTLESSERTVSDLTASLQEKERA-----------IEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1370 MD---QEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQelddlLVNQDGlrQLVNNMERKQRKFDQM 1446
Cdd:pfam15921 526 VDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ-----LVGQHG--RTAGAMQVEKAQLEKE 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1447 LAEEKTISTQYAEERDKAEAEAREKETRALTLARE-----------LETITDLK-------NELERTNKQLKAEMEDLVS 1508
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklvnagserLRAVKDIKqerdqllNEVKTSRNELNSLSEDYEV 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1509 SKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAK---LRLEVNMQ----AMKAQFDRdLQARDEQGEERR 1581
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghaMKVAMGMQkqitAKRGQIDA-LQSKIQFLEEAM 757
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 768942001 1582 KQLVKQVHELEAELEDERRQRSQAVSAKKKLEldlGELEV 1621
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMA---GELEV 794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1233 |
1.23e-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: 90.12 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 844 MLAKEDELSKVKEKqlqaeemIKEFESKQQQLNAEKMALQEQLQaetelcaEAEEMRARLVNRKQELEEILHDMESRLEE 923
Cdd:TIGR02168 672 ILERRREIEELEEK-------IEELEEKIAELEKALAELRKELE-------ELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 924 EEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNImvlddqnNKLNKEKKLLEDRIAEFSS 1003
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-------EQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1004 NLSEEEEKSRSLQKLKNKHEAIITDLEDRLrkeekqrQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQ 1083
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1084 NALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTA-AQQELRAKR 1162
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeEAEALENKI 963
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1163 ETEVAQLRkaqeEENKMHESQIAELSKKHLQA---FNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTL 1233
Cdd:TIGR02168 964 EDDEEEAR----RRLKRLENKIKELGPVNLAAieeYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1182-1918 |
5.48e-17 |
|
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: 87.82 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1182 SQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALEsefnELQIELKTLGQSKsdsEHRRKKAESQVQELQVKYGDC 1261
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE----RLRREREKAERYQ---ALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1262 ERQRQEAVEKIAKLQSELENVNSLLNESEgkntkssKDMLSLESHLQDTQELLQEETrqklaistrfrqmEEEQNSLREm 1341
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELE-------KRLEEIEQLLEELNKKIKDLG-------------EEEQLRVKE- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1342 leeeeeakknvekQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDD 1421
Cdd:TIGR02169 295 -------------KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1422 LLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELEtitDLKNELERtnkqLKA 1501
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA---DLNAAIAG----IEA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1502 EMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrdlQARDEQGEERR 1581
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR---ASEERVRGGRA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1582 KQLVKQ-----VHELEAEL--EDERRQRSQAVSAKKKleldLGELEVHIDAANKGRDEALKQ----------LKKLQVQF 1644
Cdd:TIGR02169 512 VEEVLKasiqgVHGTVAQLgsVGERYATAIEVAAGNR----LNNVVVEDDAVAKEAIELLKRrkagratflpLNKMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1645 KDMMRESEDLRLS--------------------RD----EAINSAKETEKKVK--TMEAD-------------------- 1678
Cdd:TIGR02169 588 RDLSILSEDGVIGfavdlvefdpkyepafkyvfGDtlvvEDIEAARRLMGKYRmvTLEGElfeksgamtggsraprggil 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1679 -AAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVD 1757
Cdd:TIGR02169 668 fSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1758 QLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELES------------------TIKSKYKSSLTALEAKVAQLEEQ 1819
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaelskleEEVSRIEARLREIEQKLNRLTLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1820 LDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELED 1899
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810
....*....|....*....
gi 768942001 1900 ANETQDTMNREVNILKSKL 1918
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKL 926
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
847-1713 |
9.43e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 847 KEDELSKVKEKQLQAEEMIKEFESKQQQlnaEKMALQEQLQAE----TELCAEAEEMRARLVNRKQE----LEEILHDME 918
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAE---DARKAEEARKAEdakrVEIARKAEDARKAEEARKAEdakkAEAARKAEE 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 919 SRLEEEEERVNQMLN-ERKKMQQNIADLEQQLDEEEAdrQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDR 997
Cdd:PTZ00121 1187 VRKAEELRKAEDARKaEAARKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 998 IAEFSSNL-SEEEEKSRSLQKLKNKHEAiitdleDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLA 1076
Cdd:PTZ00121 1265 FARRQAAIkAEEARKADELKKAEEKKKA------DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1077 NKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQ 1156
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1157 EL-RAKRETEvaQLRKAQEEENKMHESQIAELSKKhlqafnemneQLEQAKRNKLSVEKAKQALESEfnelqiELKTLGQ 1235
Cdd:PTZ00121 1419 KAdEAKKKAE--EKKKADEAKKKAEEAKKADEAKK----------KAEEAKKAEEAKKKAEEAKKAD------EAKKKAE 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1236 SKSDSEHRRKKAESqvqelQVKYGDCERQRQEAVEKIAKLQSELENVNSllNESEGKNTKSSKDMLSLESHLQDTQELLQ 1315
Cdd:PTZ00121 1481 EAKKADEAKKKAEE-----AKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1316 EETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREfDTVK 1395
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEK 1632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1396 LQLEEKEAAYEKLERTKTRLQQELDDLLVNQDglrQLVNNMERKQRKFDQMLAEEKtistqyaEERDKAEAEAREKETra 1475
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAA---EEAKKAEEDKKKAEEAKKAEE-------DEKKAAEALKKEAEE-- 1700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1476 ltlARELETITDLKNELERTNKQLKAEMEdlvsskdDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRL 1555
Cdd:PTZ00121 1701 ---AKKAEELKKKEAEEKKKAEELKKAEE-------ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1556 EVNMQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKklELDLGELEVHIDAANKGRDEAlk 1635
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSKNMQLEEA-- 1846
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1636 qlkkLQVQFKDMMRESEDLRLSRDEAiNSAKETEKKvktmeadaaqfQEDLATAERLKRQMQAERDELQDEINGNNTK 1713
Cdd:PTZ00121 1847 ----DAFEKHKFNKNNENGEDGNKEA-DFNKEKDLK-----------EDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1743 |
1.23e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 828 FTKVKPLLQVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAEtELCAEAEEmrARLVNRK 907
Cdd:PTZ00121 1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAE-EAKKKAED--ARKAEEA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 908 QELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMkalegnimvldDQNNKL 987
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKA-----------EDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 988 NKEKKLLEDRIAEfSSNLSEEEEKSRSLQKLKnkheaiitdlEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQ 1067
Cdd:PTZ00121 1203 EAARKAEEERKAE-EARKAEDAKKAEAVKKAE----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1068 IadlRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKfyrskngqRCKELEKELEAIKNKLDD 1147
Cdd:PTZ00121 1272 I---KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK--------KAEEAKKKADAAKKKAEE 1340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1148 T--LDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEfnE 1225
Cdd:PTZ00121 1341 AkkAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK--K 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1226 LQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKdmlsLES 1305
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK----AEE 1494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1306 HLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQisvlqgqlgdmKKKMDQevssLESAEESRK 1385
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE-----------KKKADE----LKKAEELKK 1559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1386 RLQ-REFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDglrqlvnnmERKQRKFDQMLAEEKtiSTQYAEERDKA 1464
Cdd:PTZ00121 1560 AEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE---------EEKKMKAEEAKKAEE--AKIKAEELKKA 1628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1465 EAEAREKETRALTLARELETITDLKNElERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDE 1544
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1545 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKqlvkqVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHID 1624
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK-----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1625 AANKGRDEalKQLKKLQVQFKDMMRESEDLRLSRDEA---INSAKETEKKVKTMEADAAQFQEDLATAerlkrqMQAERD 1701
Cdd:PTZ00121 1783 EELDEEDE--KRRMEVDKKIKDIFDNFANIIEGGKEGnlvINDSKEMEDSAIKEVADSKNMQLEEADA------FEKHKF 1854
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 768942001 1702 ELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSE 1743
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1180-1726 |
1.34e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 86.25 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1180 HESQIAELSKKhlqaFNEMNEQLEQAKRNKlsvEKAKQALEsEFNELQIELKTLgqsksdsehrrkkaESQVQELQVKYG 1259
Cdd:PRK02224 211 LESELAELDEE----IERYEEQREQARETR---DEADEVLE-EHEERREELETL--------------EAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1260 DCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHlQDTQELLQEETRQKLA-ISTRFRQMEEEQNSL 1338
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLEeCRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1339 REMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQE 1418
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1419 LDDLLVNqdgLRQLVNNMERKQRkfdqMLAEEKTIST-QYAEERDKAEAeAREKETRALTLARELETITDLKNELERTNK 1497
Cdd:PRK02224 428 EAELEAT---LRTARERVEEAEA----LLEAGKCPECgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1498 QLK--AEMEDLVSSKDDAGKNVHELERSKRAT----EQQLEEIKTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlQ 1571
Cdd:PRK02224 500 RAEdlVEAEDRIERLEERREDLEELIAERRETieekRERAEELRERAAELEAEAEEKREAA------------------A 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1572 ARDEQGEERRKQLvkqvheleAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKgRDEALKQLKKLQVQFKDMMRES 1651
Cdd:PRK02224 562 EAEEEAEEAREEV--------AELNSKLAELKERIESLERIRTLLAAIADAEDEIER-LREKREALAELNDERRERLAEK 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1652 EDLRLSRDEAINsaketEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEA 1726
Cdd:PRK02224 633 RERKRELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1421 |
3.27e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKmalqEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESR 920
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 921 LEEEEERVNQM------LNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLN---KEK 991
Cdd:PRK03918 268 IEELKKEIEELeekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 992 KLLEDRIAEFSSNLsEEEEKSRSLQKLKNKHEAIITDLEdrLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADL 1071
Cdd:PRK03918 348 KELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1072 RAQLankeEELQNALIR-------IEEEAAANMASQ--KKIKELEAQILELDEDLEREKfyrskngQRCKELEKELEAIK 1142
Cdd:PRK03918 425 KKAI----EELKKAKGKcpvcgreLTEEHRKELLEEytAELKRIEKELKEIEEKERKLR-------KELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1143 NKLddTLDTTAAQ-QELRAKRETEVAQLRKAQEEENKMHESQIAELsKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALES 1221
Cdd:PRK03918 494 ELI--KLKELAEQlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1222 EFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELEnvnsllnESEGKNTKSSKDML 1301
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD-------KAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1302 SLESHLQDTQELLQEETRQKlaISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKmDQEVSSLESAE 1381
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA-KKELEKLEKAL 720
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 768942001 1382 ESRKRLQREFDtvKLQLEEKEAAYEKLERTKTRLQQELDD 1421
Cdd:PRK03918 721 ERVEELREKVK--KYKALLKERALSKVGEIASEIFEELTE 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1050-1916 |
4.78e-16 |
|
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: 84.73 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1050 LEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEeaaanmaSQKKIKELEAQILELDEDLEREKFYRSKnGQ 1129
Cdd:TIGR02169 140 LQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEE-------VEENIERLDLIIDEKRQQLERLRREREK-AE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1130 RCKELEKELEAIKNKLddtldTTAAQQELRAKRETEVAQLRKAQEEENKMhESQIAELSKKhlqaFNEMNEQLEQ--AKR 1207
Cdd:TIGR02169 212 RYQALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEKL-TEEISELEKR----LEEIEQLLEElnKKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1208 NKLSVEKAKQaLESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLN 1287
Cdd:TIGR02169 282 KDLGEEEQLR-VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1288 ESEgkntkssKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMleeeeeakknvekqisvlQGQLGDMK 1367
Cdd:TIGR02169 361 ELK-------EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE------------------LDRLQEEL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1368 KKMDQEVSSLESAEESRKRLQREFDTVKLQLEEK-EAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQM 1446
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1447 LAEEKTISTqyaEERDKAEAEAREKETRALTLAreleTITDLKNELERTNKQLK----AEMEDLVSSKDDAGKNVHELER 1522
Cdd:TIGR02169 496 EAQARASEE---RVRGGRAVEEVLKASIQGVHG----TVAQLGSVGERYATAIEvaagNRLNNVVVEDDAVAKEAIELLK 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1523 SK---RATEQQLEEIKTQLEELEdelQATEDAKLRLEVNMQAMKAQFD-------------RDLQ-ARDEQGEERRKQLV 1585
Cdd:TIGR02169 569 RRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEaARRLMGKYRMVTLE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1586 KQVHELEAELEDERRQRSQAVSAKKKLELDLGELevhidaankgRDEalkqLKKLQVQFKDMMRESEDLRLSRDEAINSA 1665
Cdd:TIGR02169 646 GELFEKSGAMTGGSRAPRGGILFSRSEPAELQRL----------RER----LEGLKRELSSLQSELRRIENRLDELSQEL 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1666 KETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNntknsmlQDEKRRLEARITQLEEELEEEQLNSEMA 1745
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-------KSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1746 NDRNKRTtlQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSkykssltaLEAKVAQLEEQLDTEIK 1825
Cdd:TIGR02169 785 EARLSHS--RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE--------LQEQRIDLKEQIKSIEK 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1826 ERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQD 1905
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
890
....*....|.
gi 768942001 1906 TMNREVNILKS 1916
Cdd:TIGR02169 935 EIEDPKGEDEE 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1160-1910 |
4.99e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1160 AKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEfNELQIELKTLGQSKSD 1239
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE-DARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1240 SEHRRKKAESQVQELQVKYGDCER----QRQEAVEKIAKLQsELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQ 1315
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKaeaaRKAEEVRKAEELR-KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1316 EETRQKlaiSTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVlqgqlgdmKKKMDQEVSSLESAEESRKRLQ-REFDTV 1394
Cdd:PTZ00121 1233 EEAKKD---AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI--------KAEEARKADELKKAEEKKKADEaKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1395 KLQLEEKEAAYEKleRTKTRLQQELDDLLVNQDGLRQlvnNMERKQRKFDQMLAEEKtistqyaEERDKAEAEAREKETR 1474
Cdd:PTZ00121 1302 KKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAE-------AAADEAEAAEEKAEAA 1369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1475 ALTLARELETITDLKNELERTNKQlkaemEDLVSSKDDAGKNVHELERsKRATEQQLEEIKTQLEELEDELQATEDAKLR 1554
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1555 LEVNMQAMKAQFDRDLQARDEQGEERRKqlvkqVHELEAELEDERRqrsqAVSAKKKLEldlgELEVHIDAANKGRDEAL 1634
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKK-----ADEAKKKAEEAKK----ADEAKKKAE----EAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1635 K--QLKKLQVQfkdmmRESEDLRlsRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDElQDEINGNNT 1712
Cdd:PTZ00121 1511 KadEAKKAEEA-----KKADEAK--KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE-EDKNMALRK 1582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1713 KNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNkrttLQVDQLTAELSAERSAAQRlegARSQAERKNKELSLKLQ 1792
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK----IKAEELKKAEEEKKKVEQL---KKKEAEEKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1793 ELESTIKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQL 1872
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 768942001 1873 KRQLEEAE---EEVTRANAYRRKLQRELEDANETQDTMNRE 1910
Cdd:PTZ00121 1736 KKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
907-1660 |
5.94e-16 |
|
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: 84.40 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 907 KQELEEILHDMESRLEEEEERVNQM--LNERKK--MQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNimvLDD 982
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESneLHEKQKfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ---LQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 983 QNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELE------------KNRRKL 1050
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMStmhfrslgsaisKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1051 EGDSTDLHDQIADLQAQIADLRAQLANKEEEL-QNALIRIEEeaaanmasqkKIKELEAQILELDEDLEREKfyrskngQ 1129
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQ----------LISEHEVEITGLTEKASSAR-------S 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1130 RCKELEKELEAIKnklDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQleQAKRNK 1209
Cdd:pfam15921 293 QANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEA--RTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1210 LSVEKAK-----QALESEFNELQIEL------------KTLGQSKSDSEHRR----KKAESQVQELQVK------YGDCE 1262
Cdd:pfam15921 368 FSQESGNlddqlQKLLADLHKREKELslekeqnkrlwdRDTGNSITIDHLRRelddRNMEVQRLEALLKamksecQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1263 RQ------RQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAIS---TRFR---- 1329
Cdd:pfam15921 448 RQmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeiTKLRsrvd 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1330 -------QMEEEQNSLREMLEEEEEAKKNVEKQ---ISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLE 1399
Cdd:pfam15921 528 lklqelqHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1400 EKEAAYEKLERTKTRLQQELDDL------LVNQdGLRQLVNNMERKQRKfDQMLAEEKT-------ISTQYAEERDKAEA 1466
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLelekvkLVNA-GSERLRAVKDIKQER-DQLLNEVKTsrnelnsLSEDYEVLKRNFRN 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1467 EAREKETRALTLARELETItdlKNELERTNKQLKAE-------------MEDLVSSK------------------DDAGK 1515
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSA---QSELEQTRNTLKSMegsdghamkvamgMQKQITAKrgqidalqskiqfleeamTNANK 762
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1516 NVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR---------DLQARDEQGEERRK-QLV 1585
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKaslqfaecqDIIQRQEQESVRLKlQHT 842
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1586 KQVHELEA--------------ELEDERRQRSQAVSAKKKLELdlgeLEVHIDAANKGRDEALKQLKKLQVQFKDMMRES 1651
Cdd:pfam15921 843 LDVKELQGpgytsnssmkprllQPASFTRTHSNVPSSQSTASF----LSHHSRKTNALKEDPTRDLKQLLQELRSVINEE 918
|
....*....
gi 768942001 1652 EDLRLSRDE 1660
Cdd:pfam15921 919 PTVQLSKAE 927
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1102-1887 |
5.99e-16 |
|
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: 84.40 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1102 KIKELEAQILELDEDLEREKFYRSkngQRCKELEKELEAIKNKLDdtldttaAQQELRAKRETEVAQLRkaQEEENKMHE 1181
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLR---QSVIDLQTKLQEMQMERD-------AMADIRRRESQSQEDLR--NQLQNTVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1182 SQIAELSKKHLqaFNEMNEQLEQAKRNKLSVEKAKQALES---EFNELQ------------IELKTLGQSKSDSehrRKK 1246
Cdd:pfam15921 154 LEAAKCLKEDM--LEDSNTQIEQLRKMMLSHEGVLQEIRSilvDFEEASgkkiyehdsmstMHFRSLGSAISKI---LRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1247 AESQVQELQVKYGDCERQ----RQEAVEKIAKL-QSELENVNSLLNESEGKNTKSSKDMLSLESH---LQDTQELLQEET 1318
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQlealKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1319 RQKLAIStrFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKkkmdqevSSLESAEESRKRLQREFDTVKLQL 1398
Cdd:pfam15921 309 RNQNSMY--MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN-------SELTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1399 EEKEAAYEKLERtKTRLQQELDDLL--------VNQDGLRQLVNNMERKQRKFDQMLAEEKTiSTQYAEERDKAEAEARE 1470
Cdd:pfam15921 380 QKLLADLHKREK-ELSLEKEQNKRLwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKS-ECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1471 KEtraltlareLETITDLKNELERTNKQLKAEMEDLVSSKddagknvHELERSKRAteqqLEEIKTQLEELEDELQAT-- 1548
Cdd:pfam15921 458 ES---------LEKVSSLTAQLESTKEMLRKVVEELTAKK-------MTLESSERT----VSDLTASLQEKERAIEATna 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1549 EDAKLRLEVNMQAmkaqfdRDLQARDEQGEERRkqlvkqvhELEAELEDERRQRSQAvsaKKKLELDLGELEVHID-AAN 1627
Cdd:pfam15921 518 EITKLRSRVDLKL------QELQHLKNEGDHLR--------NVQTECEALKLQMAEK---DKVIEILRQQIENMTQlVGQ 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1628 KGRDEALKQLKKLQVQ--FKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEdlATAERLK--RQMQAERDEL 1703
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEkeINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN--AGSERLRavKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1704 QDEINGNNTKNSMLQDEKRRLEARItqleeeleeEQLNSEMANDRNKrTTLQVDQLTAELSAERSAAQRLEGARSQAERk 1783
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNF---------RNKSEEMETTTNK-LKMQLKSAQSELEQTRNTLKSMEGSDGHAMK- 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1784 nkeLSLKLQElesTIKSKyKSSLTALEAKVAQLEEQLDTEIKERQqatrMVRRTEKKMKELVLQVEDERrntEQYKDQAD 1863
Cdd:pfam15921 728 ---VAMGMQK---QITAK-RGQIDALQSKIQFLEEAMTNANKEKH----FLKEEKNKLSQELSTVATEK---NKMAGELE 793
|
810 820
....*....|....*....|....
gi 768942001 1864 KLNSRTRQLKRQLEEAEEEVTRAN 1887
Cdd:pfam15921 794 VLRSQERRLKEKVANMEVALDKAS 817
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1006-1921 |
1.34e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1006 SEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNA 1085
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1086 LI-RIEEEAAANMASQKKIKELEAQILELDEDLER-EKFYRSKNGQRCKELEKELEAIKnklddtLDTTAAQQELRAKRE 1163
Cdd:PTZ00121 1167 EEaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKaEAARKAEEERKAEEARKAEDAKK------AEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1164 tevaQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKL----SVEKAKQALESEFNELQIELKTLGQSKSD 1239
Cdd:PTZ00121 1241 ----EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkkaeEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1240 SEHRRKKAEsqvqELQVKYGDCERQRQEAVEKiaklqselenvnsllNESEGKNTKSSKDMLSLESHLQDTQELLQEETR 1319
Cdd:PTZ00121 1317 ADEAKKKAE----EAKKKADAAKKKAEEAKKA---------------AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1320 QKLAISTRfrQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVsslESAEESRKRLQ--REFDTVKLQ 1397
Cdd:PTZ00121 1378 KKADAAKK--KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK---KKADEAKKKAEeaKKADEAKKK 1452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1398 LEEKEAAYEKLERTK-TRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQmlAEEKTISTQYAEERDKAEAEAREKETRAL 1476
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1477 TLARELEtitdlknELERTNKQLKAEmEDLVSSKDDAGKNVHELERSKRATEQQLEEIKtQLEELEDELQATEDAKLRLE 1556
Cdd:PTZ00121 1531 EEAKKAD-------EAKKAEEKKKAD-ELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1557 VNMQAMKAQfdrdlQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVsaKKKLELDLGELEVHIDAANKGRDEALKQ 1636
Cdd:PTZ00121 1602 EEEKKMKAE-----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK--KKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1637 LKKlqvqfkDMMRESEDLRLSRDEAINSAKETEKKVKTMEADaaqfqedlaTAERLKRQMQAERDELQDEINGNNTKNSM 1716
Cdd:PTZ00121 1675 KKA------EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK---------EAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1717 LQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTlqvdqltAELSAERSAAQRLEGARSQAERKNKELslkLQELES 1796
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE-------KEAVIEEELDEEDEKRRMEVDKKIKDI---FDNFAN 1809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1797 TIKSKYKSSLTALEAKvaqleEQLDTEIKERQQATRMVRRTEKkmkelvlQVEDERRNTEQYKDQADKLNSRTRQLKRQL 1876
Cdd:PTZ00121 1810 IIEGGKEGNLVINDSK-----EMEDSAIKEVADSKNMQLEEAD-------AFEKHKFNKNNENGEDGNKEADFNKEKDLK 1877
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 768942001 1877 EEAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSKLRRD 1921
Cdd:PTZ00121 1878 EDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1360-1920 |
2.15e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1360 QGQLGDMKKKMDQEVSS-----LESAEESRKRLQREFDTVKlqlEEKEAAYEKLERTKTRL------QQELDDLLVNQDG 1428
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYE---EQREQARETRDEADEVLeeheerREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1429 LRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAreketrALTLArELETITDLKNELERTNKQLKAEMEDLVS 1508
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA------GLDDA-DAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1509 SKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqardEQGEERRKQLVKQV 1588
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV----------------------EDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1589 HELEAELEDerrqrsqavsakkkLELDLGELEVHIDAANKGRDEALKQLKKLQVQFK---DMMRESEDLR---------- 1655
Cdd:PRK02224 394 EELRERFGD--------------APVDLGNAEDFLEELREERDELREREAELEATLRtarERVEEAEALLeagkcpecgq 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1656 -LSRDEAINSAKETEKKVKTMEADAAQFQEDLAT-AERLKRQMQAErdELQDEIngnntknSMLQDEKRRLEARITQLEe 1733
Cdd:PRK02224 460 pVEGSPHVETIEEDRERVEELEAELEDLEEEVEEvEERLERAEDLV--EAEDRI-------ERLEERREDLEELIAERR- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1734 eleeeqlnSEMANDRNKRTTL--QVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSkykssLTALEA 1811
Cdd:PRK02224 530 --------ETIEEKRERAEELreRAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-----LERIRT 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1812 KVAQLEEQLDteikerqqatRMVRRTEKKmkELVLQVEDERRnteqykDQADKLNSRTRQLKRQ-----LEEAEEEVTRA 1886
Cdd:PRK02224 597 LLAAIADAED----------EIERLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERA 658
|
570 580 590
....*....|....*....|....*....|....
gi 768942001 1887 NAYRRKLQRELEDANETQDTMNREVNILKSKLRR 1920
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
837-1707 |
2.20e-15 |
|
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: 82.79 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 837 VTRQEEEMLAKEDELSKVKEKQLQaEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEIL-- 914
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQME-LKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLsk 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 915 -HDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKA-LEGNIMVLDDQNNKLNKEKK 992
Cdd:TIGR00606 264 iMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVdCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 993 LLEDRIAEFS--SNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDS-------TDLHDQIAD 1063
Cdd:TIGR00606 344 ELLVEQGRLQlqADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktaaqlcADLQSKERL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1064 LQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEA---QILELDEDL---EREKFYRSKNGQrCKELEKE 1137
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELrkaERELSKAEKNSL-TETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1138 LEAIKNKLDDTLDTTAAQQELRAKRETEvAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQL------EQAKRNKLS 1211
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1212 VEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGD-CERQRQEAveKIAKLQSELENVNSLLNESE 1290
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvCGSQDEES--DLERLKEEIEKSSKQRAMLA 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1291 GKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKM 1370
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1371 DQEVSSLESAEESRKRLQREFDTVKLQLEEKeaayEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEE 1450
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1451 KTISTQYAEERDKAEAEarEKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHElersKRATEQQ 1530
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQ 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1531 LEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERR------KQLVKQVHELEAELED-----ER 1599
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdkvndiKEKVKNIHGYMKDIENkiqdgKD 969
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1600 RQRSQAVSAKKKLELDLGELEVHIDAANKGR-------DEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKV 1672
Cdd:TIGR00606 970 DYLKQKETELNTVNAQLEECEKHQEKINEDMrlmrqdiDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
890 900 910
....*....|....*....|....*....|....*
gi 768942001 1673 KTMEADAAQFQEDLATAERLKRQMQAERDELQDEI 1707
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
830-1553 |
2.91e-15 |
|
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: 82.09 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 830 KVKPLLQVTRQEEEMLAKEDELS------KVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLqaeTELCAEAEEMRARL 903
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEVEitglteKASSARSQANSIQSQLEIIQEQARNQNSMYMRQL---SDLESTVSQLRSEL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 904 VNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKAL----EGNIMV 979
Cdd:pfam15921 334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdTGNSIT 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 980 LDdqnnKLNKEkklLEDRIAEfssnlseeeeksrsLQKLknkhEAIITDLedrlrKEEKQRQeLEKNRRKLEGDSTDLhD 1059
Cdd:pfam15921 414 ID----HLRRE---LDDRNME--------------VQRL----EALLKAM-----KSECQGQ-MERQMAAIQGKNESL-E 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1060 QIADLQAQIADLRAQLANKEEELQNALIRIEeeaaanmASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELE 1139
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLE-------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1140 AIKNKLDDTLDTtaaqqelrakrETEVAQLRKAQEEENKmhesqIAELSKKHLQafnEMNEQLEQAKRNKLSVEKAKQAL 1219
Cdd:pfam15921 535 HLKNEGDHLRNV-----------QTECEALKLQMAEKDK-----VIEILRQQIE---NMTQLVGQHGRTAGAMQVEKAQL 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1220 ESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQ---VKYGDCERQRQEAVEKIAKLQSELENvnsllnesEGKNTKS 1296
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKDIKQERDQLLN--------EVKTSRN 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1297 SKDMLS-----LESHLQDTQELLQEETRQ-KLAISTRFRQMEEEQNSLREMLEE---EEEAKKNVEKQISVLQGQLGDMK 1367
Cdd:pfam15921 668 ELNSLSedyevLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSdghAMKVAMGMQKQITAKRGQIDALQ 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1368 KKMDQEVSSLESAEESRKRLQREFDtvKLQLEEKEAAYEKlertkTRLQQELDDLLVNQDGLRQLVNNMErkqrkfdqmL 1447
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKN--KLSQELSTVATEK-----NKMAGELEVLRSQERRLKEKVANME---------V 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1448 AEEKTiSTQYAEERDKAEAEarEKETRALTLARELEtITDLKNELERTNKQLKAEM----------EDLVSSKDDAGKNV 1517
Cdd:pfam15921 812 ALDKA-SLQFAECQDIIQRQ--EQESVRLKLQHTLD-VKELQGPGYTSNSSMKPRLlqpasftrthSNVPSSQSTASFLS 887
|
730 740 750
....*....|....*....|....*....|....*.
gi 768942001 1518 HELERSKRATEQQLEEIKTQLEELEDELQATEDAKL 1553
Cdd:pfam15921 888 HHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQL 923
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
898-1535 |
8.17e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 898 EMRARLVNRKQELEEIL---HDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKvttdSKMKALE 974
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 975 GNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKheaiitdlEDRLRKEEKQRQELEKNRRKLEGDS 1054
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK--------AEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1055 TDLHDQIADLQAQIADlraqLANKEEELQNAlirieeeaaanmasQKKIKELEAQILELDEDLEREkfyrskngQRCKEL 1134
Cdd:PRK03918 317 SRLEEEINGIEERIKE----LEEKEERLEEL--------------KKKLKELEKRLEELEERHELY--------EEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1135 EKELEAIKNKLDD-TLDTTAAQQELRAKRETEVaqlrkaqEEENKMHESQIAELSKKhlqaFNEMNEQLEQAKRNKLSVE 1213
Cdd:PRK03918 371 KEELERLKKRLTGlTPEKLEKELEELEKAKEEI-------EEEISKITARIGELKKE----IKELKKAIEELKKAKGKCP 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1214 KAKQALESEFNELQIELKTLgqSKSDSEHRRKKAESQVQELqvkygdceRQRQEAVEKIAKLQSELENVNSLLNESegKN 1293
Cdd:PRK03918 440 VCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKL--------RKELRELEKVLKKESELIKLKELAEQL--KE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1294 TKSSKDMLSLESHLQDTQELlqEETRQKLA-ISTRFRQMEEEQNSLremlEEEEEAKKNVEKQISVLQGQLGDMKKKMDQ 1372
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEY--EKLKEKLIkLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1373 E-VSSLESAEESRKRLQ---REFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQmla 1448
Cdd:PRK03918 582 LgFESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1449 eektistqyaEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLvsskDDAGKNVHELERSKRATE 1528
Cdd:PRK03918 659 ----------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER----EKAKKELEKLEKALERVE 724
|
....*..
gi 768942001 1529 QQLEEIK 1535
Cdd:PRK03918 725 ELREKVK 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1026-1667 |
1.77e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1026 ITDLEDRLRKEEKQRQELEKNRRKLEgDSTDLHDQIADLQAQIADLRAQLANKE-EELQNALIRIEEEAAANMAsqkKIK 1104
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEA---ELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1105 ELEAQILELDEDLER-EKFYRSKNGQRCKELEKELEAIKNKLDDtldttaaqqelRAKRETEVAQLRKAQEEENKMHESQ 1183
Cdd:COG4913 313 RLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEE-----------RERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1184 IAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQE---------- 1253
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEalgldeaelp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1254 -----LQVKYGdcERQRQEAVEKI------------AKLQSELENVNSL------------LNESEGKNTKSSKDMLS-- 1302
Cdd:COG4913 462 fvgelIEVRPE--EERWRGAIERVlggfaltllvppEHYAAALRWVNRLhlrgrlvyervrTGLPDPERPRLDPDSLAgk 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1303 -----------LESHLQ--------DTQELLQEETRqklAIsTRfrqmeeeqnslremleeeeeakknvekqisvlQGQL 1363
Cdd:COG4913 540 ldfkphpfrawLEAELGrrfdyvcvDSPEELRRHPR---AI-TR--------------------------------AGQV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1364 ---GDMKKKMDqevsslesaeesRKRLQRE----FDTVKlQLEEKEAAYEKLERTKTRLQQELDDllvnqdgLRQLVNNM 1436
Cdd:COG4913 584 kgnGTRHEKDD------------RRRIRSRyvlgFDNRA-KLAALEAELAELEEELAEAEERLEA-------LEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1437 ERKQRKFDQMlaeektistqyaeerdkaeAEAREKETRALTLARELETITDLKNELERTN---KQLKAEMEDLVSSKDDA 1513
Cdd:COG4913 644 QERREALQRL-------------------AEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEEL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1514 GKNVHELERSKRATEQQLEEIKTQLEELEDELQ-ATEDAKLRLEVNMQAMKAQFDRDLQARD--EQGEERRKQLVKQVHE 1590
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALGDAVERElrENLEERIDALRARLNR 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1591 LEAELEDERRQrsqavsAKKKLELDLGELEVHIDAANKGRDEaLKQLK-----KLQVQFKDMMRESEDLRLSR-----DE 1660
Cdd:COG4913 785 AEEELERAMRA------FNREWPAETADLDADLESLPEYLAL-LDRLEedglpEYEERFKELLNENSIEFVADllsklRR 857
|
....*..
gi 768942001 1661 AINSAKE 1667
Cdd:COG4913 858 AIREIKE 864
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
842-1299 |
2.76e-14 |
|
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: 78.52 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 842 EEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQ--------EQLQAETELCA-EAEEMRARLVNRK-QELE 911
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQknidkiknKLLKLELLLSNlKKKIQKNKSLESQiSELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 912 EILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEK 991
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 992 KllEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADL 1071
Cdd:TIGR04523 305 E--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1072 RAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDT 1151
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1152 TAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKkhlqaFNEMNEQLEQA----KRNKLSVEKAKQALESEFNELQ 1227
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK-----LNEEKKELEEKvkdlTKKISSLKEKIEKLESEKKEKE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1228 IELKTLGQS--KSDSEHRRKKAESQVQELQVK-------YGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSK 1298
Cdd:TIGR04523 538 SKISDLEDElnKDDFELKKENLEKEIDEKNKEieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
.
gi 768942001 1299 D 1299
Cdd:TIGR04523 618 E 618
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
929-1604 |
8.02e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 929 NQMLnERKKMQQNIADLEQQLDE-----EEADRQKlqmEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSS 1003
Cdd:COG4913 215 EYML-EEPDTFEAADALVEHFDDlerahEALEDAR---EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1004 NLSEEEEksRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDstdlhdQIADLQAQIADLRAQLANKE---E 1080
Cdd:COG4913 291 ELLEAEL--EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERErrrA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1081 ELQNALIRIEEEAAANMAS----QKKIKELEAQILELDEDLEREkfyRSKNGQRCKELEKELEAIKNKLddtldttaaqQ 1156
Cdd:COG4913 363 RLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEI----------A 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1157 ELRAKRET---EVAQLRKAQEEENKMHESQ---IAEL---------------------------SKKHLQAFNEMNEQLE 1203
Cdd:COG4913 430 SLERRKSNipaRLLALRDALAEALGLDEAElpfVGELievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1204 QAKR------------------------NKLSVE--KAKQALESEFNELQI--------ELKTL-------GQSKSDSEH 1242
Cdd:COG4913 510 LRGRlvyervrtglpdperprldpdslaGKLDFKphPFRAWLEAELGRRFDyvcvdspeELRRHpraitraGQVKGNGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1243 RRKKAESQVQELQVkYGdcerqrQEAVEKIAKLQSELENVNSLLNEsegkntksskdmlsLESHLQDTQELLQEETRQKL 1322
Cdd:COG4913 590 HEKDDRRRIRSRYV-LG------FDNRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1323 AISTRFRQMEEEQNslremleeeeeakknvekqISVLQGQLGDMkkkmDQEVSSLESAEESRKRLQREFDTVKLQLEEKE 1402
Cdd:COG4913 649 ALQRLAEYSWDEID-------------------VASAEREIAEL----EAELERLDASSDDLAALEEQLEELEAELEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1403 AAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRK-----FDQMLAE------EKTISTQYAEERDKAEAEAREK 1471
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAalgdavERELRENLEERIDALRARLNRA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1472 ETR---------------ALTLARELETITDLKNELER--TNK--QLKAEMEDLVSSkddagKNVHELERSKRATEQQLE 1532
Cdd:COG4913 786 EEEleramrafnrewpaeTADLDADLESLPEYLALLDRleEDGlpEYEERFKELLNE-----NSIEFVADLLSKLRRAIR 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1533 EIKTQLEELEDELQATE---DAKLRLEVN--------------MQAMKAQFDRDLQARDEQgEERRKQLVKQVheLEAEL 1595
Cdd:COG4913 861 EIKERIDPLNDSLKRIPfgpGRYLRLEARprpdpevrefrqelRAVTSGASLFDEELSEAR-FAALKRLIERL--RSEEE 937
|
....*....
gi 768942001 1596 EDERRQRSQ 1604
Cdd:COG4913 938 ESDRRWRAR 946
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1004-1613 |
1.66e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1004 NLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEkqrqELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQ 1083
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1084 naliRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELE---KELEAIKNKLDDTLdttaaqqELRA 1160
Cdd:PRK03918 232 ----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYI-------KLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1161 KRETEVAQLRKAQEEENKMhESQIAELSKKhLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKsds 1240
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRL-EEEINGIEER-IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE--- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1241 EHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNE-----SEGKNTKSSKDMLSLESHLQDTQELLQ 1315
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaiEELKKAKGKCPVCGRELTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1316 EETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISvlqgqlgdMKKKMDQevssLESAEESRKRLQREfdtvk 1395
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--------LKELAEQ----LKELEEKLKKYNLE----- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1396 lQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKetra 1475
Cdd:PRK03918 519 -ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER---- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1476 ltlARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERskraTEQQLEEIKTQLEEL-----EDELQATED 1550
Cdd:PRK03918 594 ---LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKELEELekkysEEEYEELRE 666
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1551 AKLRLEVNMQAMKAQFdrdlqardEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLE 1613
Cdd:PRK03918 667 EYLELSRELAGLRAEL--------EELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
832-1422 |
1.91e-13 |
|
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: 76.16 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 832 KPLLQVTRQEEEMLAKEDELSKVKEK--------------------QLQAEEMIKEFESKQQQLNAEKMALQEQLQAETE 891
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERinrarkaaplaahikavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 892 LcaEAEEMRARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTD---S 968
Cdd:TIGR00618 340 I--EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtS 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 969 KMKALEGNIMVLDDQNNKLNKEKKLLEDRIA-EFSSNLSEEEEKSRSLQKLKNKHEAI-----ITDLEDRLRKEEKQR-Q 1041
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITcTAQCEKLEKIHLQESAQSLKEREQQLqtkeqIHLQETRKKAVVLARlL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1042 ELEKNRRKLEGDSTDLHDQIADLQAQIADLR--AQLANKEEELQNALIRIEEEAaanMASQKKIKELEAQILELDEDLer 1119
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQL---TSERKQRASLKEQMQEIQQSF-- 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1120 ekfyrSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELR-----------AKRETEVAQLRKAQEEENKMHESQIAELS 1188
Cdd:TIGR00618 573 -----SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlaceqhallRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1189 KKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHrrkkAESQVQELQVKYGDCERQRQEA 1268
Cdd:TIGR00618 648 LHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ----CQTLLRELETHIEEYDREFNEI 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1269 VEKIAKLQSELENVNSLLNESEGKNTKSSKDML--SLESHLQDTQELL------QEETRQKLAISTRFRQMEEEQNSLRE 1340
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQARTVLkaRTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKT 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1341 MLEEEEEAKKNVEKQISVLQGQLGdmkkkmdQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELD 1420
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQCETLV-------QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
..
gi 768942001 1421 DL 1422
Cdd:TIGR00618 877 KL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1373-1918 |
2.42e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1373 EVSSLESAEESRKRLQREFdtvkLQLEEKEAAYEKLERTKT---RLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAE 1449
Cdd:PRK03918 136 EIDAILESDESREKVVRQI----LGLDDYENAYKNLGEVIKeikRRIERLEKFIKRTENIEELIKEKEKELEEVLREINE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1450 EKTISTQYAEERDKAEAEAREKETRALTLA---RELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRA 1526
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEeleKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1527 TEqQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR--DLQARDEQGEERRKQLVKQVHELEA---ELEDERRQ 1601
Cdd:PRK03918 292 AE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELEErheLYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1602 RSQAVSAKKKLE-LDLGELEVHIDAANKGRDEALKQLKKLqvqfKDMMRESEDLRLSRDEAINSAKETEKK--------- 1671
Cdd:PRK03918 371 KEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKI----TARIGELKKEIKELKKAIEELKKAKGKcpvcgrelt 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1672 -------VKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNT--KNSMLQDEKRRLEARiTQLEEELEEEQLNS 1742
Cdd:PRK03918 447 eehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEK-LKKYNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1743 EMANDRNKRTTLQVDQLTAELSAERsaAQRLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKVAQLEEQLDt 1822
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEK--LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN- 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1823 EIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQL-----EEAEEEVTRANAYRRKLQREL 1897
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAEL 682
|
570 580
....*....|....*....|.
gi 768942001 1898 EDANETQDTMNREVNILKSKL 1918
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEEL 703
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1009-1731 |
3.37e-13 |
|
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: 75.39 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1009 EEKSRSLQKLKNKHEAIITDLEDRLrKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLAnkEEELQNALIR 1088
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREAL-QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA--VLEETQERIN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1089 IEEEAAANMASQKKIKELEAQILELDEDLErekfyrSKNGQRCKELEKELEAIKNKLD----DTLDTTAAQQELRAKRET 1164
Cdd:TIGR00618 288 RARKAAPLAAHIKAVTQIEQQAQRIHTELQ------SKMRSRAKLLMKRAAHVKQQSSieeqRRLLQTLHSQEIHIRDAH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1165 EVAQLRKAQEEENKMHESQIaelskKHLQAFNEMNEQLEQAKRNKLSVEKAKQA----LESEFNELQIEL----KTLGQS 1236
Cdd:TIGR00618 362 EVATSIREISCQQHTLTQHI-----HTLQQQKTTLTQKLQSLCKELDILQREQAtidtRTSAFRDLQGQLahakKQQELQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1237 KSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQsELEN-----------VNSLLNESEGKNTKSSKDMLSLES 1305
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQihlqetrkkavVLARLLELQEEPCPLCGSCIHPNP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1306 HLQDTQELlQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGqlgDMKKKMDQEVSSLESAEESRK 1385
Cdd:TIGR00618 516 ARQDIDNP-GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQN 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1386 RLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDglrqlvnnmerkQRKFDQMLAEEKTISTQYAEERdkae 1465
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH------------LQQCSQELALKLTALHALQLTL---- 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1466 aeAREKETRALTLARELEtitdlknelERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDEL 1545
Cdd:TIGR00618 656 --TQERVREHALSIRVLP---------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1546 QATEDAKlrlevnmqamkaqfdRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDA 1625
Cdd:TIGR00618 725 NASSSLG---------------SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1626 ANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEainsaketekkvkTMEADAAQFQEDLAtaERLKRQMQAERDELQD 1705
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE-------------TLVQEEEQFLSRLE--EKSATLGEITHQLLKY 854
|
730 740
....*....|....*....|....*.
gi 768942001 1706 EingnntKNSMLQDEKRRLEARITQL 1731
Cdd:TIGR00618 855 E------ECSKQLAQLTQEQAKIIQL 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1355-1923 |
4.74e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1355 QISVLQgQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAayEKLERTKTRLQQELDDLLVNQDGLRQLVN 1434
Cdd:COG4913 250 QIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1435 NMERKQRKFDQMLAEektistQYAEERDKAEAEAREKETRALTLARELETItDLKNELERtnKQLKAEMEDLVSSKDDAG 1514
Cdd:COG4913 327 ELEAQIRGNGGDRLE------QLEREIERLERELEERERRRARLEALLAAL-GLPLPASA--EEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1515 KNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ-----------GEERRKQ 1583
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1584 --------------LVKQVHE--------------------LEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKG 1629
Cdd:COG4913 478 gaiervlggfaltlLVPPEHYaaalrwvnrlhlrgrlvyerVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGR 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1630 R--------DEALKQLKK---LQVQFKDM--MRESEDLRLSRDEAI--NSAKEtekKVKTMEADAAQFQEDLATAERLKR 1694
Cdd:COG4913 558 RfdyvcvdsPEELRRHPRaitRAGQVKGNgtRHEKDDRRRIRSRYVlgFDNRA---KLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1695 QMQAERDELQdeingnntknsmlqdEKRRLEARITqleeeleeeqlNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLE 1774
Cdd:COG4913 635 ALEAELDALQ---------------ERREALQRLA-----------EYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1775 GARSQAERKNKElslkLQELESTIKsKYKSSLTALEAKVAQLEEQLDteikerQQATRMVRRTEKKMKELVLQVEDERRN 1854
Cdd:COG4913 689 ALEEQLEELEAE----LEELEEELD-ELKGEIGRLEKELEQAEEELD------ELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1855 ---TEQYKDQADKLNSRTRQLKRQLEEAEEEVTRA-NAYRRKLQRELEDANETQDTMNREVNILKSKLRRDLP 1923
Cdd:COG4913 758 algDAVERELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLP 830
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
836-1652 |
6.40e-13 |
|
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: 74.70 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEM----------IKEFESKQQQLNAEKMALQEQL----QAETELCAEAEEMRA 901
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNlskimkldneIKALKSRKKQMEKDNSELELKMekvfQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 902 RLVnrkQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLD--EEEADRQKLQMEKVTTDSKMKALEGNIMV 979
Cdd:TIGR00606 312 RTV---REKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSLATRLELDGFERGPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 980 LDDQNN-------KLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEG 1052
Cdd:TIGR00606 389 ERQIKNfhtlvieRQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1053 DSTDLHDQIADLQAQIADLRAQLAN--------KEEELQNA---LIRIEEEAAANMASQKKIKELEAQILELDED-LERE 1120
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNsltetlkkEVKSLQNEkadLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDkMDKD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1121 KFYRSKNGQRCKELEKELEAIKNK--LDDTLDTTAAQ----QELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQA 1194
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGYFPNKkqLEDWLHSKSKEinqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1195 FN------------EMNEQLEQAKRNKLSVEKAKQALESEFNELQIE--------------LKTLGQSKSDSEHRRKKAE 1248
Cdd:TIGR00606 629 FDvcgsqdeesdleRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqtEAELQEFISDLQSKLRLAP 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1249 SQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQeetrqklAISTRF 1328
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-------TIMPEE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1329 RQMEEEQNSLREmleeeeeakknvekqISVLQGQLGDMKKKMDQEVSSLESAEESR---------KRLQREFDTVKLQLE 1399
Cdd:TIGR00606 782 ESAKVCLTDVTI---------------MERFQMELKDVERKIAQQAAKLQGSDLDRtvqqvnqekQEKQHELDTVVSKIE 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1400 EKEAAYEKLERTKTRLQQELDDLLVNQdglRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLA 1479
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEK---LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1480 RELETItdlkNELERTNKQLKAEMEDLVSSKDDAGKNVHELERS-KRATEQQLEEIKTQLEELEDELQATEDAKLRLEVN 1558
Cdd:TIGR00606 924 EKEELI----SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1559 MQAMKAQFD-RDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDlgELEVHIDAANKGRDEALKQL 1637
Cdd:TIGR00606 1000 MRLMRQDIDtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQ--KLEENIDLIKRNHVLALGRQ 1077
|
890
....*....|....*...
gi 768942001 1638 KKLQVQ---FKDMMRESE 1652
Cdd:TIGR00606 1078 KGYEKEikhFKKELREPQ 1095
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1174-1806 |
1.03e-12 |
|
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: 73.72 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1174 EEENKMHESQIAELSKKHlqaFNEMNEQLEQAKRNKlSVEKAKQALESEFNELQIELKT----LGQSKSDSEHRRKKAES 1249
Cdd:pfam12128 247 QQEFNTLESAELRLSHLH---FGYKSDETLIASRQE-ERQETSAELNQLLRTLDDQWKEkrdeLNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1250 QVQELQVKYG-----DCERQRQEAvEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESH--LQDTQELLQEETRQKL 1322
Cdd:pfam12128 323 ELEALEDQHGafldaDIETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1323 AISTRFRQMEEEQNSLremleeeeeakknvEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKE 1402
Cdd:pfam12128 402 IREARDRQLAVAEDDL--------------QALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1403 AAYEKLERTKTRLQQELDDLLVNQDGLRQLvnnmerkQRKFDQMLAEEKTIStQYAEERDKAEAEARE------------ 1470
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQA-------RKRRDQASEALRQAS-RRLEERQSALDELELqlfpqagtllhf 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1471 --------KETRALTLARELETITDLKNE------------------LERTNKQLKAEMEDLVSSKDDAGKNVHELERSK 1524
Cdd:pfam12128 540 lrkeapdwEQSIGKVISPELLHRTDLDPEvwdgsvggelnlygvkldLKRIDVPEWAASEEELRERLDKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1525 -RATEQQLEEIKTQLE----ELEDELQATEDAKL---RLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQV----HELE 1592
Cdd:pfam12128 620 qAAAEEQLVQANGELEkasrEETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqldKKHQ 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1593 AELEDERRQRSQAVSAKKK--------LELDLGELEVHIDAANKGRDEALKQLKklqvqfKDMMRESEDLRLSRDEAINS 1664
Cdd:pfam12128 700 AWLEEQKEQKREARTEKQAywqvvegaLDAQLALLKAAIAARRSGAKAELKALE------TWYKRDLASLGVDPDVIAKL 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1665 AKETEKKVKTMEaDAAQFQEDLATAER-LKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSE 1743
Cdd:pfam12128 774 KREIRTLERKIE-RIAVRRQEVLRYFDwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE 852
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1744 MANDR------------NKRTTLQVDQLTAElsAERSAAQRLEgARSQAERKNKELSLKLQE----LESTIKSKYKSSL 1806
Cdd:pfam12128 853 KQQVRlsenlrglrcemSKLATLKEDANSEQ--AQGSIGERLA-QLEDLKLKRDYLSESVKKyvehFKNVIADHSGSGL 928
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1467-1920 |
1.46e-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: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1467 EAREKETRALTLARELETITDLKNELERTNKQLKA--EMEDLVSSKDDAGKNVHELERSKRAT-----EQQLEEIKTQLE 1539
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1540 ELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLEL----D 1615
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLplpaS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1616 LGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKR- 1694
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1695 ---------QMQAERDELQDEING--NNTKNSMLQDEK-----------RRLEARITQLEEELEEEQLnsemandrnKRT 1752
Cdd:COG4913 459 elpfvgeliEVRPEEERWRGAIERvlGGFALTLLVPPEhyaaalrwvnrLHLRGRLVYERVRTGLPDP---------ERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1753 TLQVDQLTAELSAERSAA-----QRLEG------ARSQAERKNKELSLKLQEL------------ESTIKSKY------K 1803
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPFrawleAELGRrfdyvcVDSPEELRRHPRAITRAGQvkgngtrhekddRRRIRSRYvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1804 SSLTALEAKVAQLEEQLDT------EIKERQQATRMVRRTEKKMKEL------VLQVEDERRNTEQYKDQADKLNSRTRQ 1871
Cdd:COG4913 610 AKLAALEAELAELEEELAEaeerleALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAA 689
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 768942001 1872 LKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSKLRR 1920
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1152-1920 |
1.75e-12 |
|
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: 72.84 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1152 TAAQQELRAKRETEVAQLRKAQEEENKMH-ESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIEl 1230
Cdd:pfam15921 47 TFTQIPIFPKYEVELDSPRKIIAYPGKEHiERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQME- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1231 ktlgqskSDSEHRRKKAESQVQElqvkygDCERQRQEAVEKIAKLQSELENvnsLLNESEGKNTKSSKDMLSLESHLQDT 1310
Cdd:pfam15921 126 -------RDAMADIRRRESQSQE------DLRNQLQNTVHELEAAKCLKED---MLEDSNTQIEQLRKMMLSHEGVLQEI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1311 QELL---QEETRQKLaistrFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMdqEVSSLESAEESRKRL 1387
Cdd:pfam15921 190 RSILvdfEEASGKKI-----YEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQL--EALKSESQNKIELLL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1388 QREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLlvnQDGLRQLVNNMERKQRKFDQMLAE-EKTISTQYAEERDKA-- 1464
Cdd:pfam15921 263 QQHQDRIEQLISEHEVEITGLTEKASSARSQANSI---QSQLEIIQEQARNQNSMYMRQLSDlESTVSQLRSELREAKrm 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1465 -EAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVH-ELERSKRATEQQLEEIKTqLEELE 1542
Cdd:pfam15921 340 yEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlEKEQNKRLWDRDTGNSIT-IDHLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1543 DELQATEDAKLRLEVNMQAMKA----QFDRDL---QARDE----------QGEERRKQLVKQVHELEAE---LEDERRQR 1602
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSecqgQMERQMaaiQGKNEslekvssltaQLESTKEMLRKVVEELTAKkmtLESSERTV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1603 SQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQ---FKDMMRESEDLRLSrdeainsAKETEKKVKTMEADA 1679
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQ-------MAEKDKVIEILRQQI 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1680 AQFQEDLATAERLKRQMQAERDELQDEINGNN---TKNSMLQDEK----RRLEARITqleeeleeeqlnsemanDRNKRT 1752
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlelQEFKILKDKKdakiRELEARVS-----------------DLELEK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1753 TLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSlKLQELESTIKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATR 1832
Cdd:pfam15921 635 VKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN-SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1833 MVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREVN 1912
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE 793
|
....*...
gi 768942001 1913 ILKSKLRR 1920
Cdd:pfam15921 794 VLRSQERR 801
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1524 |
2.14e-12 |
|
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: 72.45 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 862 EEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQ-----------ELEEILHDMESRLEEEEERVNQ 930
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEkqvsllliqitEKENKMKDLTFLLEESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 931 MLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKlledriaefssNLSEEEE 1010
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE-----------AQMEELN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1011 KSRSLQKL-KNKHEAIITDLEDRLRKEEkqrQELEKNRRKLEGDSTDLHDQIADLQaqiaDLRAQLANKEEELQnaliri 1089
Cdd:pfam05483 342 KAKAAHSFvVTEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEVELE------ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1090 eeeaaanmasqkkikELEaQILELDEDLEREKfyrskngqrcKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQL 1169
Cdd:pfam05483 409 ---------------ELK-KILAEDEKLLDEK----------KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1170 RKAQEEENKMHESQIAELSKKHLQafnemNEQLeQAKRNKLSVEKAKqaLESEFNELQIELKTLGQSKSDSEHRRKKAES 1249
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLK-----NIEL-TAHCDKLLLENKE--LTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1250 QVQELQVKygdcERQRQEAVEKIAK-LQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRF 1328
Cdd:pfam05483 535 QIENLEEK----EMNLRDELESVREeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1329 RQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFdtvklqLEEKEAAYEKL 1408
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL------LEEVEKAKAIA 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1409 ERTkTRLQQELDdlLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYaeerdkaeaEAREKETRALTLARELEtITDL 1488
Cdd:pfam05483 685 DEA-VKLQKEID--KRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY---------KNKEQEQSSAKAALEIE-LSNI 751
|
650 660 670
....*....|....*....|....*....|....*.
gi 768942001 1489 KNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSK 1524
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
840-1076 |
3.15e-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: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 840 QEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMES 919
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 920 RLEEEEERVNQMLNERKKMQQN--IADLEQQLDEEEADRQKLQMEKVTtdskmKALEGNIMVLDDQNNKLNKEKKLLEDR 997
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQppLALLLSPEDFLDAVRRLQYLKYLA-----PARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 998 IAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEgdstdlhDQIADLQAQIADLRAQLA 1076
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
837-1279 |
3.44e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 837 VTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCA----EAEEMRARLVNRKQELEE 912
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGltpeKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 913 ILHDMESRLEEEEERVNQM---LNERKKMQQNIADLEQQLDEEEadrQKLQMEKVTtdSKMKALEGNIMVLDDQNNKLNK 989
Cdd:PRK03918 406 EISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGRELTEEH---RKELLEEYT--AELKRIEKELKEIEEKERKLRK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 990 EKKLLEDRIAEfSSNLSEEEEKSRSLQKLKNKHEAIitDLEDrLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIA 1069
Cdd:PRK03918 481 ELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKY--NLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1070 DLRA---QLANKEEELQNALIRIEEEAAanmasqKKIKELEAQILELdedlerEKFYRSKNgqRCKELEKELEAIKNKLD 1146
Cdd:PRK03918 557 KLAElekKLDELEEELAELLKELEELGF------ESVEELEERLKEL------EPFYNEYL--ELKDAEKELEREEKELK 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1147 DTLDTTAAQQELRAKRETEVAQLRKAQEE-ENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALEsefnE 1225
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE----K 698
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1226 LQIELKTLGQSKSDSEhRRKKAESQVQELQVKYGDCERQ-RQEAVEKIAKLQSEL 1279
Cdd:PRK03918 699 LKEELEEREKAKKELE-KLEKALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
838-1437 |
4.20e-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: 71.59 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 838 TRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDM 917
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 918 ESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDR 997
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 998 IAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDST---DLHDQIADLQAQIADLRAQ 1074
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLNNQ 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1075 lanKEEELqnalirieeeaaanmasqkkIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAA 1154
Cdd:TIGR04523 304 ---KEQDW--------------------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1155 QQELRAKRETEVAQLRKAQE---EENKMHESQIAELSKKHLQA---FNEMNEQLEQAKRNKLSVEKAKQALESEFNELQI 1228
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQeklNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1229 ELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQ 1308
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1309 DTQELLQEETRQKLAISTRFRQMEEEQNSLremleEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQ 1388
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 768942001 1389 REFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNME 1437
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
939-1170 |
4.94e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.20 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 939 QQNIADLEQQLDEEEADRQKLQMEKvttdskmkalegNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKL 1018
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKN------------GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1019 KNKHEAIITDLED--RLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLankEEELQNALIRIEEEAAan 1096
Cdd:COG3206 249 LGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELE-- 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1097 mASQKKIKELEAQILELDEDLEREkfyrSKNGQRCKELEKELEAIKNKLDDTLdttAAQQELRAKRETEVAQLR 1170
Cdd:COG3206 324 -ALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1025-1920 |
6.97e-12 |
|
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: 71.23 E-value: 6.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1025 IITDLEDRLRKEEKQRQELEKNRRKlegdSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRieeeaaanmasQKKIK 1104
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEK----ACEIRDQITSKEAQLESSREIVKSYENELDPLKNR-----------LKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1105 ELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLD--------TTAAQQELRAKRETEVAQLRKAQEEE 1176
Cdd:TIGR00606 259 HNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrTVREKERELVDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1177 NKMHESQIAELSKKHLQA---------------FNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSE 1241
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQAdrhqehirardsliqSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1242 HRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGkntkSSKDMLSLEshlqdtQELLQEETRQK 1321
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG----SSDRILELD------QELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1322 LAistrfrqmeeEQNSLremleeeEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQrefdtvkLQLEEK 1401
Cdd:TIGR00606 489 KA----------EKNSL-------TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME-------MLTKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1402 EAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMlaeektistqyaeerdkaeaearekETRALTLARE 1481
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT-------------------------RDRLAKLNKE 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1482 LETITDLKNELertNKQLKAEMEDLVSSKDdagkNVHELERSKrATEQQLEEIKTQLEELEDELQ--ATEDAKLRLEVNM 1559
Cdd:TIGR00606 600 LASLEQNKNHI---NNELESKEEQLSSYED----KLFDVCGSQ-DEESDLERLKEEIEKSSKQRAmlAGATAVYSQFITQ 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1560 QAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAK-KKLELDLGELEVHIDAANKGRDEALKQLK 1638
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKeKRRDEMLGLAPGRQSIIDLKEKEIPELRN 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1639 KLQVQFKDMMRESEDLRLSRD--EAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAErdelQDEINGNNTknsm 1716
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETllGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK----LQGSDLDRT---- 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1717 LQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTlQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELES 1796
Cdd:TIGR00606 824 VQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1797 TIKSKyKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQY-----KDQADKLNSRTRQ 1871
Cdd:TIGR00606 903 EIKDA-KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkDDYLKQKETELNT 981
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 768942001 1872 LKRQLEEAEEevtranaYRRKLQRELEDANETQDTMNREVNILKSKLRR 1920
Cdd:TIGR00606 982 VNAQLEECEK-------HQEKINEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
869-1637 |
7.65e-12 |
|
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: 70.77 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 869 ESKQQQLNAEKMALQEQLQAET-----ELCAEAEEMRARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIA 943
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEfakkkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 944 DLEQQLDEEEAdRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLedRIAEFSSNLSEEEEKSrslqklknkhE 1023
Cdd:TIGR00618 244 YLTQKREAQEE-QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQA----------Q 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1024 AIITDLEDRLRKEEKQRQEleknRRKLEGDSTDLHDQIADLQaqiadlraQLANKEEELQNAliriEEEAAANMASQKKI 1103
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMK----RAAHVKQQSSIEEQRRLLQ--------TLHSQEIHIRDA----HEVATSIREISCQQ 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1104 KELEAQILELDEDLEREKfyrSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRK-AQEEENKMHES 1182
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLT---QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYaELCAAAITCTA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1183 QIAELSKKHL----QAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRkkaesqvQELQVKY 1258
Cdd:TIGR00618 452 QCEKLEKIHLqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR-------QDIDNPG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1259 GDCERQrQEAVEKIAKLQSELENVNSLLnESEGKNTKSSKDMLSLESHlqDTQELLQEETRQKLAISTRFRQMEEEQNSL 1338
Cdd:TIGR00618 525 PLTRRM-QRGEQTYAQLETSEEDVYHQL-TSERKQRASLKEQMQEIQQ--SFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1339 REMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQE 1418
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1419 LDDLLvnQDGLRQLVNNMERKQRKfDQMLAEEKTISTQYAEERDKAEAEArekETRALTLARELETITDLKNELERTNK- 1497
Cdd:TIGR00618 681 ALQKM--QSEKEQLTYWKEMLAQC-QTLLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDALNQSLKELMHQARt 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1498 QLKAEMEDlvsskddaGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQG 1577
Cdd:TIGR00618 755 VLKARTEA--------HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1578 EERRKQLVKQVHELEA----------ELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQL 1637
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSAtlgeithqllKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKF 896
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1355-1917 |
1.21e-11 |
|
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: 70.05 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1355 QISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTK--------------TRLQQELD 1420
Cdd:TIGR04523 76 KIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKkenkknidkflteiKKKEKELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1421 DLLVNQDGLRQLVNNMERKQRKF-DQMLAEEKTIstqyaeerDKAEAEAREKETRALTLARELETITDLK---NELERTN 1496
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1497 KQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFdrdLQARDEQ 1576
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI---SDLNNQK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1577 GEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRL 1656
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1657 SRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELE 1736
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1737 EEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKsKYKSSLTALEAKVAQL 1816
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1817 EEQLDT-------------------EIKERQQATRMVRRTEKKMKELVLQVEDERRNTeqyKDQADKLNSRTRQLKRQLE 1877
Cdd:TIGR04523 544 EDELNKddfelkkenlekeideknkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL---IKEIEEKEKKISSLEKELE 620
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 768942001 1878 EAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSK 1917
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
798-1451 |
1.22e-11 |
|
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: 70.46 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 798 KRQQQLTAMKVIQRNCAAY---LKLRNWQWWRLFTKVKPLLQVTRQEEEMLAKEDELSKVKEKQLQ-AEEMIKEFESKQQ 873
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCADLqskERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqLEGSSDRILELDQ 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 874 QLN--------AEKMALQEQLQAETE-LCAEAEEMRARLVNRKQELEEILHDMESRLEEEEERVNQMLNE---RKKMQQN 941
Cdd:TIGR00606 479 ELRkaerelskAEKNSLTETLKKEVKsLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDeqiRKIKSRH 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 942 IADLEQQLDEEEADRQ------KLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFS------------- 1002
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgsqdee 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1003 ---SNLSEEEEKSRS----LQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQL 1075
Cdd:TIGR00606 639 sdlERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1076 ANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQ 1155
Cdd:TIGR00606 719 KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQ 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1156 QELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQ 1235
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT 878
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1236 SKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKD--------------ML 1301
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKvndikekvknihgyMK 958
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1302 SLESHLQDTQELLQEETRQKLA-ISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKmdqevSSLESA 1380
Cdd:TIGR00606 959 DIENKIQDGKDDYLKQKETELNtVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE-----NELKEV 1033
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1381 EESRKRLQREFDtvKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEK 1451
Cdd:TIGR00606 1034 EEELKQHLKEMG--QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
897-1315 |
1.35e-11 |
|
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: 68.56 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 897 EEMRARLVNRKQELEEiLHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGn 976
Cdd:pfam19220 6 ELLRVRLGEMADRLED-LRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 977 imvlddqnnklnkEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTD 1056
Cdd:pfam19220 84 -------------ELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1057 LHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAanmasqkKIKELEAqileldedlerekfyrskngqRCKELEK 1136
Cdd:pfam19220 151 AEKALQRAEGELATARERLALLEQENRRLQALSEEQAA-------ELAELTR---------------------RLAELET 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1137 ELEAIKNKLDDTLDTTAAQQELRAKRETevaqlrkAQEEENKMHESQIAELSKK--HLQAFNEMNEQLEQAKRNKL-SVE 1213
Cdd:pfam19220 203 QLDATRARLRALEGQLAAEQAERERAEA-------QLEEAVEAHRAERASLRMKleALTARAAATEQLLAEARNQLrDRD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1214 KAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQvkygdceRQRQEAVEKIAKLQSELENVNSLLNESEGKN 1293
Cdd:pfam19220 276 EAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQ-------RARAELEERAEMLTKALAAKDAALERAEERI 348
|
410 420
....*....|....*....|...
gi 768942001 1294 TKSSKDMLSLES-HLQDTQELLQ 1315
Cdd:pfam19220 349 ASLSDRIAELTKrFEVERAALEQ 371
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
996-1222 |
1.54e-11 |
|
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: 68.25 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 996 DRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQL 1075
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1076 ANKEEELQNALIrieeeAAANMASQKKIKELEAQilELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQ 1155
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1156 QELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESE 1222
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
933-1121 |
1.69e-11 |
|
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: 68.25 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 933 NERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEK- 1011
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1012 ---SRSLQKLKNK---------------------HEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQ 1067
Cdd:COG4942 107 aelLRALYRLGRQpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1068 IADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREK 1121
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
846-1915 |
2.35e-11 |
|
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: 69.70 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 846 AKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQeQLQAETELCAEAEEMRARLVNRKQEleeILHDMESRLEEEE 925
Cdd:TIGR01612 463 ALEKRFFEIFEEEWGSYDIKKDIDENSKQDNTVKLILM-RMKDFKDIIDFMELYKPDEVPSKNI---IGFDIDQNIKAKL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 926 ER-----VNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEkvttdskMKALEGNIMVLDDQNNKLNKEKKLLEDRIAE 1000
Cdd:TIGR01612 539 YKeieagLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKE-------IKDLFDKYLEIDDEIIYINKLKLELKEKIKN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1001 FSSNlSEEEEKSRSLQKLKNKHEAIITDLEdrlRKEEKQRQELEKNRRKL------------EGDSTDLHDQIADL---- 1064
Cdd:TIGR01612 612 ISDK-NEYIKKAIDLKKIIENNNAYIDELA---KISPYQVPEHLKNKDKIystikselskiyEDDIDALYNELSSIvken 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1065 -------QAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKikELEAQILELDEDLerekfyrskNGQRCKELEKE 1137
Cdd:TIGR01612 688 aidntedKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKN--ELLDIIVEIKKHI---------HGEINKDLNKI 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1138 LEAIKNKlddtldttaaQQELRAKreteVAQLRKAQEEENKmHESQIAELSKKHLQAFNEMNEQLEQAKRNklsVEKAKQ 1217
Cdd:TIGR01612 757 LEDFKNK----------EKELSNK----INDYAKEKDELNK-YKSKISEIKNHYNDQINIDNIKDEDAKQN---YDKSKE 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1218 ALESefnelqIELKTLGQSKSDSEHRRKKAE--SQVQelqvKYGDCERQRQEavekiaKLQSELENVNSLLNESegKNTK 1295
Cdd:TIGR01612 819 YIKT------ISIKEDEIFKIINEMKFMKDDflNKVD----KFINFENNCKE------KIDSEHEQFAELTNKI--KAEI 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1296 SSKDMLSLESHLQDTQELLQEETRQklaistrfrqMEEEQNSLREMLEEEEEAK--KNVEKQISVLQGQLGDMKKKMDQE 1373
Cdd:TIGR01612 881 SDDKLNDYEKKFNDSKSLINEINKS----------IEEEYQNINTLKKVDEYIKicENTKESIEKFHNKQNILKEILNKN 950
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1374 VSSLESAEESRKRLQREFDTV----KLQLEE--KEAAYEKLERTKTRLQQELDDLLVNQ------------DGLRQLVNN 1435
Cdd:TIGR01612 951 IDTIKESNLIEKSYKDKFDNTlidkINELDKafKDASLNDYEAKNNELIKYFNDLKANLgknkenmlyhqfDEKEKATND 1030
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1436 MERKQRKFDQMLAE-EKTISTQYAEERDKAEAE-AREKETRALTLARELET----ITDLKNELERTN-----KQLKAEME 1504
Cdd:TIGR01612 1031 IEQKIEDANKNIPNiEIAIHTSIYNIIDEIEKEiGKNIELLNKEILEEAEInitnFNEIKEKLKHYNfddfgKEENIKYA 1110
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1505 DLVSS-KDD-------AGKNVHELERSKRATEQQLEEIKTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQAR 1573
Cdd:TIGR01612 1111 DEINKiKDDiknldqkIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIY 1189
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1574 DEQgeerrKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGElevHIDAANKGRDEALKQLKKLQVQFKDMMRESED 1653
Cdd:TIGR01612 1190 DEI-----KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLE---KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPE 1261
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1654 LRLSRDEAINSAKETEkkvkTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKnSMLQDEKRRLEARITqlee 1733
Cdd:TIGR01612 1262 IENEMGIEMDIKAEME----TFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEE-SDINDIKKELQKNLL---- 1332
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1734 elEEEQLNSEMANDRNKRTTLQVdqlTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKS-KYKSSLTALEAK 1812
Cdd:TIGR01612 1333 --DAQKHNSDINLYLNEIANIYN---ILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKiKDDINLEECKSK 1407
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1813 VaqlEEQLDteikerqqaTRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEvtraNAYRRK 1892
Cdd:TIGR01612 1408 I---ESTLD---------DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNK----SQHILK 1471
|
1130 1140
....*....|....*....|...
gi 768942001 1893 LQREledaNETQDtMNREVNILK 1915
Cdd:TIGR01612 1472 IKKD----NATND-HDFNINELK 1489
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1220-1849 |
2.85e-11 |
|
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: 68.89 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1220 ESEFNELQIELKTLgqsKSDSEHRRKKAESqvqeLQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKD 1299
Cdd:TIGR04523 32 DTEEKQLEKKLKTI---KNELKNKEKELKN----LDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1300 MLSLESHLQDTQEllqeetrQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLES 1379
Cdd:TIGR04523 105 LSKINSEIKNDKE-------QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1380 AEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAE 1459
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1460 ERDKAEAEAREKETRALTLARELETITDLKNELertnKQLKAEMEDLVSSKD-DAGKNVHE----LERSKRATEQQLEEI 1534
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----NQLKSEISDLNNQKEqDWNKELKSelknQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1535 KTQLEELEDELQATEDAKLRLEVNMQAMKAQFD------RDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSA 1608
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEekqneiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1609 KKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLAT 1688
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1689 AERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTL--QVDQLTAELSae 1766
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIE-- 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1767 rsaaqRLEGARSQAERKNKELSLKLQELESTIKsKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVL 1846
Cdd:TIGR04523 572 -----ELKQTQKSLKKKQEEKQELIDQKEKEKK-DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
...
gi 768942001 1847 QVE 1849
Cdd:TIGR04523 646 EVK 648
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
25-70 |
3.00e-11 |
|
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: 59.75 E-value: 3.00e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 768942001 25 ASKKLVWIPSEKLGFEPGSVKEELGDECMVElTDSGRKVKVNKDDI 70
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVE-TEDGKTVTVKKDDV 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1412-1912 |
6.08e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1412 KTRLQQELDDLLVNQdgLRQLVNNMERKQRKFDQMLAEEktistqyAEERDKAEAEAREKETRALTLARELETITDLKNE 1491
Cdd:COG4717 36 KSTLLAFIRAMLLER--LEKEADELFKPQGRKPELNLKE-------LKELEEELKEAEEKEEEYAELQEELEELEEELEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1492 LERTNKQLKAEMEDLvsskdDAGKNVHELERSKRATEQQLEEIKTQLEELED---ELQATEDAKLRLEVNMQAMKAQFDR 1568
Cdd:COG4717 107 LEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1569 DLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEvhidaANKGRDEALKQLKKLQVQFKdmm 1648
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-----NELEAAALEERLKEARLLLL--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1649 reSEDLRLSRDEAINSAKETEKKVKTMEADAAQFqedLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARI 1728
Cdd:COG4717 254 --IAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1729 TQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQR-----------LEGARSQAERKNK--ELSLKLQELE 1795
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagvedEEELRAALEQAEEyqELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1796 STIKSKYKSSLTALEA-KVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEqykdqADKLNSRTRQLKR 1874
Cdd:COG4717 409 EQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKA 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 768942001 1875 QLEEAEEEVTRANAYRRKLQRELEDA-NETQDTMNREVN 1912
Cdd:COG4717 484 ELRELAEEWAALKLALELLEEAREEYrEERLPPVLERAS 522
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
854-1546 |
7.14e-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: 67.94 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 854 VKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQaetelcaeaeEMRARLVNRKQELEEILHDMESRLeeeeervnQMLN 933
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWK----------EKRDELNGELSAADAAVAKDRSEL--------EALE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 934 ERKKMQQNIADLEQQLDEEEADRQKLQMEKVttDSKMKALEGNImvlDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSR 1013
Cdd:pfam12128 329 DQHGAFLDADIETAAADQEQLPSWQSELENL--EERLKALTGKH---QDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1014 -SLQKLKNKHEAIITDLEDRLRKE-EKQRQELEKNRRKLEGDSTDLHDQIADLQAQiADLRAQLANKEEELQNALIRIEE 1091
Cdd:pfam12128 404 eARDRQLAVAEDDLQALESELREQlEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1092 EAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRK 1171
Cdd:pfam12128 483 ANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1172 AQEEENKMHESQIAELS----KKHLQAFnEMNE--QLEQAKRNKLSveKAKQALESEFNELQIELKTLGQsksdsehrrk 1245
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNlygvKLDLKRI-DVPEwaASEEELRERLD--KAEEALQSAREKQAAAEEQLVQ---------- 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1246 kAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNEsegkntksskdmlSLESHLQDTQELLQEETRQKLAIS 1325
Cdd:pfam12128 630 -ANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK-------------ALAERKDSANERLNSLEAQLKQLD 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1326 TRFRQMEEEQnslremleeEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKR----LQREFDTVKLQLEEK 1401
Cdd:pfam12128 696 KKHQAWLEEQ---------KEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAelkaLETWYKRDLASLGVD 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1402 EAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEK-TISTQYAEERDKAEAEAREKETRALTLAR 1480
Cdd:pfam12128 767 PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLsNIERAISELQQQLARLIADTKLRRAKLEM 846
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768942001 1481 ELETITDLKNELERTNKQLKAEMEDLVSSKDDAgkNVHELERSKRATEQQLEEIKTQLEELEDELQ 1546
Cdd:pfam12128 847 ERKASEKQQVRLSENLRGLRCEMSKLATLKEDA--NSEQAQGSIGERLAQLEDLKLKRDYLSESVK 910
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
918-1109 |
7.22e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 66.39 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 918 ESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNImvlDDQNNKLNKEKKLLEDR 997
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 998 IAEF---------------SSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIA 1062
Cdd:COG3883 92 ARALyrsggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768942001 1063 DLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQ 1109
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1362-1881 |
9.96e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1362 QLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQR 1441
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1442 KFDQMlaeektistqyaEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELE 1521
Cdd:PRK03918 274 EIEEL------------EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1522 RskraTEQQLEEIKTQLEELEDELQATEDAKlRLEVNMQAMKAQFD----RDLQARDEQGEERRKQLVKQVHELE---AE 1594
Cdd:PRK03918 342 E----LKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITariGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1595 LEDERRQRSQAVSAKKKL---------ELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLR--LSRDEAIN 1663
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELI 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1664 SAKETEKKVKTMEADAAQFQ-EDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEAritQLEEELEEEQLNS 1742
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE---LEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1743 EMANDRNKRTTLQVDQLTAELSAERSAAQR---LEGARSQAERKNKELSLKLQELESTIK--SKYKSSLTALEAKVAQLE 1817
Cdd:PRK03918 574 ELLKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEelAETEKRLEELRKELEELE 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1818 EQLDTEIKERQqatrmvrrtEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEE 1881
Cdd:PRK03918 654 KKYSEEEYEEL---------REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1137-1919 |
2.07e-10 |
|
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: 66.22 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1137 ELEAIKNKLDDTLDTT---AAQQELRAKRETEVAQLRKAQEEEN--KMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLS 1211
Cdd:TIGR00606 167 EGKALKQKFDEIFSATryiKALETLRQVRQTQGQKVQEHQMELKylKQYKEKACEIRDQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1212 VEKAKQALE------SEFNELQIELKTLGQSKSDSEHRRKKAESQV--------QELQVKYGDCERQRQEAVEKIAKLQS 1277
Cdd:TIGR00606 247 LDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTVREKERELVDCQR 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1278 ELENVNSLLNESEGKNTK--SSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQ 1355
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTEllVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1356 ISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNN 1435
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1436 MER--KQRKFDQMLAEEKTISTQYAE--ERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKD 1511
Cdd:TIGR00606 487 LSKaeKNSLTETLKKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1512 DAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQgEERRKQLVKQVHEL 1591
Cdd:TIGR00606 567 GYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ-LSSYEDKLFDVCGS 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1592 EAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFK---DMMRESEDLRLSRDEAINSAKET 1668
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1669 EKKVKTMEAdaaQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDR 1748
Cdd:TIGR00606 715 ESELKKKEK---RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1749 nkrTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKskykssltaleaKVAQLEEQLDTEIKERQ 1828
Cdd:TIGR00606 792 ---TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSKIELNRKLIQDQQ 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1829 QATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMN 1908
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
810
....*....|....*
gi 768942001 1909 R----EVNILKSKLR 1919
Cdd:TIGR00606 937 KkaqdKVNDIKEKVK 951
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1189-1939 |
2.18e-10 |
|
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: 66.15 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1189 KKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEfnELQIELKTLGQSKSDSEHRRKKAESQVQELQVKygDCERQRQEA 1268
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLA--ELIIDLEELKLQELKLKEQAKKALEYYQLKEKL--ELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1269 VEKIAKLQSELENVNSLLNESEGKNTKSSKDMlsleshlQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEA 1348
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEI-------EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1349 KKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDG 1428
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1429 LRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNElertNKQLKAEMEDLVS 1508
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1509 SKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQL---- 1584
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlgva 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1585 ----------VKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDL 1654
Cdd:pfam02463 538 venykvaistAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1655 RLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEE 1734
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1735 LEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKva 1814
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE-- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1815 qLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQ 1894
Cdd:pfam02463 776 -LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 768942001 1895 RELEDANETQDTMNREVNILKSKLRRDLPFTIRTVNRSGLESDDD 1939
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
870-1095 |
2.83e-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: 64.40 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 870 SKQQQLNAEKMALQEQLQaetelcaEAEEMRARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQL 949
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 950 DEEEA--DRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKL-LEDRIAEFSSNLSEE-EEKSRSLQKLKNKHEAI 1025
Cdd:COG4942 93 AELRAelEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEElRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1026 ITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQlankEEELQNALIRIEEEAAA 1095
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE----AEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1127-1609 |
3.81e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1127 NGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKM-----HESQIAELS--KKHLQAFNEMN 1199
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqLLPLYQELEalEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1200 EQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSehrrkkAESQVQELQVKYGDCERQRQEAVEKIAKLQSEL 1279
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1280 ENVnsllnesegkntKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFrqmeeeqnSLREMLEEEEEAKKNVEKQISVL 1359
Cdd:COG4717 223 EEL------------EEELEQLENELEAAALEERLKEARLLLLIAAALL--------ALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1360 QGQLGDMKKKMDQEVSSLESAEESRKRLQREFDtvkLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERK 1439
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEE---LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1440 QRKFDQMLAEEKtISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLvsSKDDAGKNVHE 1519
Cdd:COG4717 360 EEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1520 LERSKRATEQQLEEIKTQLEELEDELQATEDaklrlEVNMQAMKAQFDRdLQARDEQGEERRKQLVKQVHELEAELEDER 1599
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEE-LKAELRELAEEWAALKLALELLEEAREEYR 510
|
490
....*....|
gi 768942001 1600 RQRSQAVSAK 1609
Cdd:COG4717 511 EERLPPVLER 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1033-1881 |
5.52e-10 |
|
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: 64.60 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1033 LRKEEKQRQELEKNRRKLE---GDSTDLHDQIADLQAQIADLRAqlANKEEELQNALIRIEEEAAANMASQKKIKELEAQ 1109
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEqkkGRGRILAAKKSETEEVIHDLLK--LDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1110 ILELD--EDLEREKFYRSKngqrckELEKELEAIKNKLD-DTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQiae 1186
Cdd:TIGR00618 172 LFPLDqyTQLALMEFAKKK------SLHGKAELLTLRSQlLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1187 lskkhlqafnEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAesQVQELQVKYGDCERQRQ 1266
Cdd:TIGR00618 243 ----------AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1267 EAvekIAKLQSELENVNSLLNesegKNTKSSKDMLSLESHLQDTQELLQEETRqklaistrFRQMEEEQNSLREMLEEEE 1346
Cdd:TIGR00618 311 RI---HTELQSKMRSRAKLLM----KRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQH 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1347 EAKKnvekQISVLQGQLGDMKKKmdqevssLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQ 1426
Cdd:TIGR00618 376 TLTQ----HIHTLQQQKTTLTQK-------LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1427 DGLR---QLVNNMERKQRKFDQMLAEEKTistqyaEERDKAEAEAREKETRALTLAReLETITDLKNELERTNKQLKAEM 1503
Cdd:TIGR00618 445 AAITctaQCEKLEKIHLQESAQSLKEREQ------QLQTKEQIHLQETRKKAVVLAR-LLELQEEPCPLCGSCIHPNPAR 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1504 EDLVSSKDD-----AGKNVH-ELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdlqardeqg 1577
Cdd:TIGR00618 518 QDIDNPGPLtrrmqRGEQTYaQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN--------- 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1578 eeRRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFK-DMMRESEDLRL 1656
Cdd:TIGR00618 589 --LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALS 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1657 SRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAErdelqdeingnntKNSMLQDEKRRLEARITQLEEELE 1736
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL-------------ETHIEEYDREFNEIENASSSLGSD 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1737 EEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGArsqaerknKELSLKLQELESTIKSKYKSsLTALEAKVAQL 1816
Cdd:TIGR00618 734 LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA--------LQTGAELSHLAAEIQFFNRL-REEDTHLLKTL 804
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1817 EEQLDTEIKERQQatrmvrrtekkmkELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEE 1881
Cdd:TIGR00618 805 EAEIGQEIPSDED-------------ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1169 |
1.10e-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: 60.71 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1005 LSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLAN--KEEEL 1082
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1083 QNALIRIEeeaaanmASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTL-DTTAAQQELRAK 1161
Cdd:COG1579 92 EALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELaELEAELEELEAE 164
|
....*...
gi 768942001 1162 RETEVAQL 1169
Cdd:COG1579 165 REELAAKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
836-1253 |
1.11e-09 |
|
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: 63.50 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQaetelcaeaeemrarlvNRKQELEEILH 915
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE-----------------EKQNEIEKLKK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 916 DMESRleeeeervnqmLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLE 995
Cdd:TIGR04523 378 ENQSY-----------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 996 DRIAefssnlseeeEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTD---LHDQIADLQAQIADLR 1072
Cdd:TIGR04523 447 NQDS----------VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLT 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1073 ---AQLANKEEELQNALIRIEeeaaanmasqKKIKELEAQILELDEDLEREKFYRSKNgqrckELEKELEAIKNKLDDTL 1149
Cdd:TIGR04523 517 kkiSSLKEKIEKLESEKKEKE----------SKISDLEDELNKDDFELKKENLEKEID-----EKNKEIEELKQTQKSLK 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1150 DTTAAQQELRAKRETEVAQLRKAQEEenkmHESQIAELSKKhLQAFNEMNEQLEQAKRNklsVEKAKQALESEFNELQIE 1229
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEE----KEKKISSLEKE-LEKAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKET 653
|
410 420
....*....|....*....|....
gi 768942001 1230 LKTLGQSKSDSEHRRKKAESQVQE 1253
Cdd:TIGR04523 654 IKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1200-1818 |
2.49e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1200 EQLEQAKRNKLSVEKakqalesEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQV---KYGDCERQRQEAVEKIAKLQ 1276
Cdd:PRK03918 158 DDYENAYKNLGEVIK-------EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1277 SELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQE------ETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKK 1350
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEElkkeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1351 NVEKQISVLQGQLGDMKKKMDQevssLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERtktrlqqelddllvnqdgLR 1430
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEE------------------AK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1431 QLVNNMERKQRKFDqmlaeektistqyAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKaemedlvssk 1510
Cdd:PRK03918 369 AKKEELERLKKRLT-------------GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK---------- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1511 ddagKNVHELERSKRA--------TEQQ----LEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRD-----LQAR 1573
Cdd:PRK03918 426 ----KAIEELKKAKGKcpvcgrelTEEHrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselikLKEL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1574 DEQGEERRKQLVK-QVHELEAELEDERRQRSQAVSAKKKLELDLGELEvHIDAANKGRDEALKQLKKLQVQFKDMMRESE 1652
Cdd:PRK03918 502 AEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1653 DLRLSrdeainSAKETEKKVKTMEADAAQFQEdLATAERLKRQMQAERDELQDEIngnNTKNSMLQDEKRRLEaRITQLE 1732
Cdd:PRK03918 581 ELGFE------SVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEEL---DKAFEELAETEKRLE-ELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1733 EELEEEQLNSEMANDRNKRTtlqvdQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELEstiksKYKSSLTALEAK 1812
Cdd:PRK03918 650 EELEKKYSEEEYEELREEYL-----ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-----KAKKELEKLEKA 719
|
....*.
gi 768942001 1813 VAQLEE 1818
Cdd:PRK03918 720 LERVEE 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1375-1613 |
2.53e-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: 61.32 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1375 SSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDllvnqdgLRQLVNNMERKQRKFDQMLAEektis 1454
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-------LERRIAALARRIRALEQELAA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1455 tqyaEERDKAEAEAREKETRAlTLARELETITDLKNELERTNKQLKAEMedLVSSKD--DAGKNVHELERSKRATEQQLE 1532
Cdd:COG4942 81 ----LEAELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1533 EIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQgEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKL 1612
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
.
gi 768942001 1613 E 1613
Cdd:COG4942 233 E 233
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
904-1449 |
2.89e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 904 VNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQ 983
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 984 NNKLN---KEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDL----EDRLRKEEKQRQELEKNRRKLEGDSTD 1056
Cdd:PRK01156 241 LNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDIENKKQILSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1057 L------HDQIADLQAQIADLrAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQR 1130
Cdd:PRK01156 321 InkyhaiIKKLSVLQKDYNDY-IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1131 C----KELEKELEAIKNKLDD-TLDTTAAQQELRAKRETEVAQLRKAQEEENK---------MHESQIAELSKKHLQAFN 1196
Cdd:PRK01156 400 QeidpDAIKKELNEINVKLQDiSSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1197 EMNEQLEQAKRN-------KLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDC-ERQRQEA 1268
Cdd:PRK01156 480 RLEEKIREIEIEvkdidekIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIkNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1269 VEKIAKLQSELENVNSLLNESEGKNTKSSKDMLS--LESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLRemleEEE 1346
Cdd:PRK01156 560 LEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKkqLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN----NKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1347 EAKKNVEKQISVLQGQLGDMKKkmdqEVSSLESAEESRKrlqrefdTVKLQLEEKEAAYEKLERtktrlqqELDDLLVNQ 1426
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKK----QIAEIDSIIPDLK-------EITSRINDIEDNLKKSRK-------ALDDAKANR 697
|
570 580
....*....|....*....|...
gi 768942001 1427 DGLRQLVNNMERKQRKFDQMLAE 1449
Cdd:PRK01156 698 ARLESTIEILRTRINELSDRIND 720
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1022-1496 |
3.03e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1022 HEAIITDLEDRLRKEekqRQELEKNRRKLegdSTDLHDQIADLQAQIADLRAQlankEEELQNALIRIEEEAAANMASQK 1101
Cdd:COG4717 40 LAFIRAMLLERLEKE---ADELFKPQGRK---PELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1102 KIKELEAQILELDEDLEREKFYrskngQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEEnkmhE 1181
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLY-----QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL----E 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1182 SQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQV----- 1256
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1257 --KYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTR------- 1327
Cdd:COG4717 261 llGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspeell 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1328 --FRQMEEEQNSLREMLEEEEEAKKNVEKQisVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAY 1405
Cdd:COG4717 341 elLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1406 EKLER--TKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQ---MLAEEKTISTQYAEERD-KAEAEAREKETRALTLA 1479
Cdd:COG4717 419 EELLEalDEEELEEELEELEEELEELEEELEELREELAELEAeleQLEEDGELAELLQELEElKAELRELAEEWAALKLA 498
|
490
....*....|....*..
gi 768942001 1480 RELetITDLKNELERTN 1496
Cdd:COG4717 499 LEL--LEEAREEYREER 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1241-1843 |
4.60e-09 |
|
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: 61.66 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1241 EHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQ 1320
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1321 KlaiSTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEE 1400
Cdd:pfam05483 280 Q---DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1401 KEAAYEKLERTKtrlQQELDDllvNQDGLRQLVNNMERKQRKFDQMlaeektistqyAEERDKAEAEAREKETraltLAR 1480
Cdd:pfam05483 357 TTCSLEELLRTE---QQRLEK---NEDQLKIITMELQKKSSELEEM-----------TKFKNNKEVELEELKK----ILA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1481 ELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQA--------TEDAK 1552
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknielTAHCD 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1553 LRLEVNMQAMKAQFDRDLQARDEQGE--ERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGR 1630
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1631 DEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAE----RLKRQMQAERDELQDE 1706
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEikvnKLELELASAKQKFEEI 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1707 IngnNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLegarsqAERKNKE 1786
Cdd:pfam05483 656 I---DNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKI------IEERDSE 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1787 LSL--KLQELESTIKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKE 1843
Cdd:pfam05483 727 LGLykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1016-1280 |
7.27e-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: 60.16 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1016 QKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNAlirieeeaaa 1095
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1096 nmasQKKIKELEAQILELDEDLEREKFYRSKNGQRckeleKELEAIKNKLDdtldttAAQQELRAKRETEVAQLRKAQEE 1175
Cdd:COG4942 89 ----EKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPED------FLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1176 enkmhesqiaelskkhlqafnEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQ 1255
Cdd:COG4942 154 ---------------------ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|....*
gi 768942001 1256 VKYGDCERQRQEAVEKIAKLQSELE 1280
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1464-1681 |
8.83e-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: 59.78 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1464 AEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELED 1543
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1544 ELQATEDAKLRLEVNMQAMK--------------AQFDRDLQARDEQGEERRKQ---LVKQVHELEAELEDERRQRSQAV 1606
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQaeeLRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1607 SAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQ 1681
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
836-1223 |
9.59e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVkEKQLQAEEMIKEFESKQQQLNAEKM---ALQEQLQAETELCAEAEEMRARLVNRKQELEE 912
Cdd:COG4717 103 ELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPErleELEERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 913 ILhdmESRLEEEEERVNQMLNERKKMQQNIADLEQQLDE-----EEADRQKLQMEKVTTDSKMK---------------- 971
Cdd:COG4717 182 LL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEaqeelEELEEELEQLENELEAAALEerlkearlllliaaal 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 972 -ALEGNIMVLDDQNN------------------KLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDR 1032
Cdd:COG4717 259 lALLGLGGSLLSLILtiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1033 LRKEEKQRQELEKNRRKLEGDSTDLhdQIADLQAQIADLRAQL-ANKEEELQNALIRIEEEAAAnmasQKKIKELEAQIL 1111
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAgVEDEEELRAALEQAEEYQEL----KEELEELEEQLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1112 ELDEDLEREKFYRSKngqrcKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEeenkmhesqIAELSKKH 1191
Cdd:COG4717 413 ELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQEL 478
|
410 420 430
....*....|....*....|....*....|....*
gi 768942001 1192 LQAFNEMNEQLEQAKRNKLS---VEKAKQALESEF 1223
Cdd:COG4717 479 EELKAELRELAEEWAALKLAlelLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
836-1276 |
1.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAEtELCAEAEEMRARLVNRKQELEEILH 915
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 916 DMEsrleeeeeRVNQMLNERKKMQQNIADLEQQLDEEEADRQklqmekVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLE 995
Cdd:COG4717 154 RLE--------ELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 996 DRIAEFSSNLSEEEEKSRSLQKLKNKHEAIItdledrLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQL 1075
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARL------LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1076 ANKEEELQNALIRIEEEAAANMASQKKIKELEAQiLELDEDLEREKFYR-SKNGQRCKELEKELEAIKNKLDDTLDTTAA 1154
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAA-LGLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1155 QQELRAKRETEVAQLRKAQEEENKMHE--SQIAELSKKHLQAFNEMNEQLEQAkrNKLSVEKAKQALESEFNELQIELKT 1232
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 768942001 1233 LGQSKSDSEHRRKKAESQ--VQELQVKYGDCERQRQEAVEKIAKLQ 1276
Cdd:COG4717 451 LREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1311-1554 |
1.18e-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: 59.39 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1311 QELLQEETRQKL-AISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQR 1389
Cdd:COG4942 18 QADAAAEAEAELeQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1390 EFDTVKLQLEEKEAAYEKLERtktrlqQELDDLLVNQDGLRQLVnnmeRKQRKFDQMLAEEKTISTQYAEERDKAEAEAR 1469
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGR------QPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1470 EKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATE 1549
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 768942001 1550 DAKLR 1554
Cdd:COG4942 248 FAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1465 |
1.25e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 860 QAEEMIKEFEskqqQLN-AEKMALQEQLQAET--ELCAEAEEmRARLVNRKQELEEILHdmESRLEEEEERVNQMLNERK 936
Cdd:COG4913 226 AADALVEHFD----DLErAHEALEDAREQIELlePIRELAER-YAAARERLAELEYLRA--ALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 937 KMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGN-IMVLDDQNNKLNKEKKLLEDRIAEFSSNLS----EEEEK 1011
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAalglPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1012 SRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQI-----------ADLRAQLANKEE 1080
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllalrDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1081 ELQNA--LIRIEEEAAA-NMASQKKI----------KELEAQILELdedLEREKFYRSKNGQRCKELEKELEAIK----- 1142
Cdd:COG4913 459 ELPFVgeLIEVRPEEERwRGAIERVLggfaltllvpPEHYAAALRW---VNRLHLRGRLVYERVRTGLPDPERPRldpds 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1143 --NKLDdtLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQI--AELSKKHLQAFnEMNEQLEQAKRNKL--SVEKAK 1216
Cdd:COG4913 536 laGKLD--FKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAItrAGQVKGNGTRH-EKDDRRRIRSRYVLgfDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1217 QALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQ--VKYGDCERQRQEAVEKIAKLQSELENVnsllnesegknT 1294
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERL-----------D 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1295 KSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDmkkKMDQEV 1374
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAA 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1375 SSLESAEESRKRLQREFDTVKlqlEEKEAAYEKLERTKTRLQQELDDLLVNQDG-----------LRQLVNN-MERKQRK 1442
Cdd:COG4913 759 LGDAVERELRENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDAdleslpeylalLDRLEEDgLPEYEER 835
|
650 660
....*....|....*....|....*...
gi 768942001 1443 FDQMLAEEKT-----ISTQYAEERDKAE 1465
Cdd:COG4913 836 FKELLNENSIefvadLLSKLRRAIREIK 863
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1355-1683 |
1.38e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1355 QISVLQGQLGDMKKKMDQEVSSLESAE-----ESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLlvnqdgl 1429
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEkarevERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1430 rqlvnNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSS 1509
Cdd:pfam17380 354 -----RQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1510 KDDAGKnvHELERSKRATEQQLEEIKtqLEELEDELQATedaKLRL-EVNMQAMKAQFDRDLQARDEQGEERRKQLVKQV 1588
Cdd:pfam17380 429 QEEARQ--REVRRLEEERAREMERVR--LEEQERQQQVE---RLRQqEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1589 HELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDE-ALKQLKKLQVQfkdMMRESEDlrLSRDEAINSAKE 1667
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqEMEERRRIQEQ---MRKATEE--RSRLEAMERERE 576
|
330
....*....|....*.
gi 768942001 1668 TEKKVKTMEADAAQFQ 1683
Cdd:pfam17380 577 MMRQIVESEKARAEYE 592
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
883-1202 |
1.63e-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: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 883 QEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLeeeeeRVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQme 962
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-----EALQRLAEYSWDEIDVASAEREIAELEAELERLD-- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 963 kvTTDSKMKALEgnimvldDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEekQRQE 1042
Cdd:COG4913 682 --ASSDDLAALE-------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1043 LEKnRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRI----EEEAAANMASQKKIKELEAQILEL-DEDL 1117
Cdd:COG4913 751 LEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDRLeEDGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1118 ER--EKFYRSKN-------GQRCKELEKELEAIKNKLD---DTL------DTTAAQQELRAKRETEVAQLRKAQEEENKM 1179
Cdd:COG4913 830 PEyeERFKELLNensiefvADLLSKLRRAIREIKERIDplnDSLkripfgPGRYLRLEARPRPDPEVREFRQELRAVTSG 909
|
330 340
....*....|....*....|...
gi 768942001 1180 HESQIAELSKKHLQAFNEMNEQL 1202
Cdd:COG4913 910 ASLFDEELSEARFAALKRLIERL 932
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
952-1427 |
2.48e-08 |
|
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: 58.98 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 952 EEADRQKLQMEK------VTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKnkhEAI 1025
Cdd:pfam05557 12 SQLQNEKKQMELehkrarIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL---EAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1026 ITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIA---DLRAQLANKEEELQNALIRIEEEAAA---NMAS 1099
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSeleELQERLDLLKAKASEAEQLRQNLEKQqssLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1100 QKKIKELEAQILELDEDLEREKFYRSKNGqRCKELEKELEAIKNKlDDTLDTTAAQQELrakRETEVAQLRKAQEEENKM 1179
Cdd:pfam05557 169 EQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPELEKELERLREH-NKHLNENIENKLL---LKEEVEDLKRKLEREEKY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1180 HESQIA-ELSKKHLQAfnEMNEQLEQAKRNKLSVEKAkQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKy 1258
Cdd:pfam05557 244 REEAATlELEKEKLEQ--ELQSWVKLAQDTGLNLRSP-EDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1259 gdcerqRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQD-TQELLQEETRQKLaiSTRFRQMEEEQNS 1337
Cdd:pfam05557 320 ------LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESyDKELTMSNYSPQL--LERIEEAEDMTQK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1338 LRemleeeeEAKKNVEKQISVLQGQLG---DMKKKMDQEVSSLESAEESRKR--LQREFDTVKLQLEEKEAAYEKLERTK 1412
Cdd:pfam05557 392 MQ-------AHNEEMEAQLSVAEEELGgykQQAQTLERELQALRQQESLADPsySKEEVDSLRRKLETLELERQRLREQK 464
|
490
....*....|....*
gi 768942001 1413 TRLQQELDDLLVNQD 1427
Cdd:pfam05557 465 NELEMELERRCLQGD 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
866-1221 |
2.53e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.98 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 866 KEFESKQQQLNAEKMAlQEQLQAEtelcaeaEEMRARLVNRKQELEEILHDMESRLEEEEE---RVNQMLNERKKMQQNI 942
Cdd:pfam17380 282 KAVSERQQQEKFEKME-QERLRQE-------KEEKAREVERRRKLEEAEKARQAEMDRQAAiyaEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 943 ADLEQQLDEEEADRQKLQMEKvttdSKMKALEGNIMVLDDQNNKLNKEkkLLEDRIAEFssnlsEEEEKSRSLQKLKNKH 1022
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEI----SRMRELERLQMERQQKNERVRQE--LEAARKVKI-----LEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1023 EAIITDLEDRlRKEEKQRQELEKNRrklEGDSTDLHDQiaDLQAQIADLRAQlankEEELQNALIRIEEEAaanmASQKK 1102
Cdd:pfam17380 423 EQIRAEQEEA-RQREVRRLEEERAR---EMERVRLEEQ--ERQQQVERLRQQ----EEERKRKKLELEKEK----RDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1103 IKELEAQILELDEDLEREKFYRSKNGQrcKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEvaQLRKAQEEENKMHEs 1182
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKR--KLLEKEMEERQKAIYEEERRREAEEERRKQQEME--ERRRIQEQMRKATE- 563
|
330 340 350
....*....|....*....|....*....|....*....
gi 768942001 1183 qiaelSKKHLQAFNEMNEQLEQAKRNklsvEKAKQALES 1221
Cdd:pfam17380 564 -----ERSRLEAMEREREMMRQIVES----EKARAEYEA 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1375-1885 |
3.60e-08 |
|
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: 58.60 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1375 SSLESAEESRKRLQREFDTVKLQLEEKEAAY-EKLERTKTRLQQELDDLlvnqdglrQLVNNMERKQRKFDQMLAEEKTI 1453
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALkRQLDRESDRNQELQKRI--------RLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1454 STQYAEERDKAEAEAREKETRALTLAREL-ETITDLKNELERTNKQLKA---EMEDLVSSKDDAGKNVHELERSKRATEQ 1529
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLkNELSELRRQIQRAELELQStnsELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1530 QLEEIKT---QLEELEDELQATEDAKLRLEvNMQAMKAQFDrDLQARDEQGEERRKQLVK----------QVHELEAELE 1596
Cdd:pfam05557 161 QQSSLAEaeqRIKELEFEIQSQEQDSEIVK-NSKSELARIP-ELEKELERLREHNKHLNEnienklllkeEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1597 DERRQRSQAVSAKKKLELDLGELE--------------VHIDAANK-----GRDEALKQLK-KLQVQFKDMMRESEDLRL 1656
Cdd:pfam05557 239 REEKYREEAATLELEKEKLEQELQswvklaqdtglnlrSPEDLSRRieqlqQREIVLKEENsSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1657 SRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQdEKRRLEARITQLEEELE 1736
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1737 EEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAE-----RKNKELSLKLQELESTIKSkykssltaLEA 1811
Cdd:pfam05557 398 EMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvdslrRKLETLELERQRLREQKNE--------LEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1812 KVAQLEEQLDTEIKE------RQQATRMVRRTEKKMKELvLQVEDER-----RNTEQYKDQADKLNS--------RTRQL 1872
Cdd:pfam05557 470 ELERRCLQGDYDPKKtkvlhlSMNPAAEAYQQRKNQLEK-LQAEIERlkrllKKLEDDLEQVLRLPEttstmnfkEVLDL 548
|
570
....*....|...
gi 768942001 1873 KRQLEEAEEEVTR 1885
Cdd:pfam05557 549 RKELESAELKNQR 561
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1625-1843 |
4.22e-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: 57.47 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1625 AANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQ 1704
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1705 DEINGNNtknsmlQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTL----------QVDQLTAELSAERSAAQRLE 1774
Cdd:COG4942 97 AELEAQK------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1775 GARSQAERKNKELSLKLQELESTIKSKyKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKE 1843
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1460-1868 |
4.25e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1460 ERDKAEA-EAREKETRALT-LARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGK------NVHELErsKRATEQQ- 1530
Cdd:PRK04863 292 RRELYTSrRQLAAEQYRLVeMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKieryqaDLEELE--ERLEEQNe 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1531 -LEEIKTQLEELEDELQATEDAKLRLEVNM----QAMKAQFDRDLQARDE-QGEERRKQL-------VKQVHELEAELED 1597
Cdd:PRK04863 370 vVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAvQALERAKQLcglpdltADNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1598 ERRQRSQAV-SAKKKLELDlgelevhiDAANKGRDEALKQLKKLQVQfkdmmresedlrLSRDEAINSAKETEKKVKTME 1676
Cdd:PRK04863 450 KEQEATEELlSLEQKLSVA--------QAAHSQFEQAYQLVRKIAGE------------VSRSEAWDVARELLRRLREQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1677 ADAAQFQedlataerlkrQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEeeleeeqlnsemandrnkrttlQV 1756
Cdd:PRK04863 510 HLAEQLQ-----------QLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED----------------------EL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1757 DQLTAELSAERSAAQrlEGARSQAERKNkELSLKLQELESTIKSKYKSSLTALEA--KVAQLEEQLDTEIKERQQATRMV 1834
Cdd:PRK04863 557 EQLQEELEARLESLS--ESVSEARERRM-ALRQQLEQLQARIQRLAARAPAWLAAqdALARLREQSGEEFEDSQDVTEYM 633
|
410 420 430
....*....|....*....|....*....|....
gi 768942001 1835 RRTEKKMKELVLQVEDERRNTEQYKDQADKLNSR 1868
Cdd:PRK04863 634 QQLLERERELTVERDELAARKQALDEEIERLSQP 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1397-1828 |
5.06e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1397 QLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQmlaeektistqyAEERDKAEAEAREKETRAL 1476
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------------YQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1477 TLARELETITDLKNELERTNKQLKAEMEDLVsskddagknvHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLE 1556
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1557 VNMQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAEL----EDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDE 1632
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1633 ALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQ-----AERDELQDEI 1707
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1708 NGNN----TKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDrnkrtTLQVDQLTAELSAERSAAQRLEGARSQAERK 1783
Cdd:COG4717 380 GVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 768942001 1784 NKELSLKLQELEStikskyKSSLTALEAKVAQLEEQLDTEIKERQ 1828
Cdd:COG4717 455 LAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWA 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1497-1920 |
6.15e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1497 KQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAqfdrdlqardeq 1576
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE------------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1577 gEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEvhidaankgrdEALKQLKKLQVQFKDMMRESEDLRL 1656
Cdd:COG4717 117 -ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-----------ELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1657 SRDEAinsakeTEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELE 1736
Cdd:COG4717 185 QLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1737 EEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKVAQL 1816
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1817 EEQLDTEIKERQQATRMVRRTEKKMKELVLQV-------------EDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEV 1883
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQeiaallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
410 420 430
....*....|....*....|....*....|....*....
gi 768942001 1884 TRANAY--RRKLQRELEDANETQDTMNREVNILKSKLRR 1920
Cdd:COG4717 419 EELLEAldEEELEEELEELEEELEELEEELEELREELAE 457
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
932-1281 |
6.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 932 LNERKKMQQNIADLEQQLDEEEADRQKLQmekvTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDrIAEFSSNLSEEEEK 1011
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1012 SRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIE- 1090
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEe 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1091 -EEAAANMASQKKIKELEAQILELDEDL-----------------------------------------EREKFYRSKNG 1128
Cdd:COG4717 225 lEEELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1129 QRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETE----VAQLRKAQEEENKMHES-QIAELSKKHLQAFNEMNEQLE 1203
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLElldrIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1204 QAKRNKLSVEKAKQALESEFNEL--QIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELEN 1281
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELeeQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1093-1288 |
7.93e-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: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1093 AAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKA 1172
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1173 QEEENKMHESQIAELSkKHLQAFNEMNEQ-----------LEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSE 1241
Cdd:COG4942 92 IAELRAELEAQKEELA-ELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768942001 1242 HRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNE 1288
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
942-1113 |
8.10e-08 |
|
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: 55.32 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 942 IADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNk 1021
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1022 heaiITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQK 1101
Cdd:COG1579 91 ----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170
....*....|...
gi 768942001 1102 KI-KELEAQILEL 1113
Cdd:COG1579 167 ELaAKIPPELLAL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1059-1297 |
8.66e-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: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1059 DQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKfyrskngQRCKELEKEL 1138
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1139 EAIKNKLDdtldttaAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSK--KHLQAFNE-MNEQLEQAKRNKLSVEKA 1215
Cdd:COG4942 93 AELRAELE-------AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPaRREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1216 KQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTK 1295
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
..
gi 768942001 1296 SS 1297
Cdd:COG4942 246 AG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1565 |
9.29e-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: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1352 VEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLlvnQDGLRQ 1431
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ---KEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1432 LVNNMERKQRKFDQMLAeektistqyAEERDKAEAEAREKETRALTLAR--ELETITDLKNELERTNKQLKAEMEDLVSS 1509
Cdd:COG4942 109 LLRALYRLGRQPPLALL---------LSPEDFLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768942001 1510 KDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQ 1565
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1433-1839 |
9.55e-08 |
|
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: 57.65 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1433 VNNMERKQRKFDQMLAEEKTistQYAEERDKAEAEAREKEtraltLARELETITDLKNELE--------RTNKQLKA--E 1502
Cdd:COG3096 274 MRHANERRELSERALELRRE---LFGARRQLAEEQYRLVE-----MARELEELSARESDLEqdyqaasdHLNLVQTAlrQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1503 MEDLVSSKDDagknVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNM----QAMKAQFDRDLQARDE-QG 1577
Cdd:COG3096 346 QEKIERYQED----LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQYQQAvQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1578 EERRKQL-------VKQVHELEAELEDERRQRSQAV-SAKKKLELDlgelevhiDAANKGRDEALKQLKKLQVQfkdmmr 1649
Cdd:COG3096 422 LEKARALcglpdltPENAEDYLAAFRAKEQQATEEVlELEQKLSVA--------DAARRQFEKAYELVCKIAGE------ 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1650 esedlrLSRDEAINSAKETEKKVKTMEADAAQFQE---DLATAE-RLKRQMQAER--DELQDEINGNNTKNSMLQDEKRR 1723
Cdd:COG3096 488 ------VERSQAWQTARELLRRYRSQQALAQRLQQlraQLAELEqRLRQQQNAERllEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1724 LEARITQLEEeleeeqlnsEMANDRNKRTTL--QVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKL---QELESTI 1798
Cdd:COG3096 562 LEAQLEELEE---------QAAEAVEQRSELrqQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALadsQEVTAAM 632
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768942001 1799 KS--KYKSSLTALEAKVAQLEEQLDTEIKERQQA-----TRMVRRTEK 1839
Cdd:COG3096 633 QQllEREREATVERDELAARKQALESQIERLSQPggaedPRLLALAER 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1267-1888 |
9.70e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1267 EAVEKIAKLQSELENVNSLlnESEGKNTKSSKDMLS-LESHLQDTQELLQEETRQKLAIS--------TRFRQMEEEQNS 1337
Cdd:COG4913 222 DTFEAADALVEHFDDLERA--HEALEDAREQIELLEpIRELAERYAAARERLAELEYLRAalrlwfaqRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1338 LREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQ-EVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTktrLQ 1416
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP---LP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1417 QELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETI-TDLKNELERT 1495
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrDALAEALGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1496 NK---------QLKAEMED----------------LVSSK--DDAGKNVHELERSKRAteqQLEEIKTQLEELEDElQAT 1548
Cdd:COG4913 457 EAelpfvgeliEVRPEEERwrgaiervlggfaltlLVPPEhyAAALRWVNRLHLRGRL---VYERVRTGLPDPERP-RLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1549 ED---AKLRLEVN------MQAMKAQFDRdLQARDEQGEERRKQ------LVKQVHELeAELEDERRQRSQAV---SAKK 1610
Cdd:COG4913 533 PDslaGKLDFKPHpfrawlEAELGRRFDY-VCVDSPEELRRHPRaitragQVKGNGTR-HEKDDRRRIRSRYVlgfDNRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1611 KLEldlgELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLR--LSRDEAINSAKETEKKVKTMEADAAQFQE---D 1685
Cdd:COG4913 611 KLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1686 LATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELeeeqlnSEMANDRNKRTTLQVDQLTAELSA 1765
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL------EAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1766 ERSAAQ---RLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKVAQLEEQLdtEIKERQQATRMVRRtEKKMK 1842
Cdd:COG4913 761 DAVERElreNLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYL--ALLDRLEEDGLPEY-EERFK 837
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 768942001 1843 ELVlqvedeRRNTEQYKDQadkLNSrtrQLKRQLEEAEEEVTRANA 1888
Cdd:COG4913 838 ELL------NENSIEFVAD---LLS---KLRRAIREIKERIDPLND 871
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1264-1485 |
1.13e-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: 56.31 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1264 QRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLRemle 1343
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1344 eeeeakKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLL 1423
Cdd:COG4942 97 ------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1424 VNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETI 1485
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1359-1915 |
1.15e-07 |
|
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: 57.04 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1359 LQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEE-----KEAAYEK---------LERTKTRLQQELDDLLV 1424
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEeiqenKDLIKENnatrhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1425 NQDGLRQ----LVNNMERKQRKFDQML--AEEKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKq 1498
Cdd:pfam05483 177 EREETRQvymdLNNNIEKMILAFEELRvqAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1499 lkaeMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELqatEDAKLRLEVNMQAMKAqFDRDLQARDeqge 1578
Cdd:pfam05483 256 ----MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL---EDIKMSLQRSMSTQKA-LEEDLQIAT---- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1579 errKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESED---LR 1655
Cdd:pfam05483 324 ---KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1656 LSRDEAINSAKETEKKVKTMEADAAQFQ----EDLATAERLKRQMQAERDELQD---EINGNNTKNSMLQDEKRRLEARI 1728
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEKKQFEkiaeELKGKEQELIFLLQAREKEIHDleiQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1729 TQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERsaaQRLEGARSQAERKNKELSlKLQELESTIKSKYKSSLTA 1808
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---EDIINCKKQEERMLKQIE-NLEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1809 LEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANA 1888
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
570 580 590
....*....|....*....|....*....|.
gi 768942001 1889 YRRKLQRELEDAN----ETQDTMNREVNILK 1915
Cdd:pfam05483 637 KVNKLELELASAKqkfeEIIDNYQKEIEDKK 667
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1105-1600 |
1.18e-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: 57.06 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1105 ELEAQILELDEDLERE--KFYRSKNgqrckELEKELEAIKNKLDDTLDTTAAQQ---ELRAKRETEVAQLRKAQEEENKM 1179
Cdd:pfam05557 6 ESKARLSQLQNEKKQMelEHKRARI-----ELEKKASALKRQLDRESDRNQELQkriRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1180 HESQIAELSKKhlqaFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYG 1259
Cdd:pfam05557 81 KKKYLEALNKK----LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1260 DCERQRQEAVEKIAKLQsELENVNSLLNES--EGKNTKSS----KDMLSLESHLQDTQELLQEETRQKLAIS-------T 1326
Cdd:pfam05557 157 NLEKQQSSLAEAEQRIK-ELEFEIQSQEQDseIVKNSKSElariPELEKELERLREHNKHLNENIENKLLLKeevedlkR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1327 RFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMD----------------QEVSSLESA----EESRKR 1386
Cdd:pfam05557 236 KLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlsrrieqlqqreivlkEENSSLTSSarqlEKARRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1387 LQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNmerkqrkFDQMLAEEKTiSTQYAEERDKAEa 1466
Cdd:pfam05557 316 LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILES-------YDKELTMSNY-SPQLLERIEEAE- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1467 eareketraltlarelETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKR--------ATEQQLEEIKTQL 1538
Cdd:pfam05557 387 ----------------DMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQqesladpsYSKEEVDSLRRKL 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1539 EELEDELQATEDAKLRLEVNMQAMKAQFDRD------LQARDEQGEERRKQLVKQVHELEAELEDERR 1600
Cdd:pfam05557 451 ETLELERQRLREQKNELEMELERRCLQGDYDpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKR 518
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1355-1578 |
1.47e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1355 QISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLlvnQDGLRQLVN 1434
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---REELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1435 NMERKQRKFD--QMLAEEKTISTQYaeerdkaeaearekeTRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDD 1512
Cdd:COG3883 94 ALYRSGGSVSylDVLLGSESFSDFL---------------DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768942001 1513 AGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGE 1578
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1363-1922 |
1.93e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1363 LGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRK 1442
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1443 FDQMLAEEKTISTQYAEERDK----AEAEAREKETRALTLARELETITD---LKNELERTNKQLKaEMEDLVSSKDDAGK 1515
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKnnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILS-NIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1516 NVHELErskrATEQQLEEIKTQLEELE---DELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQvhelE 1592
Cdd:PRK01156 330 KLSVLQ----KDYNDYIKKKSRYDDLNnqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ----E 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1593 AELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFK----DMMRESEDLRLSRDEAINSAKET 1668
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1669 EKKVKTMEADAAQFQEDLATAERLKRQMQAErdelqdEINGNNTKNSMLQDEKRRLEaritqleeeleeeqlnsemaNDR 1748
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEYLESE------EINKSINEYNKIESARADLE--------------------DIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1749 NKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLK-------LQELESTIKSKYK---SSLTALEAKVAQLEE 1818
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIslidietNRSRSNEIKKQLNdleSRLQEIEIGFPDDKS 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1819 QLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQR--- 1895
Cdd:PRK01156 616 YIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDaka 695
|
570 580 590
....*....|....*....|....*....|
gi 768942001 1896 ---ELEDANETQDTMNREVNILKSKLRRDL 1922
Cdd:PRK01156 696 nraRLESTIEILRTRINELSDRINDINETL 725
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1057-1697 |
1.96e-07 |
|
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: 56.37 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1057 LHDQIADLQAQIADLRAQLANKEEELQnalirieeeaaANMASQKKIkeleaqileLDEDLEREKFYRSKNGQRCKELEK 1136
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLG-----------SSMNSIKTF---------WSPELKKERALRKEEAARISVLKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1137 ELEAIKNKLDD-TLDTTAAQQELRAKRE---------------TEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNE 1200
Cdd:pfam10174 61 QYRVTQEENQHlQLTIQALQDELRAQRDlnqllqqdfttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1201 QLEqakrnkLSVEKAKQALESEFNELQ-----IELKTLGQSKSDSEHRRKK----AESQVQELQVKYGDCERQRQEAVEK 1271
Cdd:pfam10174 141 EME------LRIETQKQTLGARDESIKkllemLQSKGLPKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1272 IAK---LQSELENVNSLLNESEGKNTKSSkdmlSLESHLQDTQELLQ--------------EETRQKLAISTRFRQMEEE 1334
Cdd:pfam10174 215 LHRrnqLQPDPAKTKALQTVIEMKDTKIS----SLERNIRDLEDEVQmlktngllhtedreEEIKQMEVYKSHSKFMKNK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1335 QNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTR 1414
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1415 LQQELDDLLVNQDGLRQLVNNMERK----QRKFDQMLAEEKTISTQYAEERDKAEAEAREKET--RALT-----LARELE 1483
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdTALTtleeaLSEKER 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1484 TITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMK 1563
Cdd:pfam10174 451 IIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1564 AQFDR---DLQARDEQGEERRK--QLVKQVHELEAELEderRQRSQAVSAKKKLELDLGEL-EVHIDAANKgrDEALKQL 1637
Cdd:pfam10174 531 EECSKlenQLKKAHNAEEAVRTnpEINDRIRLLEQEVA---RYKEESGKAQAEVERLLGILrEVENEKNDK--DKKIAEL 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1638 KKLQV-QFKDMMRESEDLRLSRDEainsaketEKKVKTMEADAAQFQEDLATAERLKRQMQ 1697
Cdd:pfam10174 606 ESLTLrQMKEQNKKVANIKHGQQE--------MKKKGAQLLEEARRREDNLADNSQQLQLE 658
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1193-1902 |
2.31e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1193 QAFNEMNEQLeQAKRNKLSVEKAKQALESEFNELqIELKT--------------LGQSKSDSEHRRKKAESQVQ--ELQV 1256
Cdd:PRK04863 230 KAFQDMEAAL-RENRMTLEAIRVTQSDRDLFKHL-ITESTnyvaadymrhanerRVHLEEALELRRELYTSRRQlaAEQY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1257 KYGDCERQRQEAVEKIAKLQSELENVNSLLN------ESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQ 1330
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1331 MEEEQNSLRemleeeeeakknvekqisvlqGQLGDMKKKMD----------QEVSSLESAE----------ESRKRLQRE 1390
Cdd:PRK04863 388 AEEEVDELK---------------------SQLADYQQALDvqqtraiqyqQAVQALERAKqlcglpdltaDNAEDWLEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1391 F-------DTVKLQLEEK-----------EAAYEKLE---------------RTKTRLQQELDDLLVNQDGLRQLVNNME 1437
Cdd:PRK04863 447 FqakeqeaTEELLSLEQKlsvaqaahsqfEQAYQLVRkiagevsrseawdvaRELLRRLREQRHLAEQLQQLRMRLSELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1438 R---KQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSK---- 1510
Cdd:PRK04863 527 QrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawl 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1511 --DDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDaklRLEVNMQAMKAQFDRdLQARDEQGEERRKQLVKQV 1588
Cdd:PRK04863 607 aaQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLNALAERF 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1589 H-ELEAEL-EDERRQRSQAVSAKkkleldLGELEVHIDAANKGRdeALKQLKKLQvqfkDMmreSEDLRL------SRDE 1660
Cdd:PRK04863 683 GgVLLSEIyDDVSLEDAPYFSAL------YGPARHAIVVPDLSD--AAEQLAGLE----DC---PEDLYLiegdpdSFDD 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1661 AINSAKETEKKVKTMEADAA----QFQED--LATAERLKR--QMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLE 1732
Cdd:PRK04863 748 SVFSVEELEKAVVVKIADRQwrysRFPEVplFGRAAREKRieQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1733 EELEEEQLNSEMANDRNKRTTLQvDQLTAELSAERSAAQRLEGARSQAERKNK---ELSL--------KLQELESTIKS- 1800
Cdd:PRK04863 828 AVAFEADPEAELRQLNRRRVELE-RALADHESQEQQQRSQLEQAKEGLSALNRllpRLNLladetladRVEEIREQLDEa 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1801 --------KYKSSLTALEAKVAQL---EEQLDTEIKERQQATRMVRRTEKK---MKELVlqvedERRNTEQYKDQADKLN 1866
Cdd:PRK04863 907 eeakrfvqQHGNALAQLEPIVSVLqsdPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVV-----QRRAHFSYEDAAEMLA 981
|
810 820 830
....*....|....*....|....*....|....*....
gi 768942001 1867 SRTR---QLKRQLEEAEEEVTRANAYRRKLQRELEDANE 1902
Cdd:PRK04863 982 KNSDlneKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
841-1125 |
2.59e-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: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQ---LNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEE----- 912
Cdd:pfam19220 100 REAEAAKEELRIELRDKTAQAEALERQLAAETEQnraLEEENKALREEAQAAEKALQRAEGELATARERLALLEQenrrl 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 913 --ILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKA-LEGNIMVLDDQNNKLNK 989
Cdd:pfam19220 180 qaLSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAeRASLRMKLEALTARAAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 990 EKKL-------LEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRlrkeEKQRQELEKNRRKLEGDSTDLHDQIA 1062
Cdd:pfam19220 260 TEQLlaearnqLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERR----TQQFQEMQRARAELEERAEMLTKALA 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1063 DLQAQIADLRAQLANKEEELQNALIRIEEEAAAnmasqkkikeLEAQILELDEDLEREKFYRS 1125
Cdd:pfam19220 336 AKDAALERAEERIASLSDRIAELTKRFEVERAA----------LEQANRRLKEELQRERAERA 388
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1219-1803 |
2.85e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1219 LESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYgdcerqrQEAVEKIAKLQSELENVNSLLNESEGKNTKSSK 1298
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY-------NNAMDDYNNLKSALNELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1299 DMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREmleeeeeakknvekqisvLQGQLGDMKKKMDQEVSSLE 1378
Cdd:PRK01156 261 AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFK------------------YKNDIENKKQILSNIDAEIN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1379 SAEESRKRLQrefdtvklQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYA 1458
Cdd:PRK01156 323 KYHAIIKKLS--------VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1459 EERDKAEAEAREketraltLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHEL---------------ERS 1523
Cdd:PRK01156 395 EILKIQEIDPDA-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1524 KRATEQQLEE---IKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLvKQVHELEAELEDERR 1600
Cdd:PRK01156 468 NHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADL-EDIKIKINELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1601 QRSQAVSAKKklELDLGELE---------------VHIDAANKGRDEALKQLKKLQVQFKDMMRESEDlrlsrdeaINSA 1665
Cdd:PRK01156 547 KYEEIKNRYK--SLKLEDLDskrtswlnalavislIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD--------DKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1666 keTEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDeINGNNTKNSMLQDEKRRLEARITQleeeleeeqlnsemA 1745
Cdd:PRK01156 617 --IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN-YKKQIAEIDSIIPDLKEITSRIND--------------I 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1746 NDRNKRTTLQVDQLTAELSAERSAAQRLegarsqaERKNKELSLKLQELESTIKSKYK 1803
Cdd:PRK01156 680 EDNLKKSRKALDDAKANRARLESTIEIL-------RTRINELSDRINDINETLESMKK 730
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1368-1728 |
3.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1368 KKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDgLRQLVNNMERKQRKFDQML 1447
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1448 AEEKTIStQYAEERDKAEAEAREKETraltlareletitDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRAT 1527
Cdd:COG4717 153 ERLEELR-ELEEELEELEAELAELQE-------------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1528 EQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQ------------------LVKQVH 1589
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1590 ELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETE 1669
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1670 KKVKTMEA------DAAQFQEDLATAERLKRQ-------------------MQAERDELQDEINGNNTKNSMLQDEKRRL 1724
Cdd:COG4717 379 AGVEDEEElraaleQAEEYQELKEELEELEEQleellgeleellealdeeeLEEELEELEEELEELEEELEELREELAEL 458
|
....
gi 768942001 1725 EARI 1728
Cdd:COG4717 459 EAEL 462
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1375-1704 |
4.31e-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: 54.90 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1375 SSLESAEESRKRLQREFDTVKLQLEEKEAAY----EKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRkfdqmlaEE 1450
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYkrdrEQWERQRRELESRVAELKEELRQSREKHEELEEKYK-------EL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1451 KTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKaemedlvsskddagknvhelERSKRATEQQ 1530
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK--------------------ERAKKAGAQR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1531 LEEiKTQLEELEDELQATEDAKLRLEVNMQAMK-AQFDRDLQARDEQGE-ERRKQLVKQVH----ELEAELEDERRQRSQ 1604
Cdd:pfam07888 167 KEE-EAERKQLQAKLQQTEEELRSLSKEFQELRnSLAQRDTQVLQLQDTiTTLTQKLTTAHrkeaENEALLEELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1605 AVSAKKKLELDLGELEVHIDAankgRDEALKQLKKLQVQFKDMMRESEDLRLS-RDEAINSAKETEKKVKTMEADAAQFQ 1683
Cdd:pfam07888 246 LNASERKVEGLGEELSSMAAQ----RDRTQAELHQARLQAAQLTLQLADASLAlREGRARWAQERETLQQSAEADKDRIE 321
|
330 340
....*....|....*....|.
gi 768942001 1684 EDLATAERLKRQMQAERDELQ 1704
Cdd:pfam07888 322 KLSAELQRLEERLQEERMERE 342
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1093-1327 |
5.21e-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: 54.00 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1093 AAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKA 1172
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1173 QEEENKMHESQIAELSKKHLQAFNEM---NEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLgqsksdsEHRRKKAES 1249
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-------AALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1250 QVQELqvkygdcERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAISTR 1327
Cdd:COG4942 172 ERAEL-------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1497-1728 |
5.59e-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: 54.00 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1497 KQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEdaklrlevnmqamkaqfdrdlqARDEQ 1576
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE----------------------QELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1577 GEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLElDLGELEVHIDAANKgrDEALKQLKKLQVQFKDMMRESEDLRL 1656
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1657 SRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARI 1728
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
841-1661 |
5.69e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKE--DELSKVKEKQLQAEEMIKEFESK----QQQLNA-EKMALQEQ-----LQAETELC-------AEAEEMRA 901
Cdd:PRK04863 366 EQNEVVEEadEQQEENEARAEAAEEEVDELKSQladyQQALDVqQTRAIQYQqavqaLERAKQLCglpdltaDNAEDWLE 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 902 RLVNRKQELEEILHDMESRLeeeeeRVNQMLNER--KKMQ--QNIADleqQLDEEEADRQKLQMEKVTTDSKMKA--LEG 975
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKL-----SVAQAAHSQfeQAYQlvRKIAG---EVSRSEAWDVARELLRRLREQRHLAeqLQQ 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 976 NIMVLDDQNNKLNKEKKLlEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRqeleknrrklegdsT 1055
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRA-ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR--------------M 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1056 DLHDQIADLQAQIADLRAQlANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREkfyRSKNGQRCKELE 1135
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE---RDELAARKQALD 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1136 KELEAIKNK---LDDTLDTTAAQ--QELRAKRETEVAqLRKAQEEENK----MHESQIAELS--KKHLQAFNEMNEQL-- 1202
Cdd:PRK04863 659 EEIERLSQPggsEDPRLNALAERfgGVLLSEIYDDVS-LEDAPYFSALygpaRHAIVVPDLSdaAEQLAGLEDCPEDLyl 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1203 -----EQAKRNKLSVEKAKQALESEFNELQielktLGQSKSDSEHR--RKKAESQVQELQvkygdceRQRQEAVEKIAKL 1275
Cdd:PRK04863 738 iegdpDSFDDSVFSVEELEKAVVVKIADRQ-----WRYSRFPEVPLfgRAAREKRIEQLR-------AEREELAERYATL 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1276 QSELENVNSL---LNESEGKNtksskdmLSLESHLQDTQELlqEETRQKLaistrfRQMEEEQNSLREMLEEEEEAKKNV 1352
Cdd:PRK04863 806 SFDVQKLQRLhqaFSRFIGSH-------LAVAFEADPEAEL--RQLNRRR------VELERALADHESQEQQQRSQLEQA 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1353 EKQISVLQGQLGDMK-----------KKMDQEVSSLESAEESRKRLQREFDTVK----------LQLEEKEAAYEKLERT 1411
Cdd:PRK04863 871 KEGLSALNRLLPRLNlladetladrvEEIREQLDEAEEAKRFVQQHGNALAQLEpivsvlqsdpEQFEQLKQDYQQAQQT 950
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1412 KTRLQQELDDLlvnqDGLRQLVNNMERKQRKfdQMLAEEKTISTQYAEERDKAEAEAREKETRAltlareletitdlkne 1491
Cdd:PRK04863 951 QRDAKQQAFAL----TEVVQRRAHFSYEDAA--EMLAKNSDLNEKLRQRLEQAEQERTRAREQL---------------- 1008
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1492 lertnKQLKAEMedlvsskDDAGKNVHELERSKRATEQQLEEIKTQLEELedELQATEDAklrlevnmqAMKAQFDRD-L 1570
Cdd:PRK04863 1009 -----RQAQAQL-------AQYNQVLASLKSSYDAKRQMLQELKQELQDL--GVPADSGA---------EERARARRDeL 1065
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1571 QARDEQGEERRKQLVKQVHELEAELEDERRQrsqavsaKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRE 1650
Cdd:PRK04863 1066 HARLSANRSRRNQLEKQLTFCEAEMDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRE 1138
|
890
....*....|....*.
gi 768942001 1651 -----SEDLRLSRDEA 1661
Cdd:PRK04863 1139 laylsADELRSMSDKA 1154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1669-1920 |
7.77e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1669 EKKVKTMEaDAAQFQEDLATAERLKRQMQAERDELQDEINgNNTKNSMLQDEKRRLEARItqleeeleeeQLNSEMANDR 1748
Cdd:TIGR02169 170 RKKEKALE-ELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYE----------LLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1749 NKRTTL-QVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKVAQLEEQLDTEIKER 1827
Cdd:TIGR02169 238 QKEAIErQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1828 QQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLE----EAEEEVTRANAYRRKL---QRELEDA 1900
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraELEEVDKEFAETRDELkdyREKLEKL 397
|
250 260
....*....|....*....|
gi 768942001 1901 NETQDTMNREVNILKSKLRR 1920
Cdd:TIGR02169 398 KREINELKRELDRLQEELQR 417
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1051-1253 |
8.06e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1051 EGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLER-----EKFYRS 1125
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1126 --KNGQRCKELEKELEAikNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEE-ENKmhESQIAELSKKHLQAFNEMNEQL 1202
Cdd:COG3883 95 lyRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAElEAK--KAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1203 EQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQE 1253
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1183-1458 |
8.75e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1183 QIAELSKKHLQAFNEMNEQLEQAkrnklSVEKAKQALESEFNELQIELKtlgqsksdsehrrkKAESQVQELQVKYG--D 1260
Cdd:COG3206 149 LAAAVANALAEAYLEQNLELRRE-----EARKALEFLEEQLPELRKELE--------------EAEAALEEFRQKNGlvD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1261 CERQRQEAVEKIAKLQSELENVNSLLNESEGKntksskdMLSLESHLQDTQELLQEetrqkLAISTRFRQMEEEQNSLRE 1340
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEAR-------LAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1341 mleeeeeakknvekQISVLQGQLGD----MKKkMDQEVSSLEsaEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQ 1416
Cdd:COG3206 278 --------------ELAELSARYTPnhpdVIA-LRAQIAALR--AQLQQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 768942001 1417 QELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYA 1458
Cdd:COG3206 341 ARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
836-1188 |
9.23e-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: 53.98 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETEL---CAEAEEMRARLVNRKQELEE 912
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 913 IlHDMES---RLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQK---LQMEKVTTDSKMKALEGNIMvldDQNNK 986
Cdd:pfam05557 199 I-PELEKeleRLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaatLELEKEKLEQELQSWVKLAQ---DTGLN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 987 LNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKhEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQA 1066
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQL-EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1067 QIADLRAQLANKEEELQNA------LIRIEEEAAANMASQKKIKELEAQILELDEDLEREKfyrskngQRCKELEKELEA 1140
Cdd:pfam05557 354 ERDGYRAILESYDKELTMSnyspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYK-------QQAQTLERELQA 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 768942001 1141 IK--NKLDDTLDTTAAQQELRAKRETEVAQlRKAQEEENKMHESQIAELS 1188
Cdd:pfam05557 427 LRqqESLADPSYSKEEVDSLRRKLETLELE-RQRLREQKNELEMELERRC 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
841-1078 |
9.94e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQA----ETELCAEAEEMRARLVNRKQELEEILHD 916
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAlqaeIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 917 MeSRLEEEEERVNQMLNerkkmQQNIADLEQQLD--EEEADRQKLQMEKVTTDSKmkalegnimvlddqnnKLNKEKKLL 994
Cdd:COG3883 95 L-YRSGGSVSYLDVLLG-----SESFSDFLDRLSalSKIADADADLLEELKADKA----------------ELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 995 EDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQ 1074
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....
gi 768942001 1075 LANK 1078
Cdd:COG3883 233 AAAA 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
865-1125 |
1.15e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 865 IKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQEL-EEILHDMESrleeeeervNQMLNERkkMQQNIA 943
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKyDELVEEAKT---------IKAEIEE--LTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 944 DLEQQLDEEEADRQKLQMEKVTTDSKMKalegnimvlddqnnKLNKEKKLLEDR--IAEFSSNLSEEEEKsrsLQKLKNK 1021
Cdd:PHA02562 245 NLVMDIEDPSAALNKLNTAAAKIKSKIE--------------QFQKVIKMYEKGgvCPTCTQQISEGPDR---ITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1022 heaiITDLEDRLRKEEKQRQELEknrrKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQK 1101
Cdd:PHA02562 308 ----LKELQHSLEKLDTAIDELE----EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
250 260
....*....|....*....|....*..
gi 768942001 1102 KIKELEAQILELDE---DLEREKFYRS 1125
Cdd:PHA02562 380 ELAKLQDELDKIVKtksELVKEKYHRG 406
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
841-1845 |
1.24e-06 |
|
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: 53.90 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKEDELSK-VKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEmrarlvNRKQELEEILHDMES 919
Cdd:TIGR01612 670 EDDIDALYNELSSiVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIE------NKKNELLDIIVEIKK 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 920 RLEeeeervNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIA 999
Cdd:TIGR01612 744 HIH------GEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSK 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1000 EFSSNLS-EEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAqlaNK 1078
Cdd:TIGR01612 818 EYIKTISiKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKF---ND 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1079 EEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLERekfYRSKNGQRCKELEKELEAIKNklddtldTTAAQQEL 1158
Cdd:TIGR01612 895 SKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEK---FHNKQNILKEILNKNIDTIKE-------SNLIEKSY 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1159 RAKRETEVaqLRKAQEEENKMHESQIAELSKKH---LQAFNEMNEQLEQAKRNklsvekakqALESEFNELQielktlgQ 1235
Cdd:TIGR01612 965 KDKFDNTL--IDKINELDKAFKDASLNDYEAKNnelIKYFNDLKANLGKNKEN---------MLYHQFDEKE-------K 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1236 SKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSL---------LNESEGKNTKSSKDMLSLESH 1306
Cdd:TIGR01612 1027 ATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILeeaeinitnFNEIKEKLKHYNFDDFGKEEN 1106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1307 LQDTQELlqeeTRQKLAISTRFRQMEEEQNSLremleeeEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSlesaeESRKR 1386
Cdd:TIGR01612 1107 IKYADEI----NKIKDDIKNLDQKIDHHIKAL-------EEIKKKSENYIDEIKAQINDLEDVADKAISN-----DDPEE 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1387 LQREFDTVKLQLEEKEAAYE----------KLERTKTRLQ----------QELDDLLVNQ-----DGLRQLVNNMERKQR 1441
Cdd:TIGR01612 1171 IEKKIENIVTKIDKKKNIYDeikkllneiaEIEKDKTSLEevkginlsygKNLGKLFLEKideekKKSEHMIKAMEAYIE 1250
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1442 KFDQMLAEEKTISTQYAEERD-KAEAEA-------------------------REKETRALTLARELETITDLKNELER- 1494
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEMGIEMDiKAEMETfnishdddkdhhiiskkhdenisdiREKSLKIIEDFSEESDINDIKKELQKn 1330
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1495 -TNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLE---EIKTQLEELEDELQATED--AKLRLEVNMQAMKAQFDR 1568
Cdd:TIGR01612 1331 lLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEytkEIEENNKNIKDELDKSEKliKKIKDDINLEECKSKIES 1410
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1569 DLQARDEQG---------------EERRKQLVKQVHELEA---------ELEDERRQ---RSQAVSAKKKLELDLGELEV 1621
Cdd:TIGR01612 1411 TLDDKDIDEcikkikelknhilseESNIDTYFKNADENNEnvlllfkniEMADNKSQhilKIKKDNATNDHDFNINELKE 1490
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1622 HIDAANKGRDEA---LKQLKKLQVQFKDMMRESEDLrLSRDEAI-------NSAKETEKKVKTMEADAAQFQEDLATAER 1691
Cdd:TIGR01612 1491 HIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEL-LNKYSALaiknkfaKTKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1692 LKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEA------RITQLEEELEEEQLNSEmaNDRNKRTTLQVDQLTAELSA 1765
Cdd:TIGR01612 1570 KIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLKETE--SIEKKISSFSIDSQDTELKE 1647
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1766 ERSAAQRLEGARSQAERKNKELSLKLQELEStIKSKYKSsltaLEAKVAQLEEQLDTEIKERQQATRMVRRTE-KKMKEL 1844
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKNIEDKKKELDE-LDSEIEK----IEIDVDQHKKNYEIGIIEKIKEIAIANKEEiESIKEL 1722
|
.
gi 768942001 1845 V 1845
Cdd:TIGR01612 1723 I 1723
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1038-1728 |
1.39e-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: 53.80 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1038 KQRQELEKNRRKLegdsTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAAnMASQKKIKELEAQILELDEDL 1117
Cdd:COG3096 289 ELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTA-LRQQEKIERYQEDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1118 EREKFY-------RSKNGQRCKELEKELEAIKNKLDD---TLDT--TAA---QQELRAKRETE----------------V 1166
Cdd:COG3096 364 EEQEEVveeaaeqLAEAEARLEAAEEEVDSLKSQLADyqqALDVqqTRAiqyQQAVQALEKARalcglpdltpenaedyL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1167 AQLRKAQEE--------ENKMHESQIA--------ELSKK------HLQAFNEMNEQLEQAKRNKLSVEKAkQALESEFN 1224
Cdd:COG3096 444 AAFRAKEQQateevlelEQKLSVADAArrqfekayELVCKiageveRSQAWQTARELLRRYRSQQALAQRL-QQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1225 ELQIEL----------KTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNT 1294
Cdd:COG3096 523 ELEQRLrqqqnaerllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1295 KSSKdmlsleshLQDTQELLQEETRQKLAIS---TRFRQMEEEQnslremleeeeeakknvEKQISVLQGQLGDMKKKMD 1371
Cdd:COG3096 603 AWLA--------AQDALERLREQSGEALADSqevTAAMQQLLER-----------------EREATVERDELAARKQALE 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1372 QEVSSLESAEESrkrlqreFDTVKLQLEEK----------------EAAY--------------EKLERTKTRLQ----- 1416
Cdd:COG3096 658 SQIERLSQPGGA-------EDPRLLALAERlggvllseiyddvtleDAPYfsalygparhaivvPDLSAVKEQLAgledc 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1417 ---------------------QELDDLLVNQDGLRQL-------VNNMERKQR--KFDQMLAEEKTISTQYAE---ERDK 1463
Cdd:COG3096 731 pedlyliegdpdsfddsvfdaEELEDAVVVKLSDRQWrysrfpeVPLFGRAARekRLEELRAERDELAEQYAKasfDVQK 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1464 ----------------AEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRAT 1527
Cdd:COG3096 811 lqrlhqafsqfvgghlAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADET 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1528 -EQQLEEIKTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFDRdLQARDEQGEERRKQLVKQVHELEaeledERR 1600
Cdd:COG3096 891 lADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVV 964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1601 QRSQAVSAKKKLEL-----DLGE-LEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKT 1674
Cdd:COG3096 965 QRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1675 MEADAAQFQEDLAtaerlkrqmQAERDELQDEINGNNTKNSMLQDEKRRLEARI 1728
Cdd:COG3096 1045 LGVQADAEAEERA---------RIRRDELHEELSQNRSRRSQLEKQLTRCEAEM 1089
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1753-1907 |
1.77e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1753 TLQVDQLTAELSAERSAAQ-RLEGARSQAERKNKELSLKLQELESTIKSkykSSLTALEAKVAQLEEQLDTEIKERQQAT 1831
Cdd:COG3206 214 AKLLLQQLSELESQLAEARaELAEAEARLAALRAQLGSGPDALPELLQS---PVIQQLRAQLAELEAELAELSARYTPNH 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1832 RMVRRTEKKMKELVLQVEDE-RRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRK---LQRELEDANETQDTM 1907
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARELYESL 370
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
967-1125 |
1.84e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.28 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 967 DSKMKALEGNIMVLDDQNNkLNKEKKL-LEDRIAEFSSNLSEEE-EKSRsLQKLKNKHEAIITDLEdrlrkeeKQRQELE 1044
Cdd:PRK09039 52 DSALDRLNSQIAELADLLS-LERQGNQdLQDSVANLRASLSAAEaERSR-LQALLAELAGAGAAAE-------GRAGELA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1045 KNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQnalirieeeaaanmASQKKIKELEAQILELD---------- 1114
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD--------------ASEKRDRESQAKIADLGrrlnvalaqr 188
|
170
....*....|..
gi 768942001 1115 -EDLERekfYRS 1125
Cdd:PRK09039 189 vQELNR---YRS 197
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1561-1708 |
2.10e-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: 51.08 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1561 AMKAQFDR--DLQARD---EQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALK 1635
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1636 QLKKL--QVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEIN 1708
Cdd:COG1579 81 QLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
901-1053 |
2.10e-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: 51.08 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 901 ARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKL--QMEKVTTDSKMKALEGNIM 978
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 979 VLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKsrsLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGD 1053
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1213-1442 |
2.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1213 EKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGK 1292
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1293 ntksskdmlsLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQ 1372
Cdd:COG4942 106 ----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1373 EVSSLESAEESRKRLQRefdtvklQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRK 1442
Cdd:COG4942 176 LEALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1035-1363 |
2.32e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1035 KEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNAlirieeeaaanmasqkkikeleaqileld 1114
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQA----------------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1115 edlerekfyrskngqrckelEKELEAIKNKLDDTLDTTAAQQELR------AKRETEVAQLRKAQEEENkmheSQIAELS 1188
Cdd:PRK11281 100 --------------------QAELEALKDDNDEETRETLSTLSLRqlesrlAQTLDQLQNAQNDLAEYN----SQLVSLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1189 KKHLQAFNEM--NEQLEQAKRNKLSVEKA--KQALESEFNELQIELKTLGQSksdSEHRRKKAESQVQeLQVKYgdcERQ 1264
Cdd:PRK11281 156 TQPERAQAALyaNSQRLQQIRNLLKGGKVggKALRPSQRVLLQAEQALLNAQ---NDLQRKSLEGNTQ-LQDLL---QKQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1265 RQEAVEKIAKLQSELENVNSLLNEsegKNTKSSKDMLSLESHLQDTQE-----LLQEETRQKLAISTRFRQMEEEQNSL- 1338
Cdd:PRK11281 229 RDYLTARIQRLEHQLQLLQEAINS---KRLTLSEKTVQEAQSQDEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLt 305
|
330 340 350
....*....|....*....|....*....|.
gi 768942001 1339 ------REMLEEEEEAKKNVEKQISVLQGQL 1363
Cdd:PRK11281 306 qqnlrvKNWLDRLTQSERNIKEQISVLKGSL 336
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
835-1049 |
2.44e-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: 52.82 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 835 LQVTRQEEemlaKEDELSKVKEKQLQAE-EMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEI 913
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 914 -----------LHDMESRLEEEEERVNQMLNERkkmQQNIADLEQQldEEEADRQKLQMEKVTTDSKMkalegnimvLDD 982
Cdd:pfam17380 426 raeqeearqreVRRLEEERAREMERVRLEEQER---QQQVERLRQQ--EEERKRKKLELEKEKRDRKR---------AEE 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 983 QNnklnkeKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRK 1049
Cdd:pfam17380 492 QR------RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1247-1475 |
2.48e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1247 AESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEetrQKLAIST 1326
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1327 RFRQMEEEQNSLremleeeeeakknveKQISVLQGQlgdmkkkmdqevSSLESAEESRKRLQREFDTVKLQLEEKEAAYE 1406
Cdd:COG3883 91 RARALYRSGGSV---------------SYLDVLLGS------------ESFSDFLDRLSALSKIADADADLLEELKADKA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1407 KLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRA 1475
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1093-1922 |
2.97e-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: 52.65 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1093 AAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIknklddtldtTAAQQELRAKRETEVAQLRKA 1172
Cdd:COG3096 270 AADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEEL----------SARESDLEQDYQAASDHLNLV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1173 QE-----EENKMHESQIAELSKKhlqaFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLgQSKSDSEHRRKka 1247
Cdd:COG3096 340 QTalrqqEKIERYQEDLEELTER----LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-QQALDVQQTRA-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1248 esqvqelqVKYgdceRQRQEAVEKiAKLQSEL-----ENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQE-----E 1317
Cdd:COG3096 413 --------IQY----QQAVQALEK-ARALCGLpdltpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQfekayE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1318 TRQKLAIST-RFRQMEEEQNSLREMLEEEEEAKknvekQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQRE---FDT 1393
Cdd:COG3096 480 LVCKIAGEVeRSQAWQTARELLRRYRSQQALAQ-----RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaAEE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1394 VKLQLEEKEAAYEKLERT-------KTRLQQELDDL--------------LVNQDGLRQL-------VNNMERKQRKFDQ 1445
Cdd:COG3096 555 LEELLAELEAQLEELEEQaaeaveqRSELRQQLEQLrarikelaarapawLAAQDALERLreqsgeaLADSQEVTAAMQQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1446 MLAEEKTIST---QYAEERDKAEAEARE-------KETRALTLAREL---------ETIT------------DLKN---- 1490
Cdd:COG3096 635 LLEREREATVerdELAARKQALESQIERlsqpggaEDPRLLALAERLggvllseiyDDVTledapyfsalygPARHaivv 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1491 -ELERTNKQLKAE---MEDL------VSSKDDAGKNVHELERS----------------------KRATEQQLEEIKTQL 1538
Cdd:COG3096 715 pDLSAVKEQLAGLedcPEDLyliegdPDSFDDSVFDAEELEDAvvvklsdrqwrysrfpevplfgRAAREKRLEELRAER 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1539 EELEDELqatedAKLRLEVN-MQAMKAQFDRDL-----QARDEQGEERRKQLVKQVHELEAELED----ERRQRSQAVSA 1608
Cdd:COG3096 795 DELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELAQhraqEQQLRQQLDQL 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1609 KkkleldlgelevhidaankgrdEALKQLKKLQVQF-----KDMMRESEDLRLSRDEAI----------NSAKETEKKVK 1673
Cdd:COG3096 870 K----------------------EQLQLLNKLLPQAnlladETLADRLEELREELDAAQeaqafiqqhgKALAQLEPLVA 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1674 TMEADAAQF---QEDLATAERLKRQMQAERDELqDEINGNNTKNSMlQDEKRRLEAritqleeeleeeqlNSEMandrnk 1750
Cdd:COG3096 928 VLQSDPEQFeqlQADYLQAKEQQRRLKQQIFAL-SEVVQRRPHFSY-EDAVGLLGE--------------NSDL------ 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1751 rttlqVDQLTAEL----SAERSAAQRLEGARSQAERKNKElslkLQELESTIKSKYKsSLTALEAKVAQLEEQLDTEIKE 1826
Cdd:COG3096 986 -----NEKLRARLeqaeEARREAREQLRQAQAQYSQYNQV----LASLKSSRDAKQQ-TLQELEQELEELGVQADAEAEE 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1827 RQQAtrmvRRTEKKMKelvLQVEDERRNteQYKDQADKLNSRTRQLKRQLEEAEEEVTranayrrKLQRELEDANETQDT 1906
Cdd:COG3096 1056 RARI----RRDELHEE---LSQNRSRRS--QLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKAGWCA 1119
|
970
....*....|....*....
gi 768942001 1907 ---MNREVNILKSKLRRDL 1922
Cdd:COG3096 1120 vlrLARDNDVERRLHRREL 1138
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
847-1217 |
3.16e-06 |
|
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: 52.42 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 847 KEDELSKVKEKQLQAEEMI---KEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLEE 923
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLdekKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 924 EEER-------VNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLED 996
Cdd:pfam05483 483 EKLKnieltahCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 997 riaEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDR---LRKE----EKQRQELEKNRRKLEGDSTDLHDQIADLQAQIA 1069
Cdd:pfam05483 563 ---EVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnLKKQienkNKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1070 DLRAQLANKEEELQNALIRIEEEAAANMASQKK-IKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDT 1148
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKI 719
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1149 LDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELsKKHLQAFNEMNEQLEQAKRNKLSVEKAKQ 1217
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL-KKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
836-1178 |
3.48e-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: 51.82 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQEleeilh 915
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 916 dMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLE 995
Cdd:pfam07888 148 -RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 996 DRIAEFSSNLSEeeekSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQL 1075
Cdd:pfam07888 227 RKEAENEALLEE----LRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1076 ANKEEELQNALirieeeaaanMASQKKIKELEAQILELDEDLEREKFYRSKngqrckeLEKELEAIKN-KLDDTLDTTAA 1154
Cdd:pfam07888 303 AQERETLQQSA----------EADKDRIEKLSAELQRLEERLQEERMEREK-------LEVELGREKDcNRVQLSESRRE 365
|
330 340
....*....|....*....|....
gi 768942001 1155 QQELRAkrETEVAQLRKAQEEENK 1178
Cdd:pfam07888 366 LQELKA--SLRVAQKEKEQLQAEK 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
836-1014 |
4.16e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQL------------QAETELCAEAEEMrARL 903
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgrQPPLALLLSPEDF-LDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 904 VNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQ 983
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
170 180 190
....*....|....*....|....*....|.
gi 768942001 984 NNKLNKEKKLLEDRIAEFSSNLSEEEEKSRS 1014
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1679-1908 |
4.27e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1679 AAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQ 1758
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1759 LTAELSAERSAAQRLEGARSQAERKNKELSLKLQE--LESTIKSKYkssLTALEAKVAQLEEQLDTEIKERQQATRMVRR 1836
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQY---LKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768942001 1837 TEKKMKELVLQVEDERRNTEQYKDQ----ADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMN 1908
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1059-1280 |
4.90e-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: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1059 DQIADLQAQIADLRAQLANKEEELQNAlirieeeaaanmasQKKIKELEAQILELDEDLErekfyrskngqrckELEKEL 1138
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDAL--------------QAELEELNEEYNELQAELE--------------ALQAEI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1139 EAIKNKLDdtldttAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSK------KHLQAFNEMNEQ----LEQAKRN 1208
Cdd:COG3883 68 DKLQAEIA------EAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIADAdadlLEELKAD 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1209 KLSVEKAKQALESEFNELQIELKTLgqsksdsEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELE 1280
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAEL-------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1481-1899 |
5.28e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1481 ELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQ---LEEIKTQLEELEDELQATEDAKLRLEV 1557
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDeksHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1558 NMQAMKAQFD--RDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAK----------KKLELDLGELEVHIDA 1625
Cdd:PRK01156 240 ALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNrnyindyfkyKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1626 ANKGRDEALKQLKKLQV---QFKDMMRESEDLRLSRDE----------AINSAKETEKKV----KTMEADAAQFQEDLAT 1688
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKdynDYIKKKSRYDDLNNQILElegyemdynsYLKSIESLKKKIeeysKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1689 AERLKRQMQAERDELQDEINGNNTKNSMLQdekrrleARITQLEEELEEEQLNSEMANDRNK----RTTLQ-------VD 1757
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLN-------QRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGeeksnhiIN 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1758 QLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTALEAKVAQLEeqlDTEIKERQQATRMVRRT 1837
Cdd:PRK01156 473 HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLE---DIKIKINELKDKHDKYE 549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1838 EKKMKELVLQVEDERRNTEQY---------------KDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELED 1899
Cdd:PRK01156 550 EIKNRYKSLKLEDLDSKRTSWlnalavislidietnRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
980-1229 |
6.62e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 980 LDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKsrsLQKLKNKHEaiITDLEDRLRKEEKQRQELEknrrklegdstdlhD 1059
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNG--LVDLSEEAKLLLQQLSELE--------------S 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1060 QIADLQAQIADLRAQLANKEEELQNAlirieEEAAANMASQKKIKELEAQILELDEDLEREKfyrskngQRCKELEKELE 1139
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSG-----PDALPELLQSPVIQQLRAQLAELEAELAELS-------ARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1140 AIKNKLddtldttaaqQELRAKRETEVAQLRKAQEEENKMHESQIAELS------KKHLQAFNEMNEQLEQAKRNKLSVE 1213
Cdd:COG3206 295 ALRAQI----------AALRAQLQQEAQRILASLEAELEALQAREASLQaqlaqlEARLAELPELEAELRRLEREVEVAR 364
|
250
....*....|....*.
gi 768942001 1214 KAKQALESEFNELQIE 1229
Cdd:COG3206 365 ELYESLLQRLEEARLA 380
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
836-1402 |
7.82e-06 |
|
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: 50.88 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETE-LCAEAEEMRARLVNRKQ------ 908
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKtICQLTEEKEAQMEELNKakaahs 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 909 ----ELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEeeadRQKLQMEKVTTDSKMKALEGNIMVLDDQN 984
Cdd:pfam05483 349 fvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE----MTKFKNNKEVELEELKKILAEDEKLLDEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 985 NKLNKEKKLLEDRIAEFSSNLSEEEeksRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRK---LEGDSTDLHDQI 1061
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQARE---KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLEN 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1062 ADLQAQIADLRAQLANKEEELQNAliRIEEEAAAnmasqKKIKELEAQILELDEDLE--REKFYRSKNGQRCKeLEKELE 1139
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINC--KKQEERML-----KQIENLEEKEMNLRDELEsvREEFIQKGDEVKCK-LDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1140 AIKNKLDDTLDTTAAQQELrakrETEVAQLRKAQEEENKMHEsqiaelskkhlqafnEMNEQLEQAKRNKLSVEKAKQAL 1219
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKIL----ENKCNNLKKQIENKNKNIE---------------ELHQENKALKKKGSAENKQLNAY 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1220 ESEFNELQIELktlgqsksdsEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKD 1299
Cdd:pfam05483 635 EIKVNKLELEL----------ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1300 MLSLESHLQDTQELLQEETRQKLAIstrFRQMEEEQNSLRemleeeeeakknvekqiSVLQGQLGDMKKKMDQEVSSLES 1379
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGL---YKNKEQEQSSAK-----------------AALEIELSNIKAELLSLKKQLEI 764
|
570 580
....*....|....*....|...
gi 768942001 1380 AEESRKRLQREFDTVKLQLEEKE 1402
Cdd:pfam05483 765 EKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
850-1228 |
9.32e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 850 ELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLEEEEERVN 929
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 930 QMLNERKKMQQNIADLEQQldeeeadrqklqmEKVTTDSKMKALEGNIMVLDDQNNKLNKekklLEDRIAEFSSNLSEEE 1009
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQ-------------SVCPVCGTTLGEEKSNHIINHYNEKKSR----LEEKIREIEIEVKDID 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1010 EKSRSLQKLKNKHEA-IITDLEDRLRKEEKQRQELEKNRRKlEGDSTDLHDQIADLQAQIADLRAQ-LANKEEELQNALI 1087
Cdd:PRK01156 497 EKIVDLKKRKEYLESeEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWLNALA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1088 RIEEEAAANMASQ-----KKIKELEAQILELDEDLEREKFYrskNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKR 1162
Cdd:PRK01156 576 VISLIDIETNRSRsneikKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKI 652
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1163 ETevaqlRKAQEEENKMHESQIAELSKKHLQA---FNEMNEQLEQAKRNKLSVEKAKQALESEFNELQI 1228
Cdd:PRK01156 653 DN-----YKKQIAEIDSIIPDLKEITSRINDIednLKKSRKALDDAKANRARLESTIEILRTRINELSD 716
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1303-1702 |
9.65e-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: 50.28 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1303 LESHLQDTQELLQEETRQKlaistrfRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEE 1382
Cdd:pfam07888 36 LEECLQERAELLQAQEAAN-------RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1383 SRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNM---------ERK--QRKFDQMLAEEK 1451
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaERKqlQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1452 TISTQYAEERDKAEaearEKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDdagknvhELERSKRATEQQL 1531
Cdd:pfam07888 189 SLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQE-------RLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1532 EEI--------KTQLEELEDELQATE------DAKLRLEVNmQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAELED 1597
Cdd:pfam07888 258 EELssmaaqrdRTQAELHQARLQAAQltlqlaDASLALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1598 ERRQRsqavsakKKLELDLGELEvhiDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTmEA 1677
Cdd:pfam07888 337 ERMER-------EKLEVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET-VA 405
|
410 420
....*....|....*....|....*
gi 768942001 1678 DAAQFQEDLATAERLKRQMQAERDE 1702
Cdd:pfam07888 406 DAKWSEAALTSTERPDSPLSDSEDE 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1403-1624 |
1.10e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1403 AAYEKLERTKTR-LQQELDDLLVNQDGLRQLV---------------NNMERKQRKFDQMLAEEKTISTQYAEERDKAEA 1466
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHIQQQIktynknieeqrkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1467 EAREKETRALTLARELETITDLKNELERTNKQLK---------AEMEDLvsskDDAGKNVHELERSKRATEQQLEEIKTQ 1537
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQI----SEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1538 LEELED-ELQATEDAKLRLEVNMQAmkAQFDRDLQARDEQGeerrKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDL 1616
Cdd:PHA02562 322 IDELEEiMDEFNEQSKKLLELKNKI--STNKQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
....*...
gi 768942001 1617 GELEVHID 1624
Cdd:PHA02562 396 SELVKEKY 403
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
830-1274 |
1.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 830 KVKPLLQVTRQEEEMLAKEDelskvKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQE 909
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEED-----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 910 LEEILHDMESRLEEEEERVNQMlneRKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGnimvlddqnnklnk 989
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEEL---KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------------- 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 990 ekklledriaefssnLSEEEEKSRSLQKLKNKHeaiitdlEDRLRKEEKQRQELEKNRRKLEgdstdlhdqiadlqaqia 1069
Cdd:PTZ00121 1694 ---------------LKKEAEEAKKAEELKKKE-------AEEKKKAEELKKAEEENKIKAE------------------ 1733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1070 dlraQLANKEEELQnaliRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNGQRcKELEKELEAIKNKLDDTL 1149
Cdd:PTZ00121 1734 ----EAKKEAEEDK----KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-EEDEKRRMEVDKKIKDIF 1804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1150 DTTAAQQE--------LRAKRETEVAQLRKAQEEENKMHESqiAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALES 1221
Cdd:PTZ00121 1805 DNFANIIEggkegnlvINDSKEMEDSAIKEVADSKNMQLEE--ADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1222 EFNEL----QIELKTLGQSKSDSEHRRKKAESQVQELQV---KYGDCERQRQEAVeKIAK 1274
Cdd:PTZ00121 1883 EIEEAdeieKIDKDDIEREIPNNNMAGKNNDIIDDKLDKdeyIKRDAEETREEII-KISK 1941
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1235-1475 |
1.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1235 QSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELL 1314
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1315 qEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQIsvLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTV 1394
Cdd:COG4942 100 -EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY--LKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1395 KLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEektistqyaeeRDKAEAEAREKETR 1474
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR-----------LEAEAAAAAERTPA 245
|
.
gi 768942001 1475 A 1475
Cdd:COG4942 246 A 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
848-1024 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 848 EDELSKVKEKQLQAEEMIKEFESKQQQLNAE---KMALQEQLQAETELcAEAEEMRARLVNRKQELEEILHDMESRLEEE 924
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaKLLLQQLSELESQL-AEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 925 EE--RVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMV-LDDQNNKLNKEKKLLEDRIAEF 1001
Cdd:COG3206 260 LQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAsLEAELEALQAREASLQAQLAQL 339
|
170 180
....*....|....*....|...
gi 768942001 1002 SSNLSEEEEKSRSLQKLKNKHEA 1024
Cdd:COG3206 340 EARLAELPELEAELRRLEREVEV 362
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
887-1228 |
1.75e-05 |
|
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: 50.22 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 887 QAETELCAEAEEMRA--RLVNRKQELEEILHDM--ESRLEEEEERVNQMLNERKKMQQNIADLEQQldeeEADRQKLQME 962
Cdd:NF012221 1502 QKTLKLTAKAGSNRLefKGTGHNDGLGYILDNVvaTSESSQQADAVSKHAKQDDAAQNALADKERA----EADRQRLEQE 1577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 963 KvttDSKMKALEGNIMVLD--DQnNKLNKEKKLLEDRIAEfssnlsEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQR 1040
Cdd:NF012221 1578 K---QQQLAAISGSQSQLEstDQ-NALETNGQAQRDAILE------ESRAVTKELTTLAQGLDALDSQATYAGESGDQWR 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1041 QELEKnrRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEeeaAANMASQKKIKELEAQILELDEDLERE 1120
Cdd:NF012221 1648 NPFAG--GLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSE---AGVAQGEQNQANAEQDIDDAKADAEKR 1722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1121 KFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEEN-------------KMHESQIAEL 1187
Cdd:NF012221 1723 KDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKpnrqgaagsglsgKAYSVEGVAE 1802
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 768942001 1188 SKKHLQAFNEMN------EQLEQAKRNKLsvEKAKQALesefNELQI 1228
Cdd:NF012221 1803 PGSHINPDSPAAadgrfsEGLTEQEQEAL--EGATNAV----NRLQI 1843
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1464-1670 |
1.89e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1464 AEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELED 1543
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1544 ELQATEDAKLRLEV------------NMQAMKAQFDRDLQARDEQgEERRKQLVKQVHELEAELEDERRQRSQAVSAKKK 1611
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEEL-KADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1612 LELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEK 1670
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
836-1024 |
2.11e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEaeemRARLVNRKQE----LE 911
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE----RARALYRSGGsvsyLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 912 EIL-----HDMESR---LEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKvttDSKMKALEGNIMVLDDQ 983
Cdd:COG3883 107 VLLgsesfSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL---EAAKAELEAQQAEQEAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768942001 984 NNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEA 1024
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
852-1040 |
2.24e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 852 SKVKEKQLQAEEMIKEFESKQQQLNAEKMalqeqLQAETELCAEAEEMRARLVNRKQELEEilhdMESRLEEEEERVNQM 931
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKLRNEFEKELRERRNELQK----LEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 932 LNERKKMQQNIADLEQQLDEEEADRQKLQMEkvttdskmkalegnimvlddQNNKLNKEKKLLEdRIaefsSNLSEEEEK 1011
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEE--------------------LEELIEEQLQELE-RI----SGLTAEEAK 156
|
170 180 190
....*....|....*....|....*....|...
gi 768942001 1012 SRSLQKLKN--KHEA--IITDLEDRLRKEEKQR 1040
Cdd:PRK12704 157 EILLEKVEEeaRHEAavLIKEIEEEAKEEADKK 189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1755-1920 |
2.59e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1755 QVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKyKSSLTALEAKVAQLEEQLDTEIKERQQATRMV 1834
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-EAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1835 RRTEKKMKELVL----QVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNRE 1910
Cdd:COG4942 114 YRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170
....*....|
gi 768942001 1911 VNILKSKLRR 1920
Cdd:COG4942 194 KAERQKLLAR 203
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
792-1285 |
2.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 792 ARKAFTKRQQQLTAMKVIQRNCAAYLKLRN-----------WQWWRLFTKVKpLLQ--VTRQEEEMLAKEDELSKVKEKQ 858
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 859 LQAEEMIKEFESKQQQL-NAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLEEEEERVNQMLNErkk 937
Cdd:COG4913 319 DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 938 MQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQnnklnkekklLEDRIAEFSSNLSEEEEKSR---S 1014
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR----------LLALRDALAEALGLDEAELPfvgE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1015 LQKLKNKHEA---------------II---------------TDLEDRLR-------KEEKQRQELEKNR--RKLEGDST 1055
Cdd:COG4913 466 LIEVRPEEERwrgaiervlggfaltLLvppehyaaalrwvnrLHLRGRLVyervrtgLPDPERPRLDPDSlaGKLDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1056 DLHDQIADLQAQIADLRaqLANKEEELQNALIRIeeeAAANMASQKKikelEAQILELDEDLEREKFYRSKNGQRCKELE 1135
Cdd:COG4913 546 PFRAWLEAELGRRFDYV--CVDSPEELRRHPRAI---TRAGQVKGNG----TRHEKDDRRRIRSRYVLGFDNRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1136 KELEAIK---NKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKM--HESQIAELskkhlqafnemNEQLEQAKRNKL 1210
Cdd:COG4913 617 AELAELEeelAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAEL-----------EAELERLDASSD 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1211 SVEkakqALESEFNELQIELKTLgqsksdsehrrkkaESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSL 1285
Cdd:COG4913 686 DLA----ALEEQLEELEAELEEL--------------EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1459-1607 |
2.70e-05 |
|
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: 47.61 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1459 EERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLvSSKDDAGKNVHELErskrATEQQLEEIKTQL 1538
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-EEQLGNVRNNKEYE----ALQKEIESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1539 EELEDELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVS 1607
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAE----LAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
829-1229 |
3.40e-05 |
|
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: 49.05 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 829 TKVKPLLQ-VTRQEEEMLA---KEDELSKVKEKQLQAEEMIKEFESKQQQ----LNAEKMALQEQLQAETELCAEAEEMR 900
Cdd:pfam10174 289 NKIDQLKQeLSKKESELLAlqtKLETLTNQNSDCKQHIEVLKESLTAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 901 ARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVL 980
Cdd:pfam10174 369 QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEK 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 981 DDQNNKLNKEKKLLE----DRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDR--------LRKEEKQRQ-ELEKNR 1047
Cdd:pfam10174 449 ERIIERLKEQREREDrerlEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHasslassgLKKDSKLKSlEIAVEQ 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1048 RKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMAsqkkikELEaQILELDEDLEREKFYRSKn 1127
Cdd:pfam10174 529 KKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQA------EVE-RLLGILREVENEKNDKDK- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1128 gqRCKELEK-ELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMH-ESQIAELskkhLQAFNEMNEQLEQA 1205
Cdd:pfam10174 601 --KIAELESlTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSqQLQLEEL----MGALEKTRQELDAT 674
|
410 420
....*....|....*....|....
gi 768942001 1206 KRNKLSVEKAKQALESEFNELQIE 1229
Cdd:pfam10174 675 KARLSSTQQSLAEKDGHLTNLRAE 698
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1010-1336 |
3.60e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1010 EKSRSLQKLKNKHEAIITDLEdrlrkeEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRI 1089
Cdd:pfam00038 18 DKVRFLEQQNKLLETKISELR------QKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1090 EEEAAanmasqkKIKELEAQILELDEDLEREKFYRSkngqrckELEKELEAIKNKLDdtldttaaqqELRAKRETEVAQL 1169
Cdd:pfam00038 92 EDELN-------LRTSAENDLVGLRKDLDEATLARV-------DLEAKIESLKEELA----------FLKKNHEEEVREL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1170 RKaQEEENKMHESQIAELSKKHLQAFNEMNEQLE-QAKRNKlsvEKAKQALESEFNELQIELKT----LGQSKSD-SEHR 1243
Cdd:pfam00038 148 QA-QVSDTQVNVEMDAARKLDLTSALAEIRAQYEeIAAKNR---EEAEEWYQSKLEELQQAAARngdaLRSAKEEiTELR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1244 R--KKAESQVQELQVKYGDCERQRQEAVEKiakLQSELENVNSLLNESEGKNTKSSKDMlslESHLQDTQELLQEETRQK 1321
Cdd:pfam00038 224 RtiQSLEIELQSLKKQKASLERQLAETEER---YELQLADYQELISELEAELQETRQEM---ARQLREYQELLNVKLALD 297
|
330
....*....|....*
gi 768942001 1322 LAISTRFRQMEEEQN 1336
Cdd:pfam00038 298 IEIATYRKLLEGEEC 312
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
851-1233 |
3.95e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 851 LSKVKEKQLQAEEMIKEFESKQQQLNAEkmaLQEQLQAETElcaeaeemrarlvNRKQ--ELEEILHDMESRLeeeeerv 928
Cdd:PRK04778 100 FRKAKHEINEIESLLDLIEEDIEQILEE---LQELLESEEK-------------NREEveQLKDLYRELRKSL------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 929 nqmLNERKKMQQNIADLEQQLDEEEADRQklQMEKVTTdskmkalEGNI----MVLDDQNNKLNKEKKLLEDrIAEFssn 1004
Cdd:PRK04778 157 ---LANRFSFGPALDELEKQLENLEEEFS--QFVELTE-------SGDYvearEILDQLEEELAALEQIMEE-IPEL--- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1005 lseeeeksrsLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNrrKLEGDSTDLHDQIADLQAQIADLRaqLANKEEELQN 1084
Cdd:PRK04778 221 ----------LKELQTELPDQLQELKAGYRELVEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1085 ALIRI-------EEEAAANMASQKKIKELEAQIL-------ELDEDLER--EKFYRSKN-GQRCKELEKELEAIKNKLDD 1147
Cdd:PRK04778 287 IQERIdqlydilEREVKARKYVEKNSDTLPDFLEhakeqnkELKEEIDRvkQSYTLNESeLESVRQLEKQLESLEKQYDE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1148 TLDTTAAQQ----ELRAKRETEVAQLRKAQEEENKMHESqIAELSKKHLQAfNEMNEQLEQAKRN-KLSVEKAK-----Q 1217
Cdd:PRK04778 367 ITERIAEQEiaysELQEELEEILKQLEEIEKEQEKLSEM-LQGLRKDELEA-REKLERYRNKLHEiKRYLEKSNlpglpE 444
|
410
....*....|....*.
gi 768942001 1218 ALESEFNELQIELKTL 1233
Cdd:PRK04778 445 DYLEMFFEVSDEIEAL 460
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1635-1913 |
4.02e-05 |
|
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: 48.58 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1635 KQLKKLQVQFKDMMRESEDLRLSRDEainSAKETEKKVKTMEADAAQFQE--DLATAERLKRQMQAERDELQDEINgnnt 1712
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEE---KAREVERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIR---- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1713 knsmlQDEKRRLEARItqleeeleeeqLNSEMANDRNKRTTLQVDQLTAELSAERsAAQRLEGARSQA------ERKNKE 1786
Cdd:pfam17380 355 -----QEERKRELERI-----------RQEEIAMEISRMRELERLQMERQQKNER-VRQELEAARKVKileeerQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1787 LSLKLQELESTIKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADK-- 1864
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKil 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1865 ---LNSRTRQL-----KRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREVNI 1913
Cdd:pfam17380 498 ekeLEERKQAMieeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRI 554
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
848-1118 |
4.17e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 48.70 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 848 EDELSKVKEKQLQAE------------EMIKEFESK--QQQLNA-EKMALQEQLQAETELCAEAEEmRARLVNR--KQEL 910
Cdd:PLN03229 435 EGEVEKLKEQILKAKessskpselalnEMIEKLKKEidLEYTEAvIAMGLQERLENLREEFSKANS-QDQLMHPvlMEKI 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 911 EEILHDMESRLEEEEERVN-----QMLNE--RKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNImvlddQ 983
Cdd:PLN03229 514 EKLKDEFNKRLSRAPNYLSlkyklDMLNEfsRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEV-----A 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 984 NNKLNKEKKLLEDRIAEFSSNLSEEEE------KSRSLQ----KLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEgD 1053
Cdd:PLN03229 589 SSGASSGDELDDDLKEKVEKMKKEIELelagvlKSMGLEvigvTKKNKDTAEQTPPPNLQEKIESLNEEINKKIERVI-R 667
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1054 STDLHDQIADLQAQIA----DLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLE 1118
Cdd:PLN03229 668 SSDLKSKIELLKLEVAkaskTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAA 736
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1751-1900 |
4.27e-05 |
|
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: 47.80 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1751 RTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELEStikskYKSSLTALEAKVAQLEEQLDTeIKERQQA 1830
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDG-----ATAQLRAAQAAVKAAQAQLAQ-AQIDLAR 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1831 TR-------MVRRTEKKMKELVLQVEDERRNTEQYKDQADKlnSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDA 1900
Cdd:pfam00529 129 RRvlapiggISRESLVTAGALVAQAQANLLATVAQLDQIYV--QITQSAAENQAEVRSELSGAQLQIAEAEAELKLA 203
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
841-1427 |
4.46e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKEDELSKVKEKqlqaeemIKEFESKQQQLNAEKMALQEQLQAETE----LCAEAEEMRArLVNRKQELEEILHD 916
Cdd:PRK01156 189 EEKLKSSNLELENIKKQ-------IADDEKSHSITLKEIERLSIEYNNAMDdynnLKSALNELSS-LEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 917 MESRLEEEEERVNQM---------------------LNERKKMQQNIADLEQQLDEEEADRQKLQmEKVTTDSKMKALEG 975
Cdd:PRK01156 261 AESDLSMELEKNNYYkeleerhmkiindpvyknrnyINDYFKYKNDIENKKQILSNIDAEINKYH-AIIKKLSVLQKDYN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 976 NIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDST 1055
Cdd:PRK01156 340 DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1056 DLHDQIADLQAQIADLRaqlaNKEEELqnalirieEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKNG--QRCKE 1133
Cdd:PRK01156 420 DISSKVSSLNQRIRALR----ENLDEL--------SRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRleEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1134 LEKELEAIKNKLDD--TLDTTAAQQELRaKRETEVAQLRKAQEEENKMhESQIAELSKKHLQAfNEMNEQLeqakrNKLS 1211
Cdd:PRK01156 488 IEIEVKDIDEKIVDlkKRKEYLESEEIN-KSINEYNKIESARADLEDI-KIKINELKDKHDKY-EEIKNRY-----KSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1212 VEKAKQALESEFNELQ----IELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIaklQSELENVNSLLN 1287
Cdd:PRK01156 560 LEDLDSKRTSWLNALAvislIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI---ENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1288 ESEGKNT------KSSKDMLSLESHLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQG 1361
Cdd:PRK01156 637 EIQENKIlieklrGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSD 716
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1362 QLGDMKKKMDQeVSSLESAEESRKRLQREFDTVKLQ-LEEKEAAYEKLERTKTRLQQ---ELDDLLVNQD 1427
Cdd:PRK01156 717 RINDINETLES-MKKIKKAIGDLKRLREAFDKSGVPaMIRKSASQAMTSLTRKYLFEfnlDFDDIDVDQD 785
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
840-1122 |
4.70e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 840 QEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQE-QLQAETELCAEAEEMRARLVNRKQELEEILHDME 918
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKsRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 919 SRLEEEEERVNQMLNERKKMQQNIADLEQQLDE---------EEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNK 989
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLlieqeekikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 990 EKKLLEDRIAEF---SSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQA 1066
Cdd:pfam02463 870 QELLLKEEELEEqklKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1067 QIADL---------RAQLANKEEELQNAL-----IRIEEEAAANMASQKKIKELEAQILELDEDLEREKF 1122
Cdd:pfam02463 950 KEENNkeeeeernkRLLLAKEELGKVNLMaieefEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1575-1778 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1575 EQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMR----- 1649
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1650 -----------ESEDL-----RLSRDEAINSA-----KETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEIN 1708
Cdd:COG3883 99 ggsvsyldvllGSESFsdfldRLSALSKIADAdadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1709 GNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARS 1778
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1038-1902 |
5.07e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1038 KQRQELEKNRRKLEGDSTDLhdqiADLQAQIADLRAQLANKEEELQNALIRIEEEAAAnMASQKKIKELEAQILELDEDL 1117
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRL----VEMARELAELNEAESDLEQDYQAASDHLNLVQTA-LRQQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1118 EREKFYRSKNGQRCKELEKELEA-------IKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMH------ESQI 1184
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAaeeevdeLKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDltadnaEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1185 AELSKKHLQAFNEMNeQLEQakrnKLSVEkakQALESEFNELQIELKTLGQSKSDSE-----------HRRKKAES-QVQ 1252
Cdd:PRK04863 445 EEFQAKEQEATEELL-SLEQ----KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSEawdvarellrrLREQRHLAeQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1253 ELQVKYGDCERQRQEAvekiaklqselENVNSLLNESEGKNTKSSKDMLSLESHLQD---TQELLQEETRQKLAISTRFR 1329
Cdd:PRK04863 517 QLRMRLSELEQRLRQQ-----------QRAERLLAEFCKRLGKNLDDEDELEQLQEEleaRLESLSESVSEARERRMALR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1330 QMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDmkkkmdqevsSLESAEESRKRLQRefdtvkLQLEEKEAAYEK-- 1407
Cdd:PRK04863 586 QQLEQLQARIQRLAARAPAWLAAQDALARLREQSGE----------EFEDSQDVTEYMQQ------LLERERELTVERde 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1408 LERTKTRLQQELDDLLvNQDGlrqlvNNMERKQRkfdqmLAEE---KTISTQYA--EERDKAEAEAREKETRALTLAREL 1482
Cdd:PRK04863 650 LAARKQALDEEIERLS-QPGG-----SEDPRLNA-----LAERfggVLLSEIYDdvSLEDAPYFSALYGPARHAIVVPDL 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1483 ETITDLKNELERTnkqlkaeMEDL------VSSKDDAGKNVHELERS----------------------KRATEQQLEEI 1534
Cdd:PRK04863 719 SDAAEQLAGLEDC-------PEDLyliegdPDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQL 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1535 KTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDLQ-----ARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSA 1608
Cdd:PRK04863 792 RAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1609 KKKLELDLGELEVHIDAANKGRDEALKqlkklqvqfkDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLAT 1688
Cdd:PRK04863 867 LEQAKEGLSALNRLLPRLNLLADETLA----------DRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQ 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1689 AERLKRQMQAERDELQDeingnntknsmLQDEKRRLEaritqleeeleeeqlnsemandrnkrttlQVDQLTAELSAERs 1768
Cdd:PRK04863 937 FEQLKQDYQQAQQTQRD-----------AKQQAFALT-----------------------------EVVQRRAHFSYED- 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1769 aAQRLEGARSQAerkNKELSLKLQELESTiKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQV 1848
Cdd:PRK04863 976 -AAEMLAKNSDL---NEKLRQRLEQAEQE-RTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1849 EDERRntEQYKDQADKLN-------SRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANE 1902
Cdd:PRK04863 1051 DSGAE--ERARARRDELHarlsanrSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1079-1451 |
5.10e-05 |
|
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: 48.20 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1079 EEELQNALIRI--EEEAAANMASQKKIKELEaqilelDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQ 1156
Cdd:pfam17380 267 ENEFLNQLLHIvqHQKAVSERQQQEKFEKME------QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1157 ELRAKRETEVAQLRkaQEEENKmhesqiaelskkhlqafnemneQLEQAKRNKLSVEKAKQaleSEFNELQIElktlgqs 1236
Cdd:pfam17380 341 RMAMERERELERIR--QEERKR----------------------ELERIRQEEIAMEISRM---RELERLQME------- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1237 ksdsehRRKKAESQVQELQV--KYGDCERQRQEaveKIAKLQSELENVNSLLNESEgkntksSKDMLSLESHLQDTQELL 1314
Cdd:pfam17380 387 ------RQQKNERVRQELEAarKVKILEEERQR---KIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAREMERV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1315 QEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQ-ISVLQGQLGDMKKKMDQEvsslesaEESRKRLQREFDt 1393
Cdd:pfam17380 452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQrRKILEKELEERKQAMIEE-------ERKRKLLEKEME- 523
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1394 vklqlEEKEAAYEKLERTKT----RLQQELDDLLVNQDGLRQL------VNNMERKQRKFDQMLAEEK 1451
Cdd:pfam17380 524 -----ERQKAIYEEERRREAeeerRKQQEMEERRRIQEQMRKAteersrLEAMEREREMMRQIVESEK 586
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1044-1288 |
5.23e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1044 EKNRRKLEGDSTDLHDQIADLQAQiadlRAQLANKEEELQNALIRIEeeaaanmasqKKIKELEAQILELDEDLEREKfy 1123
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAE----------KLKEELEEKKEKLQEEEDKLL-- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1124 rskngqrcKELEKEleaiknklddtldttaAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLE 1203
Cdd:PRK00409 569 --------EEAEKE----------------AQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1204 QAKRNKLSVEKAKQALEsefnelQIELKTLGQ-----SKSDsehrrkKAESQVQE----LQVKYGDCERQRQEAVEKIAK 1274
Cdd:PRK00409 625 KKKKKQKEKQEELKVGD------EVKYLSLGQkgevlSIPD------DKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
250
....*....|....
gi 768942001 1275 LQSELENVNSLLNE 1288
Cdd:PRK00409 693 PKTVKPKPRTVSLE 706
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
902-1139 |
5.80e-05 |
|
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: 47.50 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 902 RLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQ--KLQMEKVTTDSKMKALEGNIMv 979
Cdd:pfam15905 84 ALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNEllKAKFSEDGTQKKMSSLSMELM- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 980 lddqnnklnKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLH- 1058
Cdd:pfam15905 163 ---------KLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSc 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1059 --DQIADLQAQIADLRAQLANKEEELQNALIRIEEeaaanmasqkKIKELEAQILELDEdlerekfyrskngqRCKELEK 1136
Cdd:pfam15905 234 vsEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEE----------KEQELSKQIKDLNE--------------KCKLLES 289
|
...
gi 768942001 1137 ELE 1139
Cdd:pfam15905 290 EKE 292
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
857-1107 |
6.08e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.77 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 857 KQLQAEEMIKEFESKQQQlnAEKMALQEQLQAETELCAEAeemrarlvNRKqeleeiLHDMESRLEEEEERVNQM----- 931
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQ--QQRASLLAQLKKQEEAISQA--------SRK------LRETQNTLNQLNKQIDELnasia 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 932 -LNERKKMQQNIadLEQQLDEeeADRQ----KLQM----EKVTTDSKM--------KALEGNIMVLDDQNNKLNKEKKLL 994
Cdd:PRK11637 114 kLEQQQAAQERL--LAAQLDA--AFRQgehtGLQLilsgEESQRGERIlayfgylnQARQETIAELKQTREELAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 995 EDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRrklegdsTDLHDQIADLQAQiADLRAQ 1074
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANE-------SRLRDSIARAERE-AKARAE 261
|
250 260 270
....*....|....*....|....*....|...
gi 768942001 1075 lankEEELQNALIRIEEEAAANMASQKKIKELE 1107
Cdd:PRK11637 262 ----REAREAARVRDKQKQAKRKGSTYKPTESE 290
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1432-1795 |
6.21e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1432 LVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELEtitdlknELERTNKQLKAEMEDLVSSKD 1511
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA-------ELKEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1512 DAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERR------KQLV 1585
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKqlqaklQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1586 KQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDE---ALKQLKKLQVQFKDMMRESEDLRLSRDEAI 1662
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaLLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1663 NSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQA----ERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEE 1738
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1739 QLNSEMANDRNKrttLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELE 1795
Cdd:pfam07888 345 EVELGREKDCNR---VQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLE 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1015-1225 |
6.58e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1015 LQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEgdstDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAA 1094
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYN----ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1095 ANMASQKKIKELEAqILE---LDEDLER----EKFYRSKNG--QRCKELEKELEAIKNKLDDTLDT-TAAQQELRAKR-- 1162
Cdd:COG3883 94 ALYRSGGSVSYLDV-LLGsesFSDFLDRlsalSKIADADADllEELKADKAELEAKKAELEAKLAElEALKAELEAAKae 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1163 -ETEVAQLRKAQ---EEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNE 1225
Cdd:COG3883 173 lEAQQAEQEALLaqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1414-1595 |
8.07e-05 |
|
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: 46.07 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1414 RLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLARELETItdlknele 1493
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1494 RTNKQLKAemedlvsskddAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQAR 1573
Cdd:COG1579 86 RNNKEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|..
gi 768942001 1574 DEQGEERRKQLVKQVHELEAEL 1595
Cdd:COG1579 155 EAELEELEAEREELAAKIPPEL 176
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1053-1208 |
1.00e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.58 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1053 DSTDLHDQIADLQAQIADLRAQLANkeeeLQNALIRIEEEAAAnmasQKKIKELEAQILELDEDLER-EKFYRSKNGQRc 1131
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLAR----LEAELGAEAEIAAA----EAQLAAAQAQLDLAQRELERyQALYKKGAVSQ- 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1132 keleKELEAIKNKLDdtldtTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELskkhlqafnemNEQLEQAKRN 1208
Cdd:COG1566 148 ----QELDEARAALD-----AAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQA-----------EAALAQAELN 204
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1399-1896 |
1.01e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1399 EEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEaEAREKETRALTL 1478
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1479 ARELETITDLKNELERTNKQLkaemedlvsskDDAGKNVHELERSKRateqqLEEIKTQLEELEDELQATEDAKLRLEVN 1558
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERI-----------NRARKAAPLAAHIKA-----VTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1559 MQAMKAQfdrdlqardEQGEERRKQLVKQVHELEAELedeRRQRSQAVSAKKKLELDLGELEvHIDAANKGRdEALKQLK 1638
Cdd:TIGR00618 330 RAAHVKQ---------QSSIEEQRRLLQTLHSQEIHI---RDAHEVATSIREISCQQHTLTQ-HIHTLQQQK-TTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1639 KLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTmeadaaqfqEDLATAERLKRQMQAERDELQDEIngnnTKNSMLQ 1718
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK---------QQELQQRYAELCAAAITCTAQCEK----LEKIHLQ 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1719 DEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQ------LTAELSAERSAAQRLEGARSQAERKNKELSLKLQ 1792
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1793 ELESTikskyKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQL 1872
Cdd:TIGR00618 543 SEEDV-----YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
490 500
....*....|....*....|....
gi 768942001 1873 KRQLEEAEEEVTRANAYRRKLQRE 1896
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQEL 641
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
958-1143 |
1.03e-04 |
|
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: 46.55 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 958 KLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEeeeksrslqklknkheaiITDLEDRLRKEE 1037
Cdd:smart00787 127 RLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPK------------------LRDRKDALEEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1038 KQRQELEKNRRKLEGDSTD-LHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAanmasqkKIKELEAQILELDED 1116
Cdd:smart00787 189 RQLKQLEDELEDCDPTELDrAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKK 261
|
170 180
....*....|....*....|....*..
gi 768942001 1117 LEREKFYRSKNGQRCKELEKELEAIKN 1143
Cdd:smart00787 262 LEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
928-1167 |
1.04e-04 |
|
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: 47.36 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 928 VNQMLNERKKMQQNIADLEQQLDEEEADRQKLQmekvtTDSKMKAlegNIMVLDDQNNKLNKEKKLLE-DRIAEFSSNLS 1006
Cdd:pfam05911 589 CNDVLSGKADLEDFVLELSHILDWISNHCFSLL-----DVSSMED---EIKKHDCIDKVTLSENKVAQvDNGCSEIDNLS 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1007 EEEEKSRSLQKLKNKHEAIITdlEDRLRKEEKQRQELEKNrrKLEGDSTDLHDQIADLQAQ-------IADLRAQLANKE 1079
Cdd:pfam05911 661 SDPEIPSDGPLVSGSNDLKTE--ENKRLKEEFEQLKSEKE--NLEVELASCTENLESTKSQlqeseqlIAELRSELASLK 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1080 EelQNALIrieEEAAANMA------------SQKKIKELEAQILELDEDLEREKFYRSKNGQRCKELEKELEAIKNKldD 1147
Cdd:pfam05911 737 E--SNSLA---ETQLKCMAesyedletrlteLEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK--E 809
|
250 260
....*....|....*....|
gi 768942001 1148 TLDTTAAQQELRAKRETEVA 1167
Cdd:pfam05911 810 SSNCDADQEDKKLQQEKEIT 829
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1520-1705 |
1.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1520 LERSKRATEQQLEEIKTQLEELEDELQATEDAklrlevnMQAMKAQFD-RDLQARDEQGEERRKQLVKQVHELEAELEDE 1598
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA-------LEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1599 RRQRSQAVSAKK----------------KLELDLGELEVHIDAANK--GRD-----EALKQLKKLQVQFKDMMRES-EDL 1654
Cdd:COG3206 239 EARLAALRAQLGsgpdalpellqspviqQLRAQLAELEAELAELSAryTPNhpdviALRAQIAALRAQLQQEAQRIlASL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1655 RLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQD 1705
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
839-1479 |
1.10e-04 |
|
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: 47.12 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 839 RQEEEMLAKEDELSkvkekQLQAEEMIKEFESKQQQLNAEKMALQE-----QLQAETELCAEAEEMRARlvnRKQELEEI 913
Cdd:pfam10174 122 QSEHERQAKELFLL-----RKTLEEMELRIETQKQTLGARDESIKKllemlQSKGLPKKSGEEDWERTR---RIAEAEMQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 914 LHDMESRLEEEEERVNQMLNERKKMQQNIADLEqqldEEEADRQKLQMEkvttDSKMKALEGNIMVLDDQNNKLNKEkkl 993
Cdd:pfam10174 194 LGHLEVLLDQKEKENIHLREELHRRNQLQPDPA----KTKALQTVIEMK----DTKISSLERNIRDLEDEVQMLKTN--- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 994 ledriAEFSSNLSEEEEKSRSLQK-----LKNKheaiITDLEDRLRKEEKQRQELeknRRKLEgdstDLHDQIADLQAQI 1068
Cdd:pfam10174 263 -----GLLHTEDREEEIKQMEVYKshskfMKNK----IDQLKQELSKKESELLAL---QTKLE----TLTNQNSDCKQHI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1069 ADLRAQLANKEeelQNALIRIEEEAAANMASQKK---IKELEAQILELDEDlerekfyrskngqrCKELEKELEAIKnkl 1145
Cdd:pfam10174 327 EVLKESLTAKE---QRAAILQTEVDALRLRLEEKesfLNKKTKQLQDLTEE--------------KSTLAGEIRDLK--- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1146 dDTLDTTAAQ-QELRAKRETEVAQLR--KAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRnklSVEKAKQALESE 1222
Cdd:pfam10174 387 -DMLDVKERKiNVLQKKIENLQEQLRdkDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKER---IIERLKEQRERE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1223 FNELQIELKTLGQSKsdsehrrKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLS 1302
Cdd:pfam10174 463 DRERLEELESLKKEN-------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1303 LESHLQDTQELlQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEakknvekQISVLQGQLGDM---KKKMDQEVSSLES 1379
Cdd:pfam10174 536 LENQLKKAHNA-EEAVRTNPEINDRIRLLEQEVARYKEESGKAQA-------EVERLLGILREVeneKNDKDKKIAELES 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1380 A----------EESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAE 1449
Cdd:pfam10174 608 LtlrqmkeqnkKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
650 660 670
....*....|....*....|....*....|
gi 768942001 1450 EKTISTQYAEERDKAEAEAREKETRALTLA 1479
Cdd:pfam10174 688 KDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
793-1065 |
1.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 793 RKAFTKRQQQLTAMKVIQRNCAaylkLRNWQWWRLFTKVKPLLQVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQ 872
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMA----LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 873 QQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLEEEeervnqmlNERKKMQQNIADLEQQLDEE 952
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE--------DEKKAAEALKKEAEEAKKAE 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 953 EAdRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDriaefssnLSEEEEKSRSLQKLKNKHEAIITDLEDR 1032
Cdd:PTZ00121 1706 EL-KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE--------AKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
250 260 270
....*....|....*....|....*....|....*
gi 768942001 1033 LRK--EEKQRQELEKNRRKLEGDSTDLHDQIADLQ 1065
Cdd:PTZ00121 1777 KEAviEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1180-1558 |
1.13e-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: 47.52 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1180 HESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQALESefNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYG 1259
Cdd:NF012221 1435 HGARVSELDTYTNTSLYQDLSNLTAGEVIALSFDFARRAGLS--TNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAKAG 1512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1260 ------------DCERQRQEAVEKIAKLQSELENVNSLLNESEG-KNTKSSKdmlslESHLQDTQELLQEETRQKLAIST 1326
Cdd:NF012221 1513 snrlefkgtghnDGLGYILDNVVATSESSQQADAVSKHAKQDDAaQNALADK-----ERAEADRQRLEQEKQQQLAAISG 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1327 RFRQMEE-EQNSLREMLEEEEEAKKNVEKQISVlqgQLGDMKKKMDQEVSSLESAEESRKRLQREF-----DTVKLQLEE 1400
Cdd:NF012221 1588 SQSQLEStDQNALETNGQAQRDAILEESRAVTK---ELTTLAQGLDALDSQATYAGESGDQWRNPFaggllDRVQEQLDD 1664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1401 -KEAAYEKLERTKTRLQQELDDLlvnQDGLRQL---VNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRAL 1476
Cdd:NF012221 1665 aKKISGKQLADAKQRHVDNQQKV---KDAVAKSeagVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDAN 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1477 TLARELETI--TDLKNELERTNkQLKAEMEDLVSSKDD------------AGKNvHELERSKRATEQQLEEIKTQL---- 1538
Cdd:NF012221 1742 AAANDAQSRgeQDASAAENKAN-QAQADAKGAKQDESDkpnrqgaagsglSGKA-YSVEGVAEPGSHINPDSPAAAdgrf 1819
|
410 420
....*....|....*....|....*
gi 768942001 1539 -EEL-EDELQATEDAKL---RLEVN 1558
Cdd:NF012221 1820 sEGLtEQEQEALEGATNavnRLQIN 1844
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
932-1229 |
1.20e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 932 LNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDdqnnklnkekklLEDRIAEFSSNLSeeeEK 1011
Cdd:PRK10929 57 LEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDA------------LEQEILQVSSQLL---EK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1012 SRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDL----HDQIADLQAQIADLRAQL---------ANK 1078
Cdd:PRK10929 122 SRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNtplaQAQLTALQAESAALKALVdelelaqlsANN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1079 EEElqnaLIRIEEEAAanmasQKKIKELEAQILELDEDLerekfyrskNGQRCKELEKELEAIKNKLDDTLDTTAA-QQE 1157
Cdd:PRK10929 202 RQE----LARLRSELA-----KKRSQQLDAYLQALRNQL---------NSQRQREAERALESTELLAEQSGDLPKSiVAQ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1158 LRAKRETEVAQLRKAQE-EENKMHESQIAELSKKHLQAFNEMNEQ---------LEQAKRNKLS--VEKAK-QALESEFN 1224
Cdd:PRK10929 264 FKINRELSQALNQQAQRmDLIASQQRQAASQTLQVRQALNTLREQsqwlgvsnaLGEALRAQVArlPEMPKpQQLDTEMA 343
|
....*
gi 768942001 1225 ELQIE 1229
Cdd:PRK10929 344 QLRVQ 348
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1134-1550 |
1.27e-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: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1134 LEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNKLSVE 1213
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1214 ----------KAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQvkygdceRQRQEAvekiaklQSELENVN 1283
Cdd:pfam07888 112 elseekdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG-------AQRKEE-------EAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1284 SLLNESEGKNTKSSKDMLSLESHL--QDTQEL-LQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQ 1360
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLaqRDTQVLqLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1361 GQLGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKlERTKTRLQQELDdllvnQDGLRQLVNNMERKQ 1440
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQ-ERETLQQSAEAD-----KDRIEKLSAELQRLE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1441 rkfdQMLAEEKTistqyaeERDKAEAE-AREKETRALTLARELETITDLKNELERTNKqlkaEMEDLVSSKDDAGKNVHE 1519
Cdd:pfam07888 332 ----ERLQEERM-------EREKLEVElGREKDCNRVQLSESRRELQELKASLRVAQK----EKEQLQAEKQELLEYIRQ 396
|
410 420 430
....*....|....*....|....*....|...
gi 768942001 1520 LER--SKRATEQQLEEIKTQLEELEDELQATED 1550
Cdd:pfam07888 397 LEQrlETVADAKWSEAALTSTERPDSPLSDSED 429
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
842-1227 |
1.41e-04 |
|
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: 47.25 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 842 EEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETE---LCAEAEEMRARLVNRKQELEEILHDME 918
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 919 ----------SRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEadRQKLQMEKVttdskMKALEGNIMVLddQNNKLN 988
Cdd:COG3096 365 eqeevveeaaEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQ--TRAIQYQQA-----VQALEKARALC--GLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 989 KEKklLEDRIAEFSSNLSEEEEKSRSL-QKL------KNKHEAI------ITDLEDRLRKEEKQRQELEKNRrklegDST 1055
Cdd:COG3096 436 PEN--AEDYLAAFRAKEQQATEEVLELeQKLsvadaaRRQFEKAyelvckIAGEVERSQAWQTARELLRRYR-----SQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1056 DLHDQIADLQAQIADLRAQLANKE--EELQNALI-RIEEEAAANMASQKKIKELEAQILELDEDLEREkfyrsknGQRCK 1132
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQnaERLLEEFCqRIGQQLDAAEELEELLAELEAQLEELEEQAAEA-------VEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1133 ELEKELEAIKnklddtldttAAQQELRAKreteVAQLRKAQEEENKMHESQIAEL--SKKHLQAFNEMNEQLEQAKRNKL 1210
Cdd:COG3096 582 ELRQQLEQLR----------ARIKELAAR----APAWLAAQDALERLREQSGEALadSQEVTAAMQQLLEREREATVERD 647
|
410
....*....|....*..
gi 768942001 1211 SVEKAKQALESEFNELQ 1227
Cdd:COG3096 648 ELAARKQALESQIERLS 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1537-1921 |
1.55e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1537 QLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQGEErrKQLVKQVHELEAELEDerrqrsqavsakkkLELDL 1616
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLD-QLKAQIEEKEE--KDLHERLNGLESELAE--------------LDEEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1617 GELEVHIDAANKGRDEAlkqlkklqvqfkdmmresedlrlsrDEAINSAKETEKKVKTMEADAAQFQEDLATAERLK--- 1693
Cdd:PRK02224 223 ERYEEQREQARETRDEA-------------------------DEVLEEHEERREELETLEAEIEDLRETIAETEREReel 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1694 ----RQMQAERDELQDEING-------NNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAE 1762
Cdd:PRK02224 278 aeevRDLRERLEELEEERDDllaeaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1763 LSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKYKS------SLTALEAKVAQLEEQLDtEIKERQQATRMVRR 1836
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvDLGNAEDFLEELREERD-ELREREAELEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1837 TEK-------------KMKELVLQVEDERR--NTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYrRKLQRELEDAN 1901
Cdd:PRK02224 437 TARerveeaealleagKCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLE 515
|
410 420
....*....|....*....|
gi 768942001 1902 ETQDTMNREVNILKSKLRRD 1921
Cdd:PRK02224 516 ERREDLEELIAERRETIEEK 535
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
896-1282 |
1.58e-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: 46.43 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 896 AEEMRARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEeeadrqkLQMEKVTTDSKMKALEG 975
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE-------LKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 976 NIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDST 1055
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1056 DLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEdlEREKFYRSKngQRCKELE 1135
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS--LQERLNASE--RKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1136 KELEAIKNKLDDTL------------------DTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKhlqafnE 1197
Cdd:pfam07888 258 EELSSMAAQRDRTQaelhqarlqaaqltlqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRL------E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1198 MNEQLEQAKRNKLSVEKAKqalESEFNELQIelktlgqSKSDSEHRRKKAESQVqeLQVKYGDCERQRQEAVEKIAKLQS 1277
Cdd:pfam07888 332 ERLQEERMEREKLEVELGR---EKDCNRVQL-------SESRRELQELKASLRV--AQKEKEQLQAEKQELLEYIRQLEQ 399
|
....*
gi 768942001 1278 ELENV 1282
Cdd:pfam07888 400 RLETV 404
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
848-1100 |
1.74e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 848 EDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQaetELCAEAEEMRARLVNRKQELEEILHDMeSRLEEEEER 927
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQ---ELREKRDELNEKVKELKEERDELNEKL-NELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 928 VNQMLNERKKMQQNIADLEQQLDEEEadrQKLQMEKVTTD------SKMKALEGNIMVLDDQNnKLNKEKKLLEDRIAEF 1001
Cdd:COG1340 97 LRKELAELNKAGGSIDKLRKEIERLE---WRQQTEVLSPEeekelvEKIKELEKELEKAKKAL-EKNEKLKELRAELKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1002 SSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEE 1081
Cdd:COG1340 173 RKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
250
....*....|....*....
gi 768942001 1082 LQNALIRIEEEAAANMASQ 1100
Cdd:COG1340 253 QRALKREKEKEELEEKAEE 271
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
838-1079 |
1.76e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 838 TRQEEEMLAKEDELSKVKEKQLQAEEM--------IKEFESKQQQLNAEKMALQEQLQAETELcAEAEEMRARLVNRKQE 909
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRkeyleseeINKSINEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKS 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 910 LEeiLHDMESRLEEEEERVNQMLN-ERKKMQQNIADLEQQLDEEEADRQKLQME----KVTTDSKMKALEGNIMVLDDQN 984
Cdd:PRK01156 558 LK--LEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 985 NKLnKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADL 1064
Cdd:PRK01156 636 NEI-QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
250
....*....|....*
gi 768942001 1065 QAQIADLRAQLANKE 1079
Cdd:PRK01156 715 SDRINDINETLESMK 729
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1461-1647 |
1.81e-04 |
|
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: 46.56 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1461 RDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEE 1540
Cdd:pfam05667 302 HTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1541 LEDELQATEDAKLRL---EVNMQAMKAQFD---RDLQARDEQGEERRKQLVKQVHELEaELEDERRQRSQAVSAKKKlEL 1614
Cdd:pfam05667 382 LEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALK-EAKSNKEDESQRKLEEIK-EL 459
|
170 180 190
....*....|....*....|....*....|...
gi 768942001 1615 DLGELEVHIDAANKgrDEALKQLKKlqvQFKDM 1647
Cdd:pfam05667 460 REKIKEVAEEAKQK--EELYKQLVA---EYERL 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1613-1840 |
1.83e-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: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1613 ELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLatAERL 1692
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1693 kRQMQaerdelqdeINGNNTK-------NSMLQDEKRRLEARitqleeeleeeqlnsEMANDRNKRTTLQVDQLTAELSA 1765
Cdd:COG3883 93 -RALY---------RSGGSVSyldvllgSESFSDFLDRLSAL---------------SKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1766 ERSAaqrLEGARSQAERKNKELSLKLQELESTiKSKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKK 1840
Cdd:COG3883 148 KKAE---LEAKLAELEALKAELEAAKAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1462-1608 |
1.85e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1462 DKA-----EAEAREKeTRALTLARELEtitdlknELERTNKQLKAEMEDLVSSKDDAGKnvhelERskrateqqLEEIKT 1536
Cdd:COG0542 389 DKAidlidEAAARVR-MEIDSKPEELD-------ELERRLEQLEIEKEALKKEQDEASF-----ER--------LAELRD 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1537 QLEELEDELQAtedaklrLEVNMQAMKAQFD--RDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSA 1608
Cdd:COG0542 448 ELAELEEELEA-------LKARWEAEKELIEeiQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
871-1240 |
2.02e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 871 KQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELE---EILHDMESRLEEEEERVNQMLNERKKmQQNIADLEQ 947
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAqapAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 948 QLDEEEADRQKLQMEKVTTDSKM-----------KALEGNIMVLDDQNNKLNkekklledriaefsSNLSEEEEKSRSLQ 1016
Cdd:PRK11281 129 RLAQTLDQLQNAQNDLAEYNSQLvslqtqperaqAALYANSQRLQQIRNLLK--------------GGKVGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1017 KLKNKHEAIITDLEDRLRKEEK---QRQELEKNRRKL-EGDSTDLHDQIADLQAQIADLRAQLANKE-EELQNAlirieE 1091
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYlTARIQRLEHQLQLLQEAINSKRLTLSEKTvQEAQSQ-----D 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1092 EAAANMASQKKIKELEAQiLELDEDLEREKfyrskngQRCKELEKELEAIKNKLDDTLDTTAA----------------- 1154
Cdd:PRK11281 270 EAARIQANPLVAQELEIN-LQLSQRLLKAT-------EKLNTLTQQNLRVKNWLDRLTQSERNikeqisvlkgslllsri 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1155 ----QQELRAKRE-----TEVAQLRKAQEEENKMHE------SQIAELSKKHLQAFN-EMNEQLEQ--AKRNKLSVEKAK 1216
Cdd:PRK11281 342 lyqqQQALPSADLieglaDRIADLRLEQFEINQQRDalfqpdAYIDKLEAGHKSEVTdEVRDALLQllDERRELLDQLNK 421
|
410 420
....*....|....*....|....*..
gi 768942001 1217 QaLESEFNE---LQIELKTLgQSKSDS 1240
Cdd:PRK11281 422 Q-LNNQLNLainLQLNQQQL-LSVSDS 446
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1028-1193 |
2.11e-04 |
|
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: 45.52 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1028 DLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEelqnaliRIEEEAAANMASQKKIKELE 1107
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEE-------QLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1108 AQILELDEDLEREKfyrSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELrakrETEVAQLRKAQEEENKMHESQIAEL 1187
Cdd:pfam09787 121 EELRYLEEELRRSK---ATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETLIQKQTMLEALSTEK 193
|
....*.
gi 768942001 1188 SKKHLQ 1193
Cdd:pfam09787 194 NSLVLQ 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1377-1547 |
2.30e-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: 44.92 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1377 LESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMeRKQRKFDQMLAEEKTIstq 1456
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEALQKEIESL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1457 yaeERDKAEAEAREKETraltlareLETITDLKNELERTNKQLKAEMEDLVSSKDdagknvhELERSKRATEQQLEEIKT 1536
Cdd:COG1579 102 ---KRRISDLEDEILEL--------MERIEELEEELAELEAELAELEAELEEKKA-------ELDEELAELEAELEELEA 163
|
170
....*....|.
gi 768942001 1537 QLEELEDELQA 1547
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
647-671 |
2.39e-04 |
|
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: 43.87 E-value: 2.39e-04
10 20
....*....|....*....|....*
gi 768942001 647 YKEQLGNLMTTLRNTNPNFVRCIIP 671
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
872-1275 |
2.60e-04 |
|
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: 46.37 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 872 QQQLNAEKMALQEQLQAETELCAEAEEmraRLVNRKQELEEILHDMEsrleeeeervnqmlNERKKMQQNIADLEQQLDE 951
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEE---QLVQANGELEKASREET--------------FARTALKNARLDLRRLFDE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 952 EEAdrQKLQMEKVTTDSKMKALEgnimvlddQNNKLNKEKKLLEdriaefssnlseeeeksrslqklkNKHEAIITDLED 1031
Cdd:pfam12128 662 KQS--EKDKKNKALAERKDSANE--------RLNSLEAQLKQLD------------------------KKHQAWLEEQKE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1032 RLRKEEKQRQElekNRRKLEGdstDLHDQIADLQAQIADLRAQLANKEEELQNALIRieeEAAANMASQKKIKELEAQIL 1111
Cdd:pfam12128 708 QKREARTEKQA---YWQVVEG---ALDAQLALLKAAIAARRSGAKAELKALETWYKR---DLASLGVDPDVIAKLKREIR 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1112 ELDEDLER-----------EKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQE----LRAKRETEVAQLRKAQEEE 1176
Cdd:pfam12128 779 TLERKIERiavrrqevlryFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRL 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1177 NKMHESQIAELSK--------KHLQAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAE 1248
Cdd:pfam12128 859 SENLRGLRCEMSKlatlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREE 938
|
410 420
....*....|....*....|....*..
gi 768942001 1249 SQVQELQVKYGDCERQRQEAVEKIAKL 1275
Cdd:pfam12128 939 DHYQNDKGIRLLDYRKLVPYLEQWFDV 965
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
841-1610 |
2.71e-04 |
|
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: 46.10 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 841 EEEMLAKEDELSKVKEKQLQAEEMikefESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEI---LHDM 917
Cdd:COG3096 326 EQDYQAASDHLNLVQTALRQQEKI----ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLksqLADY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 918 ESRLEEEEERV---NQMLNERKKMQQ----------NIADLEQQLD--EEEADRQKLQMEKVTTDSKM------KALEGN 976
Cdd:COG3096 402 QQALDVQQTRAiqyQQAVQALEKARAlcglpdltpeNAEDYLAAFRakEQQATEEVLELEQKLSVADAarrqfeKAYELV 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 977 IMVLD--DQNNKLNKEKKLLED---------RIAEFSSNLSEEEEKSRSLQKLKNKHEAII----------TDLEDRLRK 1035
Cdd:COG3096 482 CKIAGevERSQAWQTARELLRRyrsqqalaqRLQQLRAQLAELEQRLRQQQNAERLLEEFCqrigqqldaaEELEELLAE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1036 EEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQlANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDE 1115
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1116 DLEREkfyRSKNGQRCKELEKELE--AIKNKLDDTLDTTAAQQ---ELRAKRETEVAqLRKAQEEENKMHESQIA----- 1185
Cdd:COG3096 641 EATVE---RDELAARKQALESQIErlSQPGGAEDPRLLALAERlggVLLSEIYDDVT-LEDAPYFSALYGPARHAivvpd 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1186 -ELSKKHLQAFNEMNEQLeqakrnkLSVEKAKQAL-ESEFNELQIELKTLGQSkSDSEHR-----------RKKAESQVQ 1252
Cdd:COG3096 717 lSAVKEQLAGLEDCPEDL-------YLIEGDPDSFdDSVFDAEELEDAVVVKL-SDRQWRysrfpevplfgRAAREKRLE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1253 ELqvkygdcERQRQEAVEKIAKLQSELENVNSLLNESEGkntksskdmlSLESHLQ-----DTQELLQEetrqklaISTR 1327
Cdd:COG3096 789 EL-------RAERDELAEQYAKASFDVQKLQRLHQAFSQ----------FVGGHLAvafapDPEAELAA-------LRQR 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1328 FRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLG--------DMKKKMDQEVSSLESAEESRKRLQREFDTVK---- 1395
Cdd:COG3096 845 RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPqanlladeTLADRLEELREELDAAQEAQAFIQQHGKALAqlep 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1396 ---------LQLEEKEAAYEKLERTKTRLQQELddllvnqDGLRQLVNNMER-KQRKFDQMLAEEKTISTQYAEERDKAE 1465
Cdd:COG3096 925 lvavlqsdpEQFEQLQADYLQAKEQQRRLKQQI-------FALSEVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQAE 997
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1466 AEAREKETRALTLARELEtitdlknelertnkQLKAEMEDLVSSKDdagknvhelerskrATEQQLEEIKTQLEELedEL 1545
Cdd:COG3096 998 EARREAREQLRQAQAQYS--------------QYNQVLASLKSSRD--------------AKQQTLQELEQELEEL--GV 1047
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768942001 1546 QATEDAklrlevnmqAMKAQFDRD-LQARDEQGEERRKQLVKQVHELEAEL-----------EDERRQRSQAVSAKK 1610
Cdd:COG3096 1048 QADAEA---------EERARIRRDeLHEELSQNRSRRSQLEKQLTRCEAEMdslqkrlrkaeRDYKQEREQVVQAKA 1115
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1528-1898 |
2.73e-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: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1528 EQQLEEIKTQLEELedeLQATEDAKLRLEVNMQAMKAQfdrdlqarDEQGEERRKQLVKQVHELEAELEDERRQRSQAVS 1607
Cdd:pfam07888 33 QNRLEECLQERAEL---LQAQEAANRQREKEKERYKRD--------REQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1608 AKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLA 1687
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1688 TAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLN-------SEMANDRNKRTTLQVDQLT 1760
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALleelrslQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1761 AELSAERSAAQRLEGARSQAERKN---KELSLKLQELESTIKSKYKSSLTALEAKVAQLEEqLDTEI---KERQQATRMV 1834
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTlqlADASLALREGRARWAQERETLQQSAEADKDRIEK-LSAELqrlEERLQEERME 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1835 RrtEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELE 1898
Cdd:pfam07888 341 R--EKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
994-1143 |
2.79e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 994 LEDRIAEFSSNLSEEEEKSRSLQKLKNkhEAIITDLEDRLRKEEKQRQELEKnrrklegdstdlhdQIADLQAQIADLRA 1073
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHE--ERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDE 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1074 QLANKEEELQNALIRIEEEAAANmasqKKIKELEAQILELDEDLEREKfyrskngQRCKELEKELEAIKN 1143
Cdd:COG2433 442 RIERLERELSEARSEERREIRKD----REISRLDREIERLERELEEER-------ERIEELKRKLERLKE 500
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1410-1900 |
3.07e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1410 RTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFdqMLaeekTISTQYAEERDKAEAEAREKETRALTLARELETITDLK 1489
Cdd:COG5278 36 REASEWVEHTYEVLRALEELLSALLDAETGQRGY--LL----TGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1490 NELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRD 1569
Cdd:COG5278 110 DELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1570 LQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQFKDMMR 1649
Cdd:COG5278 190 ELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1650 ESEDLRLSRDEAINSAKETEKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARIT 1729
Cdd:COG5278 270 LAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1730 QLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKYKSSLTAL 1809
Cdd:COG5278 350 LLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1810 EAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANAY 1889
Cdd:COG5278 430 EALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALL 509
|
490
....*....|.
gi 768942001 1890 RRKLQRELEDA 1900
Cdd:COG5278 510 LAAAEAALAAA 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
830-1136 |
3.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 830 KVKPLLQVTRQEEEMLAKEDELSKVKEkqlqAEEMIKEFESKQQQLNAEKmalqeqLQAETElcaEAEEMRARLVNRKQE 909
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKE----LAEQLKELEEKLKKYNLEE------LEKKAE---EYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 910 LEEILHDMEsrleeeeeRVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTT-DSKMKALEGnimvLDDQNNKLN 988
Cdd:PRK03918 541 IKSLKKELE--------KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEElEERLKELEP----FYNEYLELK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 989 KEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIitdledRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQI 1068
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL------RKELEELEKKYSEEEYEELREEYLELSRELAGLRAEL 682
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1069 ADLRAQLankeEELQNALIRIEEEAAANMASQKKIKELEAQILELDEdlEREKFYRSKNGQRCKELEK 1136
Cdd:PRK03918 683 EELEKRR----EEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE--LREKVKKYKALLKERALSK 744
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1044-1249 |
3.59e-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: 45.98 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1044 EKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAAnmasqKKIKELeAQILE-LDEDLErekf 1122
Cdd:NF012221 1568 EADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVT-----KELTTL-AQGLDaLDSQAT---- 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1123 YRSKNGQRCKE--LEKELEAIKNKLDDTLDT------------TAAQQELR---AKRETEVAQLRKAQEEENKMHESQIA 1185
Cdd:NF012221 1638 YAGESGDQWRNpfAGGLLDRVQEQLDDAKKIsgkqladakqrhVDNQQKVKdavAKSEAGVAQGEQNQANAEQDIDDAKA 1717
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1186 ELSKKHLQAFNEMNEQLEQAKRNKLSVEKAKQ-------ALESEFNELQIELKTLGQSKSDSEHRRKKAES 1249
Cdd:NF012221 1718 DAEKRKDDALAKQNEAQQAESDANAAANDAQSrgeqdasAAENKANQAQADAKGAKQDESDKPNRQGAAGS 1788
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
839-1163 |
3.70e-04 |
|
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: 45.60 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 839 RQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETElcaeaeemrarlvNRKQELEEILHDME 918
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA-------------ERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 919 SRLEEEEERVNQMLNE--RKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLED 996
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 997 RIAEFSsnlSEEEEKSRSLQKLKnKHEAIITDLEDRLRKE-EKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQL 1075
Cdd:pfam12128 769 VIAKLK---REIRTLERKIERIA-VRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKL 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1076 ANKEEELQNALIRIEEEAAANMASQKKIKEL-------EAQiLELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDT 1148
Cdd:pfam12128 845 EMERKASEKQQVRLSENLRGLRCEMSKLATLkedanseQAQ-GSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
330
....*....|....*
gi 768942001 1149 LDTTAAQQELRAKRE 1163
Cdd:pfam12128 924 SGSGLAETWESLREE 938
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
840-1446 |
3.92e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 840 QEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQ-QQLNAEKMALQEQLQAETELcAEAEEMRARLVNRKQELEEILHDME 918
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgKNLDDEDELEQLQEELEARL-ESLSESVSEARERRMALRQQLEQLQ 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 919 SRLEEEEERVNQMLNerkkMQQNIADLEQQLDEEEADRQKLqmekvttDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRI 998
Cdd:PRK04863 593 ARIQRLAARAPAWLA----AQDALARLREQSGEEFEDSQDV-------TEYMQQLLERERELTVERDELAARKQALDEEI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 999 AEFSSNLSEEEEKsrsLQKLKNKHEAI-ITDLEDRLRKEE---------KQRQ-----ELEKNRRKLEGdSTDLHDQIAD 1063
Cdd:PRK04863 662 ERLSQPGGSEDPR---LNALAERFGGVlLSEIYDDVSLEDapyfsalygPARHaivvpDLSDAAEQLAG-LEDCPEDLYL 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1064 LQAQIADLRAQLANKeEELQNALI-----------RIEEEAA-ANMASQKKIKELEAQILELDEDLEREKFYRSKNgQRC 1131
Cdd:PRK04863 738 IEGDPDSFDDSVFSV-EELEKAVVvkiadrqwrysRFPEVPLfGRAAREKRIEQLRAEREELAERYATLSFDVQKL-QRL 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1132 KELEKELEAIKNKLDDTLDTTAAQQELRAKR---ETEVAQLrkaqEEENKMHESQiAELSKKHLQAFNEMNEQLeqakrN 1208
Cdd:PRK04863 816 HQAFSRFIGSHLAVAFEADPEAELRQLNRRRvelERALADH----ESQEQQQRSQ-LEQAKEGLSALNRLLPRL-----N 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1209 KLSVEkakqALESEFNELQIELKTLGQSKSDSeHRRKKAESQVQELQVKYgdcerqrQEAVEKIAKLQSELEnvnslLNE 1288
Cdd:PRK04863 886 LLADE----TLADRVEEIREQLDEAEEAKRFV-QQHGNALAQLEPIVSVL-------QSDPEQFEQLKQDYQ-----QAQ 948
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1289 SEGKNTKSSKDMLS----LESHL--QDTQELLQEETRQKLAISTRFRQMEEEQNSLRemleeeeeakknveKQISVLQGQ 1362
Cdd:PRK04863 949 QTQRDAKQQAFALTevvqRRAHFsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAR--------------EQLRQAQAQ 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1363 LGDMKKKMDQEVSSLESAEESRKRLQREFDTVKLQ----LEEKEAA-----YEKLERTKTRLQQELDDLLVNQDGLRQLV 1433
Cdd:PRK04863 1015 LAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPadsgAEERARArrdelHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
650
....*....|...
gi 768942001 1434 NNMERKQRKFDQM 1446
Cdd:PRK04863 1095 KKLRKLERDYHEM 1107
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1046-1307 |
4.72e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1046 NRRKLEGDSTD----------LHDQIADLQAQIADLRAQLANKEE--ELQNALI-RIEEEAAANMAS-QKKIKELEAQIL 1111
Cdd:PHA02562 151 ARRKLVEDLLDisvlsemdklNKDKIRELNQQIQTLDMKIDHIQQqiKTYNKNIeEQRKKNGENIARkQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1112 ELDEDLErekfyrskngqrckELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKaqeeENKMHE---------S 1182
Cdd:PHA02562 231 TIKAEIE--------------ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK----VIKMYEkggvcptctQ 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1183 QIAE----LSKKHLQAFnEMNEQLEQA--KRNKLSVEKAK-QALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQ 1255
Cdd:PHA02562 293 QISEgpdrITKIKDKLK-ELQHSLEKLdtAIDELEEIMDEfNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1256 VKYGDCErqrqeavEKIAKLQSELENVNSLLNESEGKntkssKDMLSLESHL 1307
Cdd:PHA02562 372 AEFVDNA-------EELAKLQDELDKIVKTKSELVKE-----KYHRGIVTDL 411
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
978-1427 |
4.78e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.42 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 978 MVLDDQNNKLNKEKKLlEDRIAEF-----------SSNLSEEEEksRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKN 1046
Cdd:PTZ00108 963 MVLFDENGKIKKYSDA-LDILKEFylvrldlykkrKEYLLGKLE--RELARLSNKVRFIKHVINGELVITNAKKKDLVKE 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1047 RRKLEGDStdlHDQIADLQAqiADLRAQLANKEEELQNALIRIEEEAAANMASQKKIkeLEAQILeldeDLEREKFyrsk 1126
Cdd:PTZ00108 1040 LKKLGYVR---FKDIIKKKS--EKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSMPIW----SLTKEKV---- 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1127 ngqrcKELEKELEAIKNKLDDTLDTTAAQQELRakretEVAQLRKAQEEENKMHESQIAELSKkhlqaFNEMNEQLEQAK 1206
Cdd:PTZ00108 1105 -----EKLNAELEKKEKELEKLKNTTPKDMWLE-----DLDKFEEALEEQEEVEEKEIAKEQR-----LKSKTKGKASKL 1169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1207 RNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVNSLL 1286
Cdd:PTZ00108 1170 RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNN 1249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1287 NESEGK-NTKSSKDMLSLESHLQDTQELLQEETRQKLAISTRfRQMEEEQNSLREMLEEeeeakknvekqisvlqgqlgd 1365
Cdd:PTZ00108 1250 SSKSSEdNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKR-PDGESNGGSKPSSPTK--------------------- 1307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1366 mKKKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQD 1427
Cdd:PTZ00108 1308 -KKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDD 1368
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1369-1730 |
4.83e-04 |
|
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: 44.67 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1369 KMDQEVSSLESAeesRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLlvnqdglRQLVNNMERKqrkfdqmLA 1448
Cdd:pfam19220 66 KLRRELAGLTRR---LSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK-------TAQAEALERQ-------LA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1449 EEKTISTQYAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATE 1528
Cdd:pfam19220 129 AETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1529 QQLEEIKTQLEELEDELQA------TEDAKLRLEVNMQAMKAQfdrDLQARDEQGEERRKQLVKQVHELEAELEDERRQR 1602
Cdd:pfam19220 209 ARLRALEGQLAAEQAERERaeaqleEAVEAHRAERASLRMKLE---ALTARAAATEQLLAEARNQLRDRDEAIRAAERRL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1603 SQAVSAKKKLELDLGELEvhidaankgrdealKQLKKLQVQFKDMMRESEDLrLSRDEAINSAKETEkkvktmeaDAAqf 1682
Cdd:pfam19220 286 KEASIERDTLERRLAGLE--------------ADLERRTQQFQEMQRARAEL-EERAEMLTKALAAK--------DAA-- 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 768942001 1683 qedLATAERLKRQMQAERDELQDEingnntknsmLQDEKRRLEARITQ 1730
Cdd:pfam19220 341 ---LERAEERIASLSDRIAELTKR----------FEVERAALEQANRR 375
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1652-1905 |
5.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1652 EDLRLSRDEAINSAKETEKKVKtmeadaaQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQL 1731
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLP-------ELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1732 EEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRlegarsqaerknkelslKLQELESTIKSKYkSSLTALEA 1811
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEA-----------------ELAELSARYTPNH-PDVIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1812 KVAQLEEQLDTEIKerqqatRMVRRTEKKMKELVLQVEDERRNTEQYKDQADKLNsrtrQLKRQLEEAEEEVTRANAYRR 1891
Cdd:COG3206 299 QIAALRAQLQQEAQ------RILASLEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYE 368
|
250
....*....|....
gi 768942001 1892 KLQRELEDANETQD 1905
Cdd:COG3206 369 SLLQRLEEARLAEA 382
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
952-1232 |
5.43e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 952 EEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIitdled 1031
Cdd:TIGR01612 1460 EMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSAL------ 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1032 rlrkeekqrqELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEAAANMASQKKIKELEAQIL 1111
Cdd:TIGR01612 1534 ----------AIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1112 ELDEDLEREKFYRSKNGQRCKELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKMHESQIAELSKKH 1191
Cdd:TIGR01612 1604 NFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEI 1683
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1192 LQAFNEMNEQL------------EQAKRNKLSVEKAKQALESEFNELQIELKT 1232
Cdd:TIGR01612 1684 EKIEIDVDQHKknyeigiiekikEIAIANKEEIESIKELIEPTIENLISSFNT 1736
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1026-1121 |
5.56e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1026 ITDLEDRLRKEEKQRQELEKNRRKLEGDS-TDLHDQIADLQAQIADLRAQLAnKEEELQNALIRIEEEAAAnmaSQKKIK 1104
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWE-AEKELIEEIQELKEELEQ---RYGKIP 488
|
90
....*....|....*..
gi 768942001 1105 ELEAQILELDEDLEREK 1121
Cdd:COG0542 489 ELEKELAELEEELAELA 505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1669-1843 |
5.59e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1669 EKKVKTMEADAAQFQED-LATAERLKRQMQAE--------RDELQDEINgnnTKNSMLQDEKRRLEARitqleeeLEEEQ 1739
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEALLEakeeihklRNEFEKELR---ERRNELQKLEKRLLQK-------EENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1740 LNSEMANDRNKRTTLQVDQLTAELsaersaaQRLEGARSQAERKNKELSLKLQELestikskykSSLTALEAKvAQLEEQ 1819
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQ-------QELEKKEEELEELIEEQLQELERI---------SGLTAEEAK-EILLEK 162
|
170 180
....*....|....*....|....
gi 768942001 1820 LDTEIkeRQQATRMVRRTEKKMKE 1843
Cdd:PRK12704 163 VEEEA--RHEAAVLIKEIEEEAKE 184
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
934-1393 |
5.75e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 934 ERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRiAEFSSNLSEEEEKSR 1013
Cdd:COG5185 84 KARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIA-DIEASYGEVETGIIK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1014 SLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIRIEEEA 1093
Cdd:COG5185 163 DIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1094 AANMASQKKIKELEaQILELDEDLEREKFYRSKngqrckELEKELEAIKNKLDDTLDTTAAQ-----QELRAKRETEVAQ 1168
Cdd:COG5185 243 SELEDLAQTSDKLE-KLVEQNTDLRLEKLGENA------ESSKRLNENANNLIKQFENTKEKiaeytKSIDIKKATESLE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1169 LRKAQEEENKMHESQIAELSKKHLQAFNEMNEQLEQAKRNklsVEKAKQALESEFNELQIElktlgQSKSDSEHRRKKAE 1248
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTEN---LEAIKEEIENIVGEVELS-----KSSEELDSFKDTIE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1249 SQVQELQVKYGDCERQRQEAVEKIAK----LQSELENVNSLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAI 1324
Cdd:COG5185 388 STKESLDEIPQNQRGYAQEILATLEDtlkaADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1325 STRfrqmeEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDT 1393
Cdd:COG5185 468 AYD-----EINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMR 531
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
927-1140 |
6.87e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 927 RVNQMLNERKKMQQNIADLEQQLDEeeadrqklqmekvtTDSKMK-ALEGNIMV--LDDQNNKLNKEKKLLEDRIAEFSS 1003
Cdd:PLN02939 157 DLEKILTEKEALQGKINILEMRLSE--------------TDARIKlAAQEKIHVeiLEEQLEKLRNELLIRGATEGLCVH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1004 NLSEEEEKSRSLQ-KLKNKHEAI------ITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLraqLA 1076
Cdd:PLN02939 223 SLSKELDVLKEENmLLKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC---WW 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1077 NKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKFYRSKN------GQRCKELEKELEA 1140
Cdd:PLN02939 300 EKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSykvellQQKLKLLEERLQA 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1437-1643 |
7.38e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1437 ERKQRKFDQMLAEEKTISTQYAEERDK-AEAEA-----REK------ETRALTLARELETITDLKNELERTNKQLKAEME 1504
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKElEEAEAaleefRQKnglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1505 DLVSSKDDAGKNVHELERSK--RATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRK 1582
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1583 QLVKQVHELEAELEDERRQRSQAvsakKKLELDLGELEVHIDAANKGRDEALKQLKKLQVQ 1643
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1763-1927 |
7.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1763 LSAERSAAQRLEGARSQAERKNKELSLKLQElestikskykssltaleaKVAQLEEQLDTEIKERQQAtrmVRRTEKKMK 1842
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKE------------------EIHKLRNEFEKELRERRNE---LQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1843 ELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRAnayRRKLQRELED-ANETQDTMNREV-NILKSKLRR 1920
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL---IEEQLQELERiSGLTAEEAKEILlEKVEEEARH 169
|
....*..
gi 768942001 1921 DLPFTIR 1927
Cdd:PRK12704 170 EAAVLIK 176
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1359-1548 |
8.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1359 LQGQLGDMKKKmdqevssLESAEESRKRLQREFDTVKLQlEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMER 1438
Cdd:COG3206 180 LEEQLPELRKE-------LEEAEAALEEFRQKNGLVDLS-EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1439 KQRK---------FDQMLAEEKTISTQYAEERDK--------AEAEAREKETRALTLARELETITDLKNE---LERTNKQ 1498
Cdd:COG3206 252 GPDAlpellqspvIQQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEleaLQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1499 LKAEMEDL---VSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQAT 1548
Cdd:COG3206 332 LQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
835-1051 |
8.91e-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: 44.34 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 835 LQVTRQEEEMLAKEdELSKVKEKQLQAEE---MIKEFESKQQQLNAEKM-ALQEQLQA-ETELCAEAEEMRARLVNRKQE 909
Cdd:pfam17380 383 LQMERQQKNERVRQ-ELEAARKVKILEEErqrKIQQQKVEMEQIRAEQEeARQREVRRlEEERAREMERVRLEEQERQQQ 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 910 LEEILHDMESRleeeeERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMekVTTDSKMKALEGNimvLDDQNNKLNK 989
Cdd:pfam17380 462 VERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKLLEKE---MEERQKAIYE 531
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768942001 990 EKkllEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQ--ELEKNRRKLE 1051
Cdd:pfam17380 532 EE---RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQivESEKARAEYE 592
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1121-1270 |
9.96e-04 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 43.88 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1121 KFYRSKNGQrcKELEKELEAIKNKLDDTLDTTAAQQelRAKREteVAQLRKAQEEENKMHESQIAELSKKhLQAFNEMNE 1200
Cdd:smart00435 222 KVFRTYNAS--ITLQEQLKELTAKDGNVAEKILAYN--RANRE--VAILCNHQRTVSKTHEKSMEKLQEK-IKALKYQLK 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1201 QLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVE 1270
Cdd:smart00435 295 RLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKKQIERLEERIEKLEVQATDKEE 364
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
928-1545 |
1.01e-03 |
|
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: 44.27 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 928 VNQMLNERKKMQQNIADLEQQLDEEEADRQ--------KLQMEKVTTDSKMKALEGNIMVLDD---QNNKLNKEKKLLED 996
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEEVKGINLSYGKnlgklfleKIDEEKKKSEHMIKAMEAYIEDLDEikeKSPEIENEMGIEMD 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 997 RIAEFSS-NLSEEEEKSRSLqkLKNKHEAIITDLEdrlrkeEKQRQELEKNRRKlegdsTDLHDQIADLQAQIADlrAQL 1075
Cdd:TIGR01612 1272 IKAEMETfNISHDDDKDHHI--ISKKHDENISDIR------EKSLKIIEDFSEE-----SDINDIKKELQKNLLD--AQK 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1076 ANKEEELQ-NALIRIEEEAAANMASQ--KKIKELEAQILELDEDLEREKFYRSKNGQRCKElEKELEAIKNKLDDTLDTT 1152
Cdd:TIGR01612 1337 HNSDINLYlNEIANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTLDDK 1415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1153 AAQQELRAKRETEVAQLrkAQEEENKMHESQIAELSKKHLQAFNEMnEQLEQAKRNKLSVEKAKQALESEFNelqieLKT 1232
Cdd:TIGR01612 1416 DIDECIKKIKELKNHIL--SEESNIDTYFKNADENNENVLLLFKNI-EMADNKSQHILKIKKDNATNDHDFN-----INE 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1233 LGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLqSELENVNSLlneseGKNTKSSKDMLS--LESHLQDT 1310
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKY-SALAIKNKF-----AKTKKDSEIIIKeiKDAHKKFI 1561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1311 QELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQgqLGDMKKKMDQEVSSLESAEesrkrlqre 1390
Cdd:TIGR01612 1562 LEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLK--ISDIKKKINDCLKETESIE--------- 1630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1391 fdtvklqleeKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVN---NMERKQRKFDQMLAEEKTISTQYAEERDKAEAE 1467
Cdd:TIGR01612 1631 ----------KKISSFSIDSQDTELKENGDNLNSLQEFLESLKDqkkNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIG 1700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1468 AREKETraltlarelETITDLKNELERTNKQLKAEMEDLVSSkddagKNVHELERSKraTEQQLEEIKTQLEELEDEL 1545
Cdd:TIGR01612 1701 IIEKIK---------EIAIANKEEIESIKELIEPTIENLISS-----FNTNDLEGID--PNEKLEEYNTEIGDIYEEF 1762
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
960-1228 |
1.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 960 QMEKVTTDsKMKALEGNIMVLDDQ----NNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLrk 1035
Cdd:PHA02562 167 EMDKLNKD-KIRELNQQIQTLDMKidhiQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1036 eekqrQELEKNRRKLEGDSTDLHDQIADLQAQIADLraqlaNKEEELQnalirieEEAAANMASQKKIKELEAQILELde 1115
Cdd:PHA02562 244 -----LNLVMDIEDPSAALNKLNTAAAKIKSKIEQF-----QKVIKMY-------EKGGVCPTCTQQISEGPDRITKI-- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1116 dlerekfyRSKNGQRCKELEKELEAIKN---KLDDTLDTTAAQQELRAKRETEVAQLrKAQEEENKMHESQIAELSKkhl 1192
Cdd:PHA02562 305 --------KDKLKELQHSLEKLDTAIDEleeIMDEFNEQSKKLLELKNKISTNKQSL-ITLVDKAKKVKAAIEELQA--- 372
|
250 260 270
....*....|....*....|....*....|....*.
gi 768942001 1193 qAFNEMNEQLEQAKRNKLSVEKAKQALESEFNELQI 1228
Cdd:PHA02562 373 -EFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1490-1616 |
1.10e-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: 43.90 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1490 NELERT-NKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFdR 1568
Cdd:pfam05911 676 NDLKTEeNKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESY-E 754
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 768942001 1569 DLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDL 1616
Cdd:pfam05911 755 DLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQL 802
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
836-1122 |
1.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILH 915
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 916 DMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLE 995
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 996 DRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQL 1075
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 768942001 1076 ANKEEELQNALIRIEEEAAANMASQKKIKELEAQILELDEDLEREKF 1122
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1312-1725 |
1.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1312 ELLQEETRQKLAISTRFRQMEEEQNSLREmleeeeeakknvekQISVLQGQLGDMKKKMDQ--EVSSLESAEESRKRLQR 1389
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEE--------------ELEELEAELEELREELEKleKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1390 EFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAEEKTISTQYAEERDKAEAEAR 1469
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1470 EKETRALTLARELETITDLKNELERTNKQ-------------------------------------LKAEMEDLVSSKDD 1512
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlglLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1513 AGKNVHELERSKRATEQQLEEIKTQLEEL----EDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQV 1588
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1589 HeleAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLKK--LQVQFKDMMRESEDLRLSRDEAINSAK 1666
Cdd:COG4717 380 G---VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1667 ETEKKVKTMEADaaqfqEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLE 1725
Cdd:COG4717 457 ELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1440-1602 |
1.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1440 QRKFDQMLAEEKTistQYAEERDKAEAEAREKetrALTLARELET-ITDLKNELERTNKQLKAEMEDLVSSKDDAGKNVH 1518
Cdd:PRK12704 37 EEEAKRILEEAKK---EAEAIKKEALLEAKEE---IHKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1519 ELERSKRATEQQLEEIKTQLEELEdELQATEDAKLRLEVNMQAMKAQfDRDLQARDEQGEERRKQLVKQVHElEAELEDE 1598
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELE-ELIEEQLQELERISGLTAEEAK-EILLEKVEEEARHEAAVLIKEIEE-EAKEEAD 187
|
....
gi 768942001 1599 RRQR 1602
Cdd:PRK12704 188 KKAK 191
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1204-1418 |
1.43e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1204 QAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVN 1283
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1284 SLLNESEGknTKSSKDMLsLEShlQDTQELLQEETRQKlAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQL 1363
Cdd:COG3883 93 RALYRSGG--SVSYLDVL-LGS--ESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 1364 GDMKKKMDQEVsslESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQE 1418
Cdd:COG3883 167 EAAKAELEAQQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1457-1615 |
1.51e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1457 YAEERDKAEAEAREKETRALTLARELETITDLKNELERTNKQLKAEmedlvsSKDDAGKNVHELERSKRATEQQLEEIKT 1536
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQE------ARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768942001 1537 qLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQvhELEAELEDERRQRSQAVSAKKKLELD 1615
Cdd:PRK12705 100 -LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLK--LLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1669-1888 |
1.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1669 EKKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDR 1748
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1749 NKRTTLQVDQLTAELSAE--RSAAQRLEGARSQAERKNKELslklqelestikSKYKSSLTALEAKVAQLEEQLDTEIKE 1826
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLL------------EELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768942001 1827 RQQAtrmvrrtEKKMKELVLQVEDERRNTEQYKDQADKLNSRTRQLKRQLEEAEEEVTRANA 1888
Cdd:COG3883 163 KAEL-------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1521-1625 |
1.90e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1521 ERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDEQGEERRKQLVK-QVHELEAELEDER 1599
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAE-AQQQELVALEGLAAELEEKQQELEAQLEQlQEKAAETSQERKQ 216
|
90 100
....*....|....*....|....*.
gi 768942001 1600 RQRSQAVSAKKKLELDLGELEVHIDA 1625
Cdd:PRK11448 217 KRKEITDQAAKRLELSEEETRILIDQ 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
867-1092 |
2.16e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 867 EFESKQQQLNAEKMALQEQLQAETELC-------AEAEEMRARLVN--RKQELEEILHDMESRLEEEEERVNQMLNERKK 937
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEAldklrsyLPKLNPLREEKKkvSVKSLEELIKDVEEELEKIEKEIKELEEEISE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 938 MQQNIADLEQQLDEEEadrqklqmekvttdsKMKALEGNIMVLDDQNN------KLNKEKKLLEDRIAEFSSNLSEEEEK 1011
Cdd:PRK05771 112 LENEIKELEQEIERLE---------------PWGNFDLDLSLLLGFKYvsvfvgTVPEDKLEELKLESDVENVEYISTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1012 SRS---LQKLKNKHEaiitDLEDRLRKEEKQRQELEKnrrklEGDSTD----LHDQIADLQAQIADLRAQLANKEEELQN 1084
Cdd:PRK05771 177 GYVyvvVVVLKELSD----EVEEELKKLGFERLELEE-----EGTPSElireIKEELEEIEKERESLLEELKELAKKYLE 247
|
....*...
gi 768942001 1085 ALIRIEEE 1092
Cdd:PRK05771 248 ELLALYEY 255
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
837-1336 |
2.19e-03 |
|
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: 43.20 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 837 VTRQEEEMLAKEDELSKVKEKQLQaeemikefesKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVN----------- 905
Cdd:pfam07111 68 ISRQLQELRRLEEEVRLLRETSLQ----------QKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGaemvrknleeg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 906 RKQELEEI--------------------------------LHDMESRLEEEEERVNQMLNE----RKKMQQNIADLEQQL 949
Cdd:pfam07111 138 SQRELEEIqrlhqeqlssltqaheealssltskaegleksLNSLETKRAGEAKQLAEAQKEaellRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 950 DEEEADRQKL------QMEKVTTDSKMKALEGNIMVLDDQNNKLNKEKKLLEDRIAEFSSNLS-EEEEKSRSLQKLKNKH 1022
Cdd:pfam07111 218 TLVESLRKYVgeqvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlQEEELTRKIQPSDSLE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1023 EAIITDLEDRLRkeeKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLANKEEELQnalirIEEEAAANMASQKK 1102
Cdd:pfam07111 298 PEFPKKCRSLLN---RWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQA-----ILQRALQDKAAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1103 IKELEAQILELdeDLEREKFYRSKNGQRCKELEKELEAIKNKLDDT---LDTTAAQQELRA------------------- 1160
Cdd:pfam07111 370 VERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTqiwLETTMTRVEQAVaripslsnrlsyavrkvht 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1161 -----KRETEVAQLR----------------------KAQEEENKMHESqiAELSKKHLQafNEMNEQLEQAKRNKLSVE 1213
Cdd:pfam07111 448 ikglmARKVALAQLRqescpppppappvdadlsleleQLREERNRLDAE--LQLSAHLIQ--QEVGRAREQGEAERQQLS 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1214 KAKQALESEFNELQIELKTLGQ----SKSDSEHRRKKAESQVQEL---QVKYGDCERQRQEAVEkiAKLQSELENVNSLL 1286
Cdd:pfam07111 524 EVAQQLEQELQRAQESLASVGQqlevARQGQQESTEEAASLRQELtqqQEIYGQALQEKVAEVE--TRLREQLSDTKRRL 601
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1287 NESEGKNTKSSKDMLSLESHL----QDTQEL--LQEETRQKLA--ISTRFRQMEEEQN 1336
Cdd:pfam07111 602 NEARREQAKAVVSLRQIQHRAtqekERNQELrrLQDEARKEEGqrLARRVQELERDKN 659
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1219-1604 |
2.34e-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: 42.75 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1219 LESEFNELQIELKTLGQSKSDSEHRRKKAESQVQELQvkygdcerQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSK 1298
Cdd:pfam05622 64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQ--------HRNEELTSLAEEAQALKDEMDILRESSDKVKKLEA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1299 DMLSLESHLQDTQEL-----LQEETRQKLAISTRfrQMEEEqnslremleeeeeakknvEKQISVLQGQLgDMKKKMDQE 1373
Cdd:pfam05622 136 TVETYKKKLEDLGDLrrqvkLLEERNAEYMQRTL--QLEEE------------------LKKANALRGQL-ETYKRQVQE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1374 VSSLESAEESRkrlqrefdTVKLQLEekeaaYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQmLAEEKTI 1453
Cdd:pfam05622 195 LHGKLSEESKK--------ADKLEFE-----YKKLEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAE-LSQADAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1454 STQYAEERDKAEAEAREKETRaltlarelETITDLKNElertNKQLKAEME--------DLVSSKDDAGKNVHELERSKR 1525
Cdd:pfam05622 261 LSPSSDPGDNLAAEIMPAEIR--------EKLIRLQHE----NKMLRLGQEgsyrerltELQQLLEDANRRKNELETQNR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1526 ATEQQLEEIKTQLEELEDELQA----TEDA---KLRLEVNM-QAMKAQfdRDLQARDEQGEERRKQLVKQVHELEAELED 1597
Cdd:pfam05622 329 LANQRILELQQQVEELQKALQEqgskAEDSsllKQKLEEHLeKLHEAQ--SELQKKKEQIEELEPKQDSNLAQKIDELQE 406
|
....*..
gi 768942001 1598 ERRQRSQ 1604
Cdd:pfam05622 407 ALRKKDE 413
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
842-1045 |
2.42e-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: 41.55 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 842 EEMLAKEDELSKVKEKQLQAEEMIKEFESKQQQLNAEKMALQEQLQ-AETEL--------------------CAEAEEMR 900
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlLEEELerteerlaealekleeaekaADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 901 ARLVNRKQELEEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVTTDSKMKALEGNIMVL 980
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768942001 981 DDQNNKLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEK 1045
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1616-1788 |
3.05e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1616 LGELEVHIDAAN-KGRDEALK----QLKKLQVQFKDMMRESEDLRlSRDEAINSAKETEKKVKTMeadaAQFQEDLAtae 1690
Cdd:COG3524 160 LAESEELVNQLSeRAREDAVRfaeeEVERAEERLRDAREALLAFR-NRNGILDPEATAEALLQLI----ATLEGQLA--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1691 rlkrQMQAERDELQDEINGNNTKNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELsAERSAA 1770
Cdd:COG3524 232 ----ELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLLAEYERLELEREFAEK-AYTSAL 306
|
170
....*....|....*...
gi 768942001 1771 QRLEGARSQAERKNKELS 1788
Cdd:COG3524 307 AALEQARIEAARQQRYLA 324
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1099-1449 |
3.17e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.53 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1099 SQKKIKELEAQILELDEDLEREKFYRSKngQRCKELEKELEAIKNKLDDTLDttaaqqelrakretEVAQLRKaQEEENK 1178
Cdd:pfam06160 58 VTKSLPDIEELLFEAEELNDKYRFKKAK--KALDEIEELLDDIEEDIKQILE--------------ELDELLE-SEEKNR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1179 mheSQIAELSKKhlqaFNEMNEQLEQakrNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHrrKKAESQVQELQVKY 1258
Cdd:pfam06160 121 ---EEVEELKDK----YRELRKTLLA---NRFSYGPAIDELEKQLAEIEEEFSQFEELTESGDY--LEAREVLEKLEEET 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1259 GDCERQRQEAVEKIAKLQSE----LENVNSLLNESEGKN-----TKSSKDMLSLESHLQDTQELLQ----EETRQKLais 1325
Cdd:pfam06160 189 DALEELMEDIPPLYEELKTElpdqLEELKEGYREMEEEGyalehLNVDKEIQQLEEQLEENLALLEnlelDEAEEAL--- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1326 trfRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQ-----------------EVSSLESAEESRKRLQ 1388
Cdd:pfam06160 266 ---EEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKElkeelervqqsytlnenELERVRGLEKQLEELE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768942001 1389 REFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQLVNNMERKQRKFDQMLAE 1449
Cdd:pfam06160 343 KRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1060-1174 |
3.48e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 41.57 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1060 QIADLQAQIADLRAQLANKEEELqNALIRIEEEAAANMASQKKIKELEAQILELDEDLErekfyrsknGQRCKELEKELE 1139
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRL-AALEAAPAAAAATAALEARLAALRAALAAAREAVA---------AAAAAALEARLA 70
|
90 100 110
....*....|....*....|....*....|....*
gi 768942001 1140 AIKNKLdDTLDTTAAQQELRAKRETEVAQLRKAQE 1174
Cdd:COG4223 71 ALEAKA-AAPEAEAAAAARAAALALAAAALRAAVE 104
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
948-1088 |
3.49e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 948 QLDEEEADRQKLQMEkvttdSKMKALEGNIMVLDDQNNkLNKEKKLLEDRIAEFSSNLSEEEEKSRSLQKLKNKHEAIIT 1027
Cdd:COG1566 75 RLDPTDLQAALAQAE-----AQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1028 DLEDRLRKEEKQRQELEKNRRKLE--GDSTDLHDQIADLQAQIADLRAQLANKEEELQNALIR 1088
Cdd:COG1566 149 ELDEARAALDAAQAQLEAAQAQLAqaQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1528-1645 |
3.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1528 EQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVS 1607
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110
....*....|....*....|....*....|....*...
gi 768942001 1608 AKkklelDLGELEVHIDAANKGRDEALKQLKKLQVQFK 1645
Cdd:PRK00409 606 AH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
788-1291 |
3.88e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 788 RGYVARKAFTKRQQQLTAMKVIQRNCAAYLKLRNWQ-----WWRLFTKVK-PLLQVTRQEEEMLAKEDELSKVKEK--QL 859
Cdd:PRK10246 327 RARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNnelagWRAQFSQQTsDREQLRQWQQQLTHAEQKLNALPAItlTL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 860 QAEEMIKEFE--SKQQQLNAEKMALQEQLQAETELCAEAEEMRARLVNRKQELEEILHDMESRLEEEeervNQMLNERKK 937
Cdd:PRK10246 407 TADEVAAALAqhAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEK----TQQLADVKT 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 938 M---QQNIADLEQQLD--------------EEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQN----NKLNKEKKLLED 996
Cdd:PRK10246 483 IceqEARIKDLEAQRAqlqagqpcplcgstSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGaalrGQLDALTKQLQR 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 997 RIAEFSSNLSEEEEKSRSLQKL---KNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEgdstdLHDQIADLQAQIADLRA 1073
Cdd:PRK10246 563 DESEAQSLRQEEQALTQQWQAVcasLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQ 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1074 QLANKEEELQNALIRI-----------------EEEAAANMASQKKIKELEAQILEL----------DEDLEREKFYRSK 1126
Cdd:PRK10246 638 QIEQRQQQLLTALAGYaltlpqedeeaswlatrQQEAQSWQQRQNELTALQNRIQQLtplletlpqsDDLPHSEETVALD 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1127 NGQ----RCKELEKELEAIKNKLddTLDTTAAQQE-------LRAKR-ETEVAQLRKAQEEENKMHESQIAELSKKHLQA 1194
Cdd:PRK10246 718 NWRqvheQCLSLHSQLQTLQQQD--VLEAQRLQKAqaqfdtaLQASVfDDQQAFLAALLDEETLTQLEQLKQNLENQRQQ 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1195 FNEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKSDSEHRRKKAESQVQElqvkygDCE-RQRQEAV-EKI 1272
Cdd:PRK10246 796 AQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQ------DADnRQQQQALmQQI 869
|
570 580
....*....|....*....|..
gi 768942001 1273 AKLQSELEN---VNSLLNESEG 1291
Cdd:PRK10246 870 AQATQQVEDwgyLNSLIGSKEG 891
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
990-1243 |
4.12e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 42.23 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 990 EKKLLEDRIaefssNLSEEEEKSRSLQklknkhEAIITDLEDRLRKEEKQRQELEKNRR-----------KLEGDSTDLh 1058
Cdd:PLN03188 1046 EKKLEQERL-----RWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1059 DQIADLQAQiadlRAQLANKEEELQNALIRIEEEAA---ANMASQKKIKELEAQILELDEDLEREKFYrskngqrckeLE 1135
Cdd:PLN03188 1114 EQYADLEEK----HIQLLARHRRIQEGIDDVKKAAAragVRGAESKFINALAAEISALKVEREKERRY----------LR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1136 KELEAIKNKLDDTLDTTAAQQEL--RAKRETE---VAQlRKAQEEENKMHES--QIAELSKKHLQAFNEMNEQLEQAKrn 1208
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEaltVAQ-KRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESR-- 1256
|
250 260 270
....*....|....*....|....*....|....*
gi 768942001 1209 klsveKAKQALESEFNELQIELKTLGQSKSDSEHR 1243
Cdd:PLN03188 1257 -----LPKEAIRPACNDDCMAKYDAGEPLSEGDQQ 1286
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
836-1084 |
4.15e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQAEEmikefESKQQQLNAEKMALQEQLQaetELCAEAEEMRArlvnrkqeleeilh 915
Cdd:pfam05667 299 RFTHTEKLQFTNEAPAATSSPPTKVETE-----EELQQQREEELEELQEQLE---DLESSIQELEK-------------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 916 dmesrleeeeervnqmlnERKKMQQNIADLEQQLDEEEADRQKLQMEKvttDSKMKALEgniMVLDDQNN--KLNKEKKL 993
Cdd:pfam05667 357 ------------------EIKKLESSIKQVEEELEELKEQNEELEKQY---KVKKKTLD---LLPDAEENiaKLQALVDA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 994 LEDRIAEfssnLSEEEEKSRSlqKLKNKHEAIitdledrlrKEEKQRQELEKnRRKLEgdstdlhdQIADLQAQIADLRA 1073
Cdd:pfam05667 413 SAQRLVE----LAGQWEKHRV--PLIEEYRAL---------KEAKSNKEDES-QRKLE--------EIKELREKIKEVAE 468
|
250
....*....|.
gi 768942001 1074 QLANKEEELQN 1084
Cdd:pfam05667 469 EAKQKEELYKQ 479
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
834-1098 |
4.47e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 834 LLQVTRQEEEMLAKED-------ELSKVKekqLQAEEmIKEFESKQQQL-NAEKmaLQEQLQAETELCAEAEEMRARLVN 905
Cdd:COG0497 174 LEELRADEAERARELDllrfqleELEAAA---LQPGE-EEELEEERRRLsNAEK--LREALQEALEALSGGEGGALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 906 R-KQELEEILhDMESRLEEEEERVNQMLNErkkMQQNIADLEQQLDEEEADRQKLQMekvttdskmkalegnimvlddqn 984
Cdd:COG0497 248 QaLRALERLA-EYDPSLAELAERLESALIE---LEEAASELRRYLDSLEFDPERLEE----------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 985 nklnkekklLEDRIAEfssnlseeeeksrsLQKLKNKHEAiitDLEDRLRKEEKQRQELEKnrrkLEGDSTDlhdqIADL 1064
Cdd:COG0497 301 ---------VEERLAL--------------LRRLARKYGV---TVEELLAYAEELRAELAE----LENSDER----LEEL 346
|
250 260 270
....*....|....*....|....*....|....*...
gi 768942001 1065 QAQIADLRAQLANKEEEL----QNALIRIEEEAAANMA 1098
Cdd:COG0497 347 EAELAEAEAELLEAAEKLsaarKKAAKKLEKAVTAELA 384
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
918-1109 |
4.53e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 918 ESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQKLQMEKVttdskmkalegnimvLDDQNNKLNKekklLEDR 997
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKE---------------LRERRNELQK----LEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 998 IAEFSSNLseeEEKSRSLQKLKNKHEAIITDLEDRLRKEEKQRQELEKN----RRKLEgdstdlhdQIADLQAQIAdlRA 1073
Cdd:PRK12704 91 LLQKEENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELieeqLQELE--------RISGLTAEEA--KE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768942001 1074 QLANK-EEELQN---ALIR-IEEEAAANmaSQKKIKELEAQ 1109
Cdd:PRK12704 158 ILLEKvEEEARHeaaVLIKeIEEEAKEE--ADKKAKEILAQ 196
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1789-1922 |
4.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1789 LKLQELESTIKsKYKSSLTALEAKVAQLEEQLDTEIKERQQATRMVRRTEKKMKELVLQVEDERRNTEQYKDQ------- 1861
Cdd:COG1579 10 LDLQELDSELD-RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnn 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768942001 1862 --ADKLNSRTRQLKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREVNILKSKLRRDL 1922
Cdd:COG1579 89 keYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1019-1166 |
4.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1019 KNKHEAIITDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADLQAQIADLRAQLankEEELQNALIRIEEEAAanma 1098
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEAD---- 587
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1099 sqKKIKELEAQILELDEDLErekfyrskngqrckelEKELEAIKNKLDDTLDTTAAQQELRAKRETEV 1166
Cdd:PRK00409 588 --EIIKELRQLQKGGYASVK----------------AHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
927-1107 |
4.74e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 927 RVNQMlNERKKMQQnIADLEQQLDEEEADRQKLQMEKVTTDSKMKAL--EGNIMVLDDQNNKLNKEKKLLEDRIAEFSSN 1004
Cdd:COG3524 166 LVNQL-SERAREDA-VRFAEEEVERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1005 LSEEeekSRSLQKLKNKHEAIitdledrlrkeekqRQELEKNRRKLEGDSTDlhDQIADLQAQIADLRAQLANKEEELQN 1084
Cdd:COG3524 244 LSPN---SPQVRQLRRRIAAL--------------EKQIAAERARLTGASGG--DSLASLLAEYERLELEREFAEKAYTS 304
|
170 180
....*....|....*....|...
gi 768942001 1085 ALIRIEeeaAANMASQKKIKELE 1107
Cdd:COG3524 305 ALAALE---QARIEAARQQRYLA 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1745-1911 |
5.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1745 ANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQAERKNKELSLKLQELESTIKSKyKSSLTALEAKVAQLEEQLDTEI 1824
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-QAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1825 KERQQA----------------------TRMVRRTEKKMKELVLQVEDERRNTEQYKDQADK-----------LNSRTRQ 1871
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAklaelealkaeLEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768942001 1872 LKRQLEEAEEEVTRANAYRRKLQRELEDANETQDTMNREV 1911
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
836-1400 |
5.21e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 836 QVTRQEEEMLAKEDELSKVKEKQLQA-EEMIKEFESKQQQLNAEKMAL-QEQLQAETELCAEAEemrARLVNRKQELEEI 913
Cdd:PRK10246 240 QQQQQSLNWLTRLDELQQEASRRQQAlQQALAAEEKAQPQLAALSLAQpARQLRPHWERIQEQS---AALAHTRQQIEEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 914 LHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQLDEEEADRQ--------KLQMEKVTTD-SKMKALEGNIMVLddqn 984
Cdd:PRK10246 317 NTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQwnnelagwRAQFSQQTSDrEQLRQWQQQLTHA---- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 985 nklnkEKKLleDRIAEFSSNLSEEEEKSRSLQKLKNKheaiitDLEDRLRKEEKQRQELEKNRRKLEGDSTDLHDQIADL 1064
Cdd:PRK10246 393 -----EQKL--NALPAITLTLTADEVAAALAQHAEQR------PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1065 QAQIADLRAQLANKEEELQNALIRIEEEAaanmasqkKIKELEAQILELD-----------EDLEREKFYR---SKNGQR 1130
Cdd:PRK10246 460 NAALNEMRQRYKEKTQQLADVKTICEQEA--------RIKDLEAQRAQLQagqpcplcgstSHPAVEAYQAlepGVNQSR 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1131 CKELEKELEAIK----------NKLDDTL--DTTAAQ------QELRAKRETEVAQL---RKAQEE------ENKMHESQ 1183
Cdd:PRK10246 532 LDALEKEVKKLGeegaalrgqlDALTKQLqrDESEAQslrqeeQALTQQWQAVCASLnitLQPQDDiqpwldAQEEHERQ 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1184 IAELSKKH-LQAfnEMNEQLEQAKRNKLSVEKAKQALESEFNELQIELKTLGQSKS-----DSEHRR-KKAESQVQELQV 1256
Cdd:PRK10246 612 LRLLSQRHeLQG--QIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASwlatrQQEAQSwQQRQNELTALQN 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1257 KYGDCE---------------------RQRQEAVEKIAKLQSELENVNSLLNESEGKNTKSSKDMLS-LESHLQDTQE-- 1312
Cdd:PRK10246 690 RIQQLTplletlpqsddlphseetvalDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTaLQASVFDDQQaf 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1313 ---LLQEETRQKL---------------AISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEV 1374
Cdd:PRK10246 770 laaLLDEETLTQLeqlkqnlenqrqqaqTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIR 849
|
650 660
....*....|....*....|....*....
gi 768942001 1375 SSLESAEESRKRLQ---REFDTVKLQLEE 1400
Cdd:PRK10246 850 QQLKQDADNRQQQQalmQQIAQATQQVED 878
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1368-1693 |
6.67e-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: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1368 KKMDQEVSSLESAEESRKRLQREFDTVKLQLEEKEAAYEKLERTktrlqqeldDLLVNQDGLRQLVNNMERKQRKFDQML 1447
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAT---------ESLEEQLAAAEAEQELEESKRETETGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1448 AEEKTISTQYAEERDKAEAEAREKETRALT---LARELETITDLKNELERTNKQLKAEMEDLVSSKDDAGKNvheLERSK 1524
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENIVGeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---LEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1525 RATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARdeqGEERRKQLVKQVHELEAELEDERRQRSQ 1604
Cdd:COG5185 416 KAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR---LEEAYDEINRSVRSKKEDLNEELTQIES 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1605 AVSAKKKleldlgELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVktmEADAAQFQE 1684
Cdd:COG5185 493 RVSTLKA------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS---NAKTDGQAA 563
|
....*....
gi 768942001 1685 DLATAERLK 1693
Cdd:COG5185 564 NLRTAVIDE 572
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1629-1817 |
6.88e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1629 GRDEALKQLKKLQVQFKDMmresedLRLSRDEAinsaketekkvKTMEADAAQFQEDLATAERLKRQMQAERDELQDEIN 1708
Cdd:PRK09039 50 GKDSALDRLNSQIAELADL------LSLERQGN-----------QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1709 gnntknsmlqdekrRLEARITQLEEELEEEQLNSEMANDrnkrttlQVDQLTAELSAERSAAQRLEGARSQAERKNKELS 1788
Cdd:PRK09039 113 --------------AAEGRAGELAQELDSEKQVSARALA-------QVELLNQQIAALRRQLAALEAALDASEKRDRESQ 171
|
170 180
....*....|....*....|....*....
gi 768942001 1789 LKLQELESTIKskyksslTALEAKVAQLE 1817
Cdd:PRK09039 172 AKIADLGRRLN-------VALAQRVQELN 193
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1447-1608 |
7.24e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.54 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1447 LAEEktISTQYAEERDKAEAEAREKETRALtLARELeTITDLKNELERTnKQLKAEMEDLvsskddagknvhELERSKRA 1526
Cdd:PTZ00491 655 LAIE--ITTKSQEAAARHQAELLEQEARGR-LERQK-MHDKAKAEEQRT-KLLELQAESA------------AVESSGQS 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1527 TEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQGEERRKQLVKQVHELEAELED-ERRQRSQA 1605
Cdd:PTZ00491 718 RAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEK----LRKRQELELEYEQAQNELEIAKAKELADiEATKFERI 793
|
...
gi 768942001 1606 VSA 1608
Cdd:PTZ00491 794 VEA 796
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1480-1639 |
7.66e-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: 40.29 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1480 RELETITDLKNELERTNKQLKAEMEDLvsskDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNM 1559
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAEL----AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1560 QAMKAQFD-RDLQARDEQGEERRKQLVKQVHELEAELEDERRQRSQAVSAKKKLELDLGELEVHIDAANKGRDEALKQLK 1638
Cdd:COG1579 83 GNVRNNKEyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
.
gi 768942001 1639 K 1639
Cdd:COG1579 163 A 163
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
871-1119 |
7.93e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 871 KQQQLNAEKMALQEQLqaetelcAEAEEMRARLVNRKQEL-EEILHDMESRLEEEEERVNQMLNERKKMQQNIADLEQQL 949
Cdd:pfam00038 19 KVRFLEQQNKLLETKI-------SELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 950 DEEEADRQKLQMEKVTTDSKMKALEGNIMVLDDQNNKLNKE----KKLLEDRIAEFSSNLSEEE-----------EKSRS 1014
Cdd:pfam00038 92 EDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElaflKKNHEEEVRELQAQVSDTQvnvemdaarklDLTSA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1015 LQKLKNKHEAIItdledrlrkeEKQRQELEKN-RRKLE---------GDS--------TDLHDQIADLQAQIADLRAQLA 1076
Cdd:pfam00038 172 LAEIRAQYEEIA----------AKNREEAEEWyQSKLEelqqaaarnGDAlrsakeeiTELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 768942001 1077 NkeeeLQNALIRIEEEAAANMAS-QKKIKELEAQILELDEDLER 1119
Cdd:pfam00038 242 S----LERQLAETEERYELQLADyQELISELEAELQETRQEMAR 281
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1272-1918 |
8.05e-03 |
|
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: 41.35 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1272 IAKLQSELEnvnSLLNESEGKNTKSSKDMLSLES----HLQDTQELLQEETRQKLAISTRFRQMEEEQNSLREMLEEEEE 1347
Cdd:pfam10174 5 LRDLQRENE---LLRRELDIKESKLGSSMNSIKTfwspELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1348 AKKNVEKQISVLQGQLGDMKKKMDQEVSSLESAEESRKRLQREFDTvklQLEEKEAAYEKLERTKTRLQQELDDLLVNQD 1427
Cdd:pfam10174 82 ELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHER---QAKELFLLRKTLEEMELRIETQKQTLGARDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1428 GLRQLVNNMERK-----QRKFDQMLAEEKTISTQYA-------EERDKAEAEAREKETRALTLARE------LETITDLK 1489
Cdd:pfam10174 159 SIKKLLEMLQSKglpkkSGEEDWERTRRIAEAEMQLghlevllDQKEKENIHLREELHRRNQLQPDpaktkaLQTVIEMK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1490 N----ELERTNKQLKAEMEDLVSSKDDAGKNVHELERSKRATEQQLEEIKTQLEELEDELQATEDAKLRLEVNMQAMKAQ 1565
Cdd:pfam10174 239 DtkisSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1566 FDRDLQARD------EQGEERRKQLVKQVHELEAELEDERR-------QRSQAVSAKKKLELDLGELEVHIDAANKGRDE 1632
Cdd:pfam10174 319 NSDCKQHIEvlkeslTAKEQRAAILQTEVDALRLRLEEKESflnkktkQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1633 ALKQLKKLQVQFKDMMRESEDLRLSRDEAINSAKETEKKVKTMEADAAqfqEDLATAERLKRQMQAERDELQDEINGNNT 1712
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS---EKERIIERLKEQREREDRERLEELESLKK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1713 KNSMLQDEKRRLEARITQLEEELEEEQLNSEMANDRNKRTTLQVDQLTAELSAERSAAQRLEGARSQA------ERKNKE 1786
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAhnaeeaVRTNPE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1787 LSLKLQELESTIKSkYKSSLTALEAKVAQLEEQL-DTEIKERQQatrmvrrtEKKMKELvlqvedERRNTEQYKDQADK- 1864
Cdd:pfam10174 556 INDRIRLLEQEVAR-YKEESGKAQAEVERLLGILrEVENEKNDK--------DKKIAEL------ESLTLRQMKEQNKKv 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 768942001 1865 --LNSRTRQLKRQLEEAEEEVTRA--NAYRRKLQRELEDANETQDTMNREVNILKSKL 1918
Cdd:pfam10174 621 anIKHGQQEMKKKGAQLLEEARRRedNLADNSQQLQLEELMGALEKTRQELDATKARL 678
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1437-1602 |
8.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1437 ERKQRKFDQMLAEEKTISTQYAEERDKAEAEAREKETRALTLAREletitDLKNELER---TNKQLKAEMEDLVSSKDda 1513
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-----ELQREEERlvqKEEQLDARAEKLDNLEN-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1514 gknvhELERSKRATEQQLEEIKTQLEELEDELQatEDAKLRLEVNMQAMKAQFDRDLqardeqgEERRKQLVKQVHElEA 1593
Cdd:PRK12705 106 -----QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EA 170
|
....*....
gi 768942001 1594 ELEDERRQR 1602
Cdd:PRK12705 171 DLEAERKAQ 179
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1132-1325 |
8.45e-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: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1132 KELEKELEAIKNKLDDTLDTTAAQQELRAKRETEVAQLRKAQEEENKmhesQIAELSKKHLQAFNEMNEQLEQAKRNKLS 1211
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAEAEAEIEERREELGERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1212 VEKAKQALESE-FNEL--QIE-LKTLGQSKSDS----EHRRKKAESQVQELQVKYGDCERQRQEAVEKIAKLQSELENVN 1283
Cdd:COG3883 102 VSYLDVLLGSEsFSDFldRLSaLSKIADADADLleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768942001 1284 SLLNESEGKNTKSSKDMLSLESHLQDTQELLQEETRQKLAIS 1325
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1154-1709 |
9.34e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 41.08 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1154 AQQELRAKRETEVA---QLRK----AQEEE--NKMHESQIAELSKKHLQAFNEMNEQLeQAKRNKLSVEKAKQALESEFN 1224
Cdd:pfam15818 12 ALEELRMRREAETQyeeQIGKiiveTQELKwqKETLQNQKETLAKQHKEAMAVFKKQL-QMKMCALEEEKGKYQLATEIK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1225 ELQIE-----LKTLGQSKSDSEHRRKKAESQVQELQVKYGDCERQRQEavekIAKLQSELENVNSLLNESEGKNTKSSKD 1299
Cdd:pfam15818 91 EKEIEglketLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNE----IEKYYATITGQFGLVKENHGKLEQNVQE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1300 MLSLESHLQDTQEllqeetRQKLAISTRFRQMEEEQNSLREMLEEEEEAKKNVEKQISVLQGQLGDMKKKMDQEVSSLES 1379
Cdd:pfam15818 167 AIQLNKRLSALNK------KQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1380 AEESRKRLQREFDTVKLQLEEKEAAYEKLERTKTRLQQELDDLLVNQDGLRQlVNNMERKQRKFDqmlaEEKTISTQYAE 1459
Cdd:pfam15818 241 INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLER-DNELQREKVKEN----EEKFLNLQNEH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1460 ERDKAEAEAREKEtraltLARELETITDLKNELERTNKQLKAEMEDLVSSK----DDAGKNVHEL-ERSKRATEQQLEEI 1534
Cdd:pfam15818 316 EKALGTWKKHVEE-----LNGEINEIKNELSSLKETHIKLQEHYNKLCNQKkfeeDKKFQNVPEVnNENSEMSTEKSENL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1535 KTQ-------------------LEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEERRKQLVKQVHELEAEL 1595
Cdd:pfam15818 391 IIQkynseqeireentksfcsdTEYRETEKKKGPPVEEIIIEDLQVLEKSFKNEIDTSVPQDKNQSEISLSKTLCTDKDL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942001 1596 EDERR-------QRSQAVSAKKKLELD----------LGELEVHIDAANKGRDEALKQLKKLQVQFKDMMRESEDLRLSR 1658
Cdd:pfam15818 471 ISQGQtlnvtdfRKSVTTEIKDKLCLEkdngcsefksPNNLFLVADQSIETEKIHLESTEGLGLHHADIHLETESNRSSF 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 768942001 1659 DEAIN-SAKETE--KKVKTMEADAAQFQEDLATAERLKRQMQAERDELQDEING 1709
Cdd:pfam15818 551 NGTLNeMAHNTNhnKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAGLDS 604
|
|
| |
