NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034599859|ref|XP_016880170|]
View 

myosin-10 isoform X6 [Homo sapiens]

Protein Classification

MYSc_Myh10 and Myosin_tail_1 domain-containing protein (domain architecture ID 12036895)

protein containing domains Myosin_N, MYSc_Myh10, and Myosin_tail_1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

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 ...
848-1928 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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 1487.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  848 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLIEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  928 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDR 1007
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1008 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAK 1087
Cdd:pfam01576  161 ISEFTSNLAEEEEKVKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1088 KEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1167
Cdd:pfam01576  241 KEEELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1168 LRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1247
Cdd:pfam01576  321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELSEQLEQAKRNKANLEKAKQALESENNELQAELKTLQQAK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1248 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1327
Cdd:pfam01576  401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLSEAEGKSIKLSKDVSSLESQLQDTQELLQEE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1328 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQR 1407
Cdd:pfam01576  481 TRQKLNLSSRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQR 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1408 LEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALS 1487
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1488 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576  641 LSRALEEALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1568 NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1647
Cdd:pfam01576  721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRDEAVKQL 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSAL 1727
Cdd:pfam01576  801 KKLQAQMKELQRELEETRASRDEILAQSKESEKKLKSLEAELLQLQEDLAASERAKRQAQQERDELADEIANGASGKSAL 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1728 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1807
Cdd:pfam01576  881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAERSFSQKSESARQQLERQNKELKAKLQEMEGT 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1808 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1887
Cdd:pfam01576  961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKANSRMKQLKRQLE 1040
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|.
gi 1034599859 1888 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAESMNREVSTLRSKL 1081
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-771 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  Cd Length: 673  Bit Score: 1451.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920    161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920    321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14920    401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14920    481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920    561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1034599859  739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920    641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
33-72 1.12e-08

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: 397036  Cd Length: 39  Bit Score: 52.38  E-value: 1.12e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034599859   33 KKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVN 72
Cdd:pfam02736    1 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVK 39
 
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 ...
848-1928 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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 1487.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  848 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLIEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  928 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDR 1007
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1008 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAK 1087
Cdd:pfam01576  161 ISEFTSNLAEEEEKVKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1088 KEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1167
Cdd:pfam01576  241 KEEELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1168 LRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1247
Cdd:pfam01576  321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELSEQLEQAKRNKANLEKAKQALESENNELQAELKTLQQAK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1248 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1327
Cdd:pfam01576  401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLSEAEGKSIKLSKDVSSLESQLQDTQELLQEE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1328 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQR 1407
Cdd:pfam01576  481 TRQKLNLSSRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQR 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1408 LEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALS 1487
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1488 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576  641 LSRALEEALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1568 NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1647
Cdd:pfam01576  721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRDEAVKQL 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSAL 1727
Cdd:pfam01576  801 KKLQAQMKELQRELEETRASRDEILAQSKESEKKLKSLEAELLQLQEDLAASERAKRQAQQERDELADEIANGASGKSAL 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1728 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1807
Cdd:pfam01576  881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAERSFSQKSESARQQLERQNKELKAKLQEMEGT 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1808 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1887
Cdd:pfam01576  961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKANSRMKQLKRQLE 1040
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|.
gi 1034599859 1888 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAESMNREVSTLRSKL 1081
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-771 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  Cd Length: 673  Bit Score: 1451.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920    161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920    321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14920    401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14920    481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920    561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1034599859  739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920    641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
Myosin_head pfam00063
Myosin head (motor domain);
87-771 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 1115.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  247 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDN 325
Cdd:pfam00063  157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:pfam00063  237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  566 PRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETafgsAYKT 645
Cdd:pfam00063  474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  646 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063  549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1034599859  726 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063  629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
80-783 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  Cd Length: 677  Bit Score: 1021.32  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859    80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 239
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIP 318
Cdd:smart00242  155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGgCLTVD 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   319 GQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGMNVMEFTRAIL 397
Cdd:smart00242  235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   398 TPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242  315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQ 557
Cdd:smart00242  394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   558 GSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtet 637
Cdd:smart00242  471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   638 afGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242  534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034599859   718 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 783
Cdd:smart00242  612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
COG5022 COG5022
Myosin heavy chain [General function prediction only];
36-1348 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 922.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022     12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022     92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  191 VIQYLAHVASSHkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022    172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  271 AVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKV 349
Cdd:COG5022    247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  350 VSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022    327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  430 ERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022    406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  510 DFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCIIHYAGKVDYK 587
Cdd:COG5022    485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  588 ADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVgldqvtgmtetafgsayktKKGMFRTVGQLYKESLTKLMAT 667
Cdd:COG5022    561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  668 LRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMDG 743
Cdd:COG5022    622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  744 KQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKVLQRNC 823
Cdd:COG5022    702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  824 AAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTKVEGELEEMERKHQqlleeknilAEQLQAETE 901
Cdd:COG5022    782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREKKLRETEEVEFSLK---------AEVLIQKFG 852
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  902 LFAEAEEMRARLaaKKQELEEilhdlesrveeeeernQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIK 981
Cdd:COG5022    853 RSLKAKKRFSLL--KKETIYL----------------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKS 914
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  982 KMEEEILLLEDQNSKFIKEKKLMEDRIAECSS--QLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTRQELEKAKRK 1059
Cdd:COG5022    915 LSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTILVREGNKANSE 993
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1060 LDGettdLQDQIAELQAQIDELKLQLAKKEEElqgalargDDETLHKNNALKVVRELQAQIAELQEdfesEKASRNKAEK 1139
Cdd:COG5022    994 LKN----FKKELAELSKQYGALQESTKQLKEL--------PVEVAELQSASKIISSESTELSILKP----LQKLKGLLLL 1057
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1140 QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEA-----QIQDMRQRHATALEELSEQLEQ 1214
Cdd:COG5022   1058 ENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKpanvlQFIVAQMIKLNLLQEISKFLSQ 1137
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1215 AkrfKANLEKNKQGLETDNKELACevkVLQQVKAESEHKRKKLDAQVQEL-----------HAKVSEGDRLRVELAEKAS 1283
Cdd:COG5022   1138 L---VNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEKRlyqsalydeksKLSSSEVNDLKNELIALFS 1211
                         1290      1300      1310      1320      1330      1340      1350
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034599859 1284 KlQNELDNVSTLLEEAEKKGI------KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1348
Cdd:COG5022   1212 K-IFSGWPRGDKLKKLISEGWvpteysTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEV 1281
PTZ00014 PTZ00014
myosin-A; Provisional
97-824 1.11e-132

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 436.77  E-value: 1.11e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014   108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:PTZ00014   188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:PTZ00014   261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  336 MGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:PTZ00014   341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014   421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  491 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 570
Cdd:PTZ00014   500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDS 576
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  571 DKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgsayKTKKGMF 650
Cdd:PTZ00014   577 NK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL 639
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  651 rtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  731 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFA 807
Cdd:PTZ00014   718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
                          730
                   ....*....|....*..
gi 1034599859  808 KKqqqlsaLKVLQRNCA 824
Cdd:PTZ00014   798 KN------IKSLVRIQA 808
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
851-1684 1.83e-39

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 161.04  E-value: 1.83e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  851 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFA----EAEEMRARLAAKKQELEEILHD 926
Cdd:COG1196    178 ERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLaklkELRKELEELEEELSRLEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  927 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMED 1006
Cdd:COG1196    258 LQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1007 RIAECSSQLAEEEEKAKNLAKIRNKQEvmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLA 1086
Cdd:COG1196    338 ELEERETLLEELEQLLAELEEAKEELE---EKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLE 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1087 KKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDTTA 1163
Cdd:COG1196    415 RLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSleaRLDRLE 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1164 AQQElRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEE---------LSEQLEQAKRFKANLEKNKQGLETdnk 1234
Cdd:COG1196    495 AEQR-ASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALEAalgnrlqavVVENEEVAKKAIEFLKENKAGRAT--- 570
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1235 elaceVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVelaekasKLQNELDN--VSTLLEEAEK--KGIKFAKDA 1310
Cdd:COG1196    571 -----FLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEP-------AVRFVLGDtlVVDDLEQARRlaRKLRIKYRI 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1311 ASLESQLQDTQELLQEETRQK---LNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKkvdddlgTI 1387
Cdd:COG1196    639 VTLDGDLVEPSGSITGGSRNKrssLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRR-------QL 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1388 ESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARY 1467
Cdd:COG1196    712 EELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQAL 791
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1468 AEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQ 1547
Cdd:COG1196    792 QEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAE 871
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1548 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVR-ELEAELEDERKQRALAVASKKKMEIDL 1626
Cdd:COG1196    872 KEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERlEVELPELEEELEEEYEDTLETELEREI 951
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034599859 1627 KDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1684
Cdd:COG1196    952 ERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRE 1009
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1005-1861 1.55e-35

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: 148.28  E-value: 1.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1005 EDRIAECSSQL------AEEEEKAKNL-AKIRNKQ-EVMISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQA 1076
Cdd:TIGR02168  192 EDILNELERQLkslerqAEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEE 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1077 QIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1156
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1157 DTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATaLEELSEQLEQAKRFKANLEKNKQGLETDNkel 1236
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI--- 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1237 acevkvlqqvkaeSEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQ 1316
Cdd:TIGR02168  424 -------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1317 LQDTQELLQEetrqKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVdddlgTIESLEEAKKk 1396
Cdd:TIGR02168  491 LDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-----VVENLNAAKK- 560
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1397 llkDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAeekSISARYAEERDRAEA 1476
Cdd:TIGR02168  561 ---AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNA 634
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1477 EAREKETKAL---------------SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1541
Cdd:TIGR02168  635 LELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1542 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLiKQVRELEAELEDERKQRALAVASKKK 1621
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE-ERLEEAEEELAEAEAEIEELEAQIEQ 793
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1622 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1701
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1702 ARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSA-- 1779
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtl 953
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1780 ------AQKSDNARQQLERQNKELKAKLQELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEK 1849
Cdd:TIGR02168  954 eeaealENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARE 1032
                          890
                   ....*....|..
gi 1034599859 1850 KLKEIFMQVEDE 1861
Cdd:TIGR02168 1033 RFKDTFDQVNEN 1044
PTZ00121 PTZ00121
MAEBL; Provisional
850-1720 1.03e-22

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 106.76  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrARLAAKKQELEEILHDLES 929
Cdd:PTZ00121  1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED--ARKAEEARKAEDARKAEEA 1145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  930 RVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDRIA 1009
Cdd:PTZ00121  1146 RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKK 1225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1010 ECSSQLAEE----EEKAKNLAKIRNKQEvmISDLEERLKKEEKTRQELEKAKRKLDGEttdlqdqiaELQAQIDELKLQL 1085
Cdd:PTZ00121  1226 AEAVKKAEEakkdAEEAKKAEEERNNEE--IRKFEEARMAHFARRQAAIKAEEARKAD---------ELKKAEEKKKADE 1294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1086 AKKEEELQGAlargdDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1165
Cdd:PTZ00121  1295 AKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1166 QELRTKREQEVAELKKALEEETKNHEAQIQ-DMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelACEVKVLQ 1244
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKAD 1447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1245 QVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNEldnvstlLEEAEKKgikfAKDAASLESQLQDTQELL 1324
Cdd:PTZ00121  1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK-------AEEAKKK----ADEAKKAAEAKKKADEAK 1516
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1325 QEETRQKlnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLADTKKKVDDDlgtiESLEEAKKKLLKDAEAL 1404
Cdd:PTZ00121  1517 KAEEAKK---ADEAKKAEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEA----KKAEEDKNMALRKAEEA 1586
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1405 SQ----RLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQR----------QVASNLEKKQKKFDQLLAEEKSISARYAEE 1470
Cdd:PTZ00121  1587 KKaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkveQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1471 RDRAEAEAREKETkalslARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTqlEE 1550
Cdd:PTZ00121  1667 AKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EA 1739
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1551 LEDELQATEdakLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQvreleaELEDERKQRALAVASKKKmeiDLKDLE 1630
Cdd:PTZ00121  1740 EEDKKKAEE---AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE------ELDEEDEKRRMEVDKKIK---DIFDNF 1807
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1631 AQIEAANKARDEVIKQLRKLQ-AQMKDY----QRELEEARASRDEIFAQSKESEK---KLKSLEAEILQLQEELASSERA 1702
Cdd:PTZ00121  1808 ANIIEGGKEGNLVINDSKEMEdSAIKEVadskNMQLEEADAFEKHKFNKNNENGEdgnKEADFNKEKDLKEDDEEEIEEA 1887
                          890
                   ....*....|....*...
gi 1034599859 1703 RRHAEQERDELADEITNS 1720
Cdd:PTZ00121  1888 DEIEKIDKDDIEREIPNN 1905
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1108-1437 1.32e-12

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 73.02  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1108 NALKVVRELQAQIAELQEDF-ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEE 1186
Cdd:NF033930    55 AAKKAYEEAKKKAEDAQKKYdEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKYRKAQRRKKSDYKKKLAEADKKIDEA 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1187 TKNHE------AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNkqgletdnkelacevkvLQQVKAESEHKRKKLDAQ 1260
Cdd:NF033930   135 KKKQKeakaefNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKK-----------------VDEAKKKVEEAKKKVEAE 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1261 VQELHAKVSEGDRLRVELAEkaskLQNELDNVSTLLEEAEKK-GIKFAKD--AASLESQLQDTQELLQEETRQKLNLSSR 1337
Cdd:NF033930   198 EAEIEKLQNEEVALEAKIAE----LENQVDNLEKELAEIDESdSEDYIKEglRAPLESELDAKQAKLAKKQTELEKLLDS 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1338 IRQLEEEKNSLqeqqeEEEEARKNLEKQVLALQSQLADTKKKVDDdlgtiesleeaKKKLLKDAEALSQRLEEKALAYDK 1417
Cdd:NF033930   274 LDPEGKTQDEL-----DKEAAEEELSKKIDELDNEVAKLEKEVSD-----------LENSDNNVADYYKEALEKDLATKK 337
                          330       340
                   ....*....|....*....|..
gi 1034599859 1418 --LEKTKNRLQQELDDLTVDLD 1437
Cdd:NF033930   338 aeLEKTQKDLDKALNELGPDGD 359
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
945-1264 3.16e-09

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 61.85  E-value: 3.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  945 KKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSK----FIKEKKLMEDRIAECSSQLAE--- 1017
Cdd:NF033930    50 VKKSEAAKKAYEEAKKKAEDAQKKYDEDQKKTEEKAKKEKKASEEEQKANLAvqkaYVKYRKAQRRKKSDYKKKLAEadk 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1018 --------EEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTdlqdQIAELQAQIDELKLQLAKKE 1089
Cdd:NF033930   130 kideakkkQKEAKAEFNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKKVDEAKK----KVEEAKKKVEAEEAEIEKLQ 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1090 EElqgalargddetlhknnalkvVRELQAQIAELQEdfESEKASRNKAEKQKRDLSEELEA-LKTELEDTLDttAAQQEL 1168
Cdd:NF033930   206 NE---------------------EVALEAKIAELEN--QVDNLEKELAEIDESDSEDYIKEgLRAPLESELD--AKQAKL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1169 rTKREQEVAELKKALEEETKNHEAQIQDmrqrhaTALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKV-----L 1243
Cdd:NF033930   261 -AKKQTELEKLLDSLDPEGKTQDELDKE------AAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVADYYKEalekdL 333
                          330       340
                   ....*....|....*....|.
gi 1034599859 1244 QQVKAESEHKRKKLDAQVQEL 1264
Cdd:NF033930   334 ATKKAELEKTQKDLDKALNEL 354
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
33-72 1.12e-08

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: 397036  Cd Length: 39  Bit Score: 52.38  E-value: 1.12e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034599859   33 KKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVN 72
Cdd:pfam02736    1 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVK 39
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1520-1867 1.71e-08

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 59.95  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1520 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATED------------------AKLRLEVNMQAMKAQFERDLQ 1581
Cdd:NF033804   133 KSDYAKQAEEIKKTTEAYKKEVAAHQAETDKINAENKAAKDkyqkdlkahqaevekintANATAKAEYEAKLAQYQKDLA 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1582 TRDEQNEEKKRLLIKQVRELEAELEdeRKQRALAVAsKKKMEIDLKDLEAQiEAANKARDEVIKQLRK-----LQAQMKD 1656
Cdd:NF033804   213 AVQKANEDSQADYQNKLSAYQTELA--RVQKANAEA-KEAYDKAVKENTAK-NAALQAENEAIKQRNEtakanYEAAMKQ 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1657 YQRELEEARASRDEIFAqskESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASG-KSALLDEKRRLE 1735
Cdd:NF033804   289 YEADLAAIKKAKEDNDA---DYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAiKQRNAAAKATYE 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1736 ARIAQLEEELEEEQSNMELlNDRFRKTTLQvdTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKAT 1815
Cdd:NF033804   366 AALKQYEADLAAVKKANAA-NEADYQAKLA--AYQTELARVQKANADAKAAYEKAVEDNKAKNAALQAENEAIKQRNAAA 442
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034599859 1816 ISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQ 1867
Cdd:NF033804   443 KADYEAKLAKYQADLAKYKKDLAEYPAKLKAYEDEQAKIKAALAELEKKKNE 494
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1531-1843 5.30e-08

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 58.00  E-value: 5.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1531 EKSKRALEQQVEEMRTQLEELEDELQATEDaklrlevnmqamKAQFERDL-QTRDEQNEEKKRLLIKQVRELEAELEDER 1609
Cdd:NF033930    54 EAAKKAYEEAKKKAEDAQKKYDEDQKKTEE------------KAKKEKKAsEEEQKANLAVQKAYVKYRKAQRRKKSDYK 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1610 KQRALAvasKKKMEIDLKDLEAQIEAANKARDEVI---KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLE 1686
Cdd:NF033930   122 KKLAEA---DKKIDEAKKKQKEAKAEFNKVRAKVVpeaEELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAEE 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1687 AEILQLQEELASSERARRHAEQERDELADE---ITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1763
Cdd:NF033930   199 AEIEKLQNEEVALEAKIAELENQVDNLEKElaeIDESDSEDYIKEGLRAPLESELDAKQAKLAKKQTELEKLLDSLDPEG 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1764 LQVDTLNAElAAERSAAQKSDNARQQLERQNKELKaKLQELEGAVKSKFKAtisALEAKIGQLEEQLEQEAKE-RAAANK 1842
Cdd:NF033930   279 KTQDELDKE-AAEEELSKKIDELDNEVAKLEKEVS-DLENSDNNVADYYKE---ALEKDLATKKAELEKTQKDlDKALNE 353

                   .
gi 1034599859 1843 L 1843
Cdd:NF033930   354 L 354
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
852-1131 1.34e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 56.84  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  852 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQ-----------LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL 920
Cdd:NF033930   108 KYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKEakaefnkvrakVVPEAEELAETKKKAEEAKAEEPVAKKKVDEAKKKV 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  921 EEIlhdlESRVEEEEERNQILQNEKKKMQAHIQdleeqldeeegarqklqlekvTAEAKIKKMEEEILLLEDQNSKFIKE 1000
Cdd:NF033930   188 EEA----KKKVEAEEAEIEKLQNEEVALEAKIA---------------------ELENQVDNLEKELAEIDESDSEDYIK 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1001 KKLMEDRIAECSSQLAEEEEKAKNLAKirnkqevmisdLEERLKKEEKTRQELEK--AKRKLDGETTDLQDQIAELQAQI 1078
Cdd:NF033930   243 EGLRAPLESELDAKQAKLAKKQTELEK-----------LLDSLDPEGKTQDELDKeaAEEELSKKIDELDNEVAKLEKEV 311
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034599859 1079 DELKLQLAKKEEELQGALARgdDETLHKNNALKVVRELQAQIAELQEDFESEK 1131
Cdd:NF033930   312 SDLENSDNNVADYYKEALEK--DLATKKAELEKTQKDLDKALNELGPDGDEEE 362
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1358-1696 1.40e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 56.46  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1358 ARKNLEKQvlalQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQEldDLTVDLD 1437
Cdd:NF033930    56 AKKAYEEA----KKKAEDAQKKYDEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKYRKAQRRKKSDYKK--KLAEADK 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1438 HQRQVASNLEKKQKKFDQLLA------EEKSISARYAEERDRAEAEAREKETKAlslaraleealeAKEEFERQNKQLRA 1511
Cdd:NF033930   130 KIDEAKKKQKEAKAEFNKVRAkvvpeaEELAETKKKAEEAKAEEPVAKKKVDEA------------KKKVEEAKKKVEAE 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1512 DMEdlmsskddvgknVHELEKSKRALEQQVEEMRTQLEELEDELqatedAKLRLEVNMQAMKAQFERDLQtrdeqneekK 1591
Cdd:NF033930   198 EAE------------IEKLQNEEVALEAKIAELENQVDNLEKEL-----AEIDESDSEDYIKEGLRAPLE---------S 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1592 RLLIKQVRELEAELEDERKQRALAVASKKKMEIdlkDLEAQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEI 1671
Cdd:NF033930   252 ELDAKQAKLAKKQTELEKLLDSLDPEGKTQDEL---DKEAAEEELSKKIDE-------LDNEVAKLEKEVSDLENSDNNV 321
                          330       340
                   ....*....|....*....|....*.
gi 1034599859 1672 FAQSKES-EKKLKSLEAEILQLQEEL 1696
Cdd:NF033930   322 ADYYKEAlEKDLATKKAELEKTQKDL 347
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1616-1928 2.74e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 55.69  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1616 VASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaQSKESEKKLKSLEAEILQLQEE 1695
Cdd:NF033930    36 VASQSKAEKDYDAAVKKSEAAKKAYEEAKKKAEDAQKKYDEDQKKTEE----------KAKKEKKASEEEQKANLAVQKA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1696 LASSERARRHAEQERDELADEItnsasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttlqvdtlnAELAA 1775
Cdd:NF033930   106 YVKYRKAQRRKKSDYKKKLAEA------DKKIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKK---------AEEAK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1776 --ERSAAQKSDNARQQLERQNKELKAKLQELEgavksKFKATISALEAKIGQLEEQleqeakeraaanklVRRTEKKLKE 1853
Cdd:NF033930   171 aeEPVAKKKVDEAKKKVEEAKKKVEAEEAEIE-----KLQNEEVALEAKIAELENQ--------------VDNLEKELAE 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034599859 1854 IfmqveDERRHADQYKEQMEK-ANARMKQLKRQLEEAEEEATRANAS---RRKLQRELDDATEANEgLSREVSTLKNRL 1928
Cdd:NF033930   232 I-----DESDSEDYIKEGLRApLESELDAKQAKLAKKQTELEKLLDSldpEGKTQDELDKEAAEEE-LSKKIDELDNEV 304
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1275-1608 1.05e-06

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 53.76  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1275 RVELAEKASKLQNELD---------NVSTLLEEAEKKGI----KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1341
Cdd:NF033930    30 RAEEAPVASQSKAEKDydaavkkseAAKKAYEEAKKKAEdaqkKYDEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKY 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1342 EEEKNSLQEQQEEEeeaRKNLEKQ---------------------VLALQSQLADTKKKVDDdlgTIESLEEAKKKL--- 1397
Cdd:NF033930   110 RKAQRRKKSDYKKK---LAEADKKideakkkqkeakaefnkvrakVVPEAEELAETKKKAEE---AKAEEPVAKKKVdea 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1398 LKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLtvdldhQRQVAsNLEKKQKKFDqllaeeKSISARYAEERDRAEAE 1477
Cdd:NF033930   184 KKKVEEAKKKVEAEEAEIEKLQNEEVALEAKIAEL------ENQVD-NLEKELAEID------ESDSEDYIKEGLRAPLE 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1478 ArEKETKALSLARAleealeakeeferqnkqlRADMEDLMSSKDDVGKNVHELEK--SKRALEQQVEEMRTQLEELEDEL 1555
Cdd:NF033930   251 S-ELDAKQAKLAKK------------------QTELEKLLDSLDPEGKTQDELDKeaAEEELSKKIDELDNEVAKLEKEV 311
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034599859 1556 qatEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDE 1608
Cdd:NF033930   312 ---SDLENSDNNVADYYKEALEKDLATKKAELEKTQKDLDKALNELGPDGDEE 361
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1604-1880 2.11e-06

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 52.61  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1604 ELEDERKQralAVASKKKMEIDLKDLEAQIEAANKARDEV-----------IKQLRKLQAQMKDYQRELEEARASRDEIF 1672
Cdd:NF033930    59 AYEEAKKK---AEDAQKKYDEDQKKTEEKAKKEKKASEEEqkanlavqkayVKYRKAQRRKKSDYKKKLAEADKKIDEAK 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1673 AQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEitnSASGKSALLDEKRRLEARIAQLEEELEEEQSnm 1752
Cdd:NF033930   136 KKQKEAKAEFNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKK---VDEAKKKVEEAKKKVEAEEAEIEKLQNEEVA-- 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1753 elLNDRFRKTTLQVDTLNAELaAERSAAQKSDNARQQLERQ-NKELKAKLQELegAVKSKFKATISALEAKIGQLEEQLE 1831
Cdd:NF033930   211 --LEAKIAELENQVDNLEKEL-AEIDESDSEDYIKEGLRAPlESELDAKQAKL--AKKQTELEKLLDSLDPEGKTQDELD 285
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034599859 1832 QEAKErAAANKLVRRTEKKLKEIFMQVED----ERRHADQYKEQMEKANARMK 1880
Cdd:NF033930   286 KEAAE-EELSKKIDELDNEVAKLEKEVSDlensDNNVADYYKEALEKDLATKK 337
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
1071-1327 8.17e-06

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: 380155 [Multi-domain]  Cd Length: 1848  Bit Score: 51.37  E-value: 8.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1071 IAELQAQIDELKLQlAKKEEELQGALArgdDETLHKNNALKVVRELQAQIAEL---QEDFES--EKASRNKAEKQKRDLS 1145
Cdd:NF012221  1537 TSESSQQADAVSKH-AKQDDAAQNALA---DKERAEADRQRLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1146 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKALEEE---TKNH-EAQIQDMRQRHATALEELSEQLE 1213
Cdd:NF012221  1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1214 QAKRFKANLEKNKQGLETDNKelacevkvlqqvKAESEHKRKKLDAQVQELHAKVSEGDrlrvelaekasklqneldnVS 1293
Cdd:NF012221  1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAESD-------------------AN 1741
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034599859 1294 TLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1327
Cdd:NF012221  1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1361-1718 2.25e-05

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 49.55  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1361 NLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEkalaydkLEKTKNrlqqelddltvdlDHQR 1440
Cdd:NF033804    93 DLDKAVKDAKSAGVNVVQDETVDKGTATTATENAQKQTEIKSDYAKQAEE-------IKKTTE-------------AYKK 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1441 QVASNlekkQKKFDQLLAEEKSISARYAEERDRAEAEArEKETKALSLARALEEALEAKEEF-----ERQNKQLRADMED 1515
Cdd:NF033804   153 EVAAH----QAETDKINAENKAAKDKYQKDLKAHQAEV-EKINTANATAKAEYEAKLAQYQKdlaavQKANEDSQADYQN 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1516 LMSSKDDVGKNVHELE-KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLL 1594
Cdd:NF033804   228 KLSAYQTELARVQKANaEAKEAYDKAVKENTAKNAALQAENEAIKQRNETAKANYEAAMKQYEADLAAIKKAKEDNDADY 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1595 IKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKA---RDEVIKQlrKLQAQMKDYQRELEEARASRDei 1671
Cdd:NF033804   308 QAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAikqRNAAAKA--TYEAALKQYEADLAAVKKANA-- 383
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1034599859 1672 fAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIT 1718
Cdd:NF033804   384 -ANEADYQAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQ 429
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1019-1163 1.88e-04

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 46.16  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1019 EEKAKNLAKIRNKQEVMISDLEERlkKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQ----- 1093
Cdd:NF038025    46 AEKDDLLDELENEQEEEPETFTEQ--KEEEDKEDLEAILDELATEANKASAELDEVNAEIQGVKEEIKEKQEQLMvldtk 123
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034599859 1094 ---GALargDDETLHKNNALKV-VRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTA 1163
Cdd:NF038025   124 eelDEL---SEEELAERQELEAeIKQLEAQLDELEEEKEELEEELKTIRKDQWSQTKEKISEKFDIPDDWKEQA 194
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1040-1447 2.15e-04

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 46.47  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1040 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVR-ELQA 1118
Cdd:NF033804   123 TENAQKQTEIKSDYAKQAEEIKKTTEAYKKEVAAHQAETDKINAENKAAKDKYQKDLKAHQAEVEKINTANATAKaEYEA 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1119 QIAELQEDFESEKASRNKAEKqkrDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMR 1198
Cdd:NF033804   203 KLAQYQKDLAAVQKANEDSQA---DYQNKLSAYQTELARVQKANAEAKEAYDKAVKENTAKNAALQAENEAIKQRNETAK 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1199 QRHATALEELSEQLEQAKRFKANLEKNKQG-LETDNKELACEVKVLQQVKA-------ESEHKRKKLDAQVQ-------- 1262
Cdd:NF033804   280 ANYEAAMKQYEADLAAIKKAKEDNDADYQAkLAAYQTELARVQKANADAKAayekaveENTAKNTAIQAENEaikqrnaa 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1263 -----ELHAKVSEGDRLRVELA---------EKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1327
Cdd:NF033804   360 akatyEAALKQYEADLAAVKKAnaaneadyqAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQaENEAIKQRN 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1328 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIE---------SLEEAKKKLL 1398
Cdd:NF033804   440 AAAKADYEAKLAKYQADLAKYKKDLAEYPAKLKAYEDEQAKIKAALAELEKKKNEDGYLSEpsaqslvydSEPNAQLSLT 519
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1399 KDAEALSQRLEEKALAYDKLEKTKNRLQqeLDDLTV-DLDHQRQVASNLE 1447
Cdd:NF033804   520 TDGKLLKASAVDEAFKKDTAQYGKKNLQ--LDNLNVtNLEQADATTSSVE 567
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1558-1724 2.21e-04

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 46.16  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1558 TEDAKLRLEvNMqAMKAQFERDLQTRDEQNEEKKRLLikQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAAN 1637
Cdd:NF038025    18 TEEALDLLE-NM-AKEKDEKQIKKAADEVTAEKDDLL--DELENEQEEEPETFTEQKEEEDKEDLEAILDELATEANKAS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1638 KARDEVIKQLRKLQAQMKDYQREL-------------EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1704
Cdd:NF038025    94 AELDEVNAEIQGVKEEIKEKQEQLmvldtkeeldelsEEELAERQELEAEIKQLEAQLDELEEEKEELEEELKTIRKDQW 173
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034599859 1705 HAEQER-----------DELADEITNSASGK 1724
Cdd:NF038025   174 SQTKEKisekfdipddwKEQATETLNQVGEK 204
BREX_BrxC NF033441
BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, ...
1005-1244 2.35e-04

BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, from BREX (bacteriophage exclusion) systems of type 1.


Pssm-ID: 380283  Cd Length: 1173  Bit Score: 46.42  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1005 EDRIAECSSQLAEEE-EKAKNLAKIRNK--------QEVMISDLEE--RLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1073
Cdd:NF033441   892 EDALAKEIREKFPELlEELKALAGRYQAggypgpdpLEPALALLEEilSIKDNEEFLKALNKKEDDLLDLIEDWEDVKSF 971
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1074 LQ-AQIDELKlQLAKKEEELQGALARGDDETLhkNNALKVVRELQA------QIAELQEDFES-EKASRNKAEKQKRDLS 1145
Cdd:NF033441   972 FEgDQLPIWD-RALRLLKEYEDNLDYELDEEA--EEAIEELRSILAdpdpysRIPDLPPLLEAlREALREALEELREAAL 1048
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1146 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKnhEAQIQDMRQRHATA-LEELSEQLEQAKRFKANLEK 1224
Cdd:NF033441  1049 EAIEEAKAELEADLEWQELSDEQQNRLLAPFDELKERIEPEVS--IASLRALLDQLADAlLDRLLDRIEALIQRFQEEKA 1126
                          250       260
                   ....*....|....*....|
gi 1034599859 1225 NKQGLETDNKELACEVKVLQ 1244
Cdd:NF033441  1127 EPEVKEAAAEPPEPKVKTVS 1146
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1532-1877 2.36e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 411407 [Multi-domain]  Cd Length: 684  Bit Score: 46.16  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1532 KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnMQAMKAQFERDLQTRDEQNEEKkrLLIKQVRELEAELEDERKQ 1611
Cdd:NF033838    58 EHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKK--LSDIKTEYLYELNVLKEKSEAE--LTSKTKKELDAAFEQFKKD 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1612 -----RALAVASKKKMEIDlKDLEAQIEAANKARDEVIKQLRKLQ-----AQMKDYQREL--EEARASRDEifAQSKESE 1679
Cdd:NF033838   134 tlepgKKVAEATKKVEEAE-KKAKDQKEEDRRNYPTNTYKTLELEiaesdVEVKKAELELvkEEAKEPRDE--EKIKQAK 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1680 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1759
Cdd:NF033838   211 AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSV 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1760 RKTTLQVDTLN-----AELAAERSAAQKSDNARQQLERQN------KELKAKLQELEGAVKS------KFKATISALEAK 1822
Cdd:NF033838   291 GEETLPSPSLKpekkvAEAEKKVEEAKKKAKDQKEEDRRNyptntyKTLELEIAESDVKVKEaelelvKEEAKEPRNEEK 370
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034599859 1823 IGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1877
Cdd:NF033838   371 IKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPA 425
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
1077-1488 3.57e-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: 380155 [Multi-domain]  Cd Length: 1848  Bit Score: 45.98  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1077 QIDELKLQLAKKeeeLQGALARGDDETLHK-NNALKVVRELQAQIAE---LQEDFESEKASRNKAEKQKRDLS------- 1145
Cdd:NF012221  1355 EIDEVGSDLGDS---LTGSVTQVETPDLNAmQNALNIDESVLSTQAPnliVNGDFEQGAEGWNSTYGVEASHSasvyglr 1431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1146 -EELEALKTELeDTLDTTAAQQELRTKREQEVAELKKALEEE---TKNHEAQIQDMRQRHATALEELSEQLEQAKRFKAN 1221
Cdd:NF012221  1432 aEGHGARVSEL-DTYTNTSLYQDLSNLTAGEVIALSFDFARRaglSTNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAK 1510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1222 LEKNK---------QGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVElAEKasklQNELDNV 1292
Cdd:NF012221  1511 AGSNRlefkgtghnDGLGYILDNVVATSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLE-QEK----QQQLAAI 1585
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1293 STLLEEAEkkgikfAKDAASLESQLQDTQELLQEE----TRQKLNLSSRIRQLEEEKNS----------------LQEQQ 1352
Cdd:NF012221  1586 SGSQSQLE------STDQNALETNGQAQRDAILEEsravTKELTTLAQGLDALDSQATYagesgdqwrnpfagglLDRVQ 1659
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1353 EEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKA-LAYDKLEKTKNRLQQELDD 1431
Cdd:NF012221  1660 EQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAeKRKDDALAKQNEAQQAESD 1739
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034599859 1432 LTVDL-------DHQRQVASNlekkqkKFDQLLAEEKSISARYAEERDRAEAEAREKETKALSL 1488
Cdd:NF012221  1740 ANAAAndaqsrgEQDASAAEN------KANQAQADAKGAKQDESDKPNRQGAAGSGLSGKAYSV 1797
BREX_BrxC NF033441
BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, ...
1277-1490 1.08e-03

BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, from BREX (bacteriophage exclusion) systems of type 1.


Pssm-ID: 380283  Cd Length: 1173  Bit Score: 44.11  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1277 ELAEKASKLQ----NELDNVSTLLEE--AEKKGIKFAKDAASLESQLQDTQELLQEeTRQKLNlSSRIRQLEEEKNSLQE 1350
Cdd:NF033441   912 ALAGRYQAGGypgpDPLEPALALLEEilSIKDNEEFLKALNKKEDDLLDLIEDWED-VKSFFE-GDQLPIWDRALRLLKE 989
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1351 -QQEEEEEARKNLEKQVLALQSQLADTK-----KKVDDDLGTIES-----LEEAKKKLLKDAEALSQRLEEKALAYDKLE 1419
Cdd:NF033441   990 yEDNLDYELDEEAEEAIEELRSILADPDpysriPDLPPLLEALREalreaLEELREAALEAIEEAKAELEADLEWQELSD 1069
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1420 KTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDR---------AEAEAREKETKALSLAR 1490
Cdd:NF033441  1070 EQQNRLLAPFDELKERIEPEVSIASLRALLDQLADALLDRLLDRIEALIQRFQEekaepevkeAAAEPPEPKVKTVSLPR 1149
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1661-1837 1.38e-03

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 43.46  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1661 LEEARASRDEifAQSKESEKKLKSLEAEILQLQE---ELASSERARRHAEQERDELA---DEITNSASGKSALLDEkrrL 1734
Cdd:NF038025    25 LENMAKEKDE--KQIKKAADEVTAEKDDLLDELEneqEEEPETFTEQKEEEDKEDLEailDELATEANKASAELDE---V 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1735 EARIAQLEEELEEEQSNMELLNdrfrkTTLQVDTLNAELAAERsaaqksdnarQQLERQNKELKAKLQELEGAVkskfka 1814
Cdd:NF038025   100 NAEIQGVKEEIKEKQEQLMVLD-----TKEELDELSEEELAER----------QELEAEIKQLEAQLDELEEEK------ 158
                          170       180
                   ....*....|....*....|...
gi 1034599859 1815 tiSALEAKIGQLEEQLEQEAKER 1837
Cdd:NF038025   159 --EELEEELKTIRKDQWSQTKEK 179
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
851-1191 2.38e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 411407 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  851 EEELQAKDEELLKV--KEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETelfaeAEEMRARLAAKKQELEEILHDLE 928
Cdd:NF033838    64 ESHLEKILSEIQKSldKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAEL-----TSKTKKELDAAFEQFKKDTLEPG 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  929 SRVEEEEERnqiLQNEKKKMQAHiqDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIL---LLEDQNSKFIKEKKL-M 1004
Cdd:NF033838   139 KKVAEATKK---VEEAEKKAKDQ--KEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVkeeAKEPRDEEKIKQAKAkV 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1005 EDRIAECSS--------QLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQEL-EKA---KRKLDGETTDLQ--DQ 1070
Cdd:NF033838   214 ESKKAEATRlekiktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLgEPAtpdKKENDAKSSDSSvgEE 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1071 IAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEA 1150
Cdd:NF033838   294 TLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQ 373
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1034599859 1151 LKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHE 1191
Cdd:NF033838   374 AKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKE 414
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1023-1378 7.53e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 411407 [Multi-domain]  Cd Length: 684  Bit Score: 41.15  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1023 KNLAKIRNKQEVMISDLEERLKKE--EKTRQELEKAKRKLDGETTDLQDQIAELQAQIDElklqlAKKEEELQgalargd 1100
Cdd:NF033838    91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEE-----AEKKAKDQ------- 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1101 DETLHKNNALKVVRELQAQIAElqEDFESEKASRN--KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1178
Cdd:NF033838   159 KEEDRRNYPTNTYKTLELEIAE--SDVEVKKAELElvKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEE 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1179 LK-----KALEEETKNHEAQIQDMRQRHAT--ALEELSEqlEQAKRFKANLEKNKQGLET--------DNKELACEVKVL 1243
Cdd:NF033838   237 AKrradaKLKEAVEKNVATSEQDKPKRRAKrgVLGEPAT--PDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVE 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1244 QQVKA----ESEHKR-------KKLDAQVQELHAKVSEGDrlrVELA-EKASKLQNElDNVSTLLEEAEKKgikfaKDAA 1311
Cdd:NF033838   315 EAKKKakdqKEEDRRnyptntyKTLELEIAESDVKVKEAE---LELVkEEAKEPRNE-EKIKQAKAKVESK-----KAEA 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1312 SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK-------------------------NSLQEQQEEEEEARKNLEKQV 1366
Cdd:NF033838   386 TRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQpqpapapqpekpapkpekpaeqpkaEKPADQQAEEDYARRSEEEYN 465
                          410
                   ....*....|..
gi 1034599859 1367 LALQSQLADTKK 1378
Cdd:NF033838   466 RLTQQQPPKTEK 477
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1101-1470 7.58e-03

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 41.46  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1101 DETLHKNNALKVVRELQAQiAELQEDFEsekasrnkaeKQKRDLSEELEALKTELedtldttAAQQELRTKREQEVAELK 1180
Cdd:NF033804   111 DETVDKGTATTATENAQKQ-TEIKSDYA----------KQAEEIKKTTEAYKKEV-------AAHQAETDKINAENKAAK 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1181 KALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEK--------------------------NKQGLETDNK 1234
Cdd:NF033804   173 DKYQKDLKAHQAEVEKINTANATAKAEYEAKLAQYQKDLAAVQKanedsqadyqnklsayqtelarvqkaNAEAKEAYDK 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1235 ELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVS--EGDRLRVELAE---------KASKLQNELDNVSTLLEEAEKKG 1303
Cdd:NF033804   253 AVKENTAKNAALQAENEAIKQRNETAKANYEAAMKqyEADLAAIKKAKedndadyqaKLAAYQTELARVQKANADAKAAY 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1304 IKFAKDAASLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEknsLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDD 1382
Cdd:NF033804   333 EKAVEENTAKNTAIQAENEAIKQRNAAaKATYEAALKQYEAD---LAAVKKANAANEADYQAKLAAYQTELARVQKANAD 409
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1383 DLGTIE-SLEEAKKK---LLKDAEALSQRLEEKALAYD-KLEKTKNRL---QQELDDLTVDL----DHQRQVASNLEK-- 1448
Cdd:NF033804   410 AKAAYEkAVEDNKAKnaaLQAENEAIKQRNAAAKADYEaKLAKYQADLakyKKDLAEYPAKLkayeDEQAKIKAALAEle 489
                          410       420
                   ....*....|....*....|..
gi 1034599859 1449 KQKKFDQLLAEEKSISARYAEE 1470
Cdd:NF033804   490 KKKNEDGYLSEPSAQSLVYDSE 511
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1096-1226 7.74e-03

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 41.15  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1096 LARGDDETLHKNNALKVVRELQAQIAELQEDFESEKAS--RNKAEKQKRDLSEELEALKTELEDT---LDTTAAQ----- 1165
Cdd:NF038025    28 MAKEKDEKQIKKAADEVTAEKDDLLDELENEQEEEPETftEQKEEEDKEDLEAILDELATEANKAsaeLDEVNAEiqgvk 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034599859 1166 QELRTKREQ---------------EVAELKKALEEETKNHEAQIQDMRQRHatalEELSEQLEQAKRFKANLEKNK 1226
Cdd:NF038025   108 EEIKEKQEQlmvldtkeeldelseEELAERQELEAEIKQLEAQLDELEEEK----EELEEELKTIRKDQWSQTKEK 179
 
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 ...
848-1928 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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 1487.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  848 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLIEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  928 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDR 1007
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1008 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAK 1087
Cdd:pfam01576  161 ISEFTSNLAEEEEKVKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1088 KEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1167
Cdd:pfam01576  241 KEEELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1168 LRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1247
Cdd:pfam01576  321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELSEQLEQAKRNKANLEKAKQALESENNELQAELKTLQQAK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1248 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1327
Cdd:pfam01576  401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLSEAEGKSIKLSKDVSSLESQLQDTQELLQEE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1328 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQR 1407
Cdd:pfam01576  481 TRQKLNLSSRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQR 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1408 LEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALS 1487
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1488 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576  641 LSRALEEALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1568 NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1647
Cdd:pfam01576  721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRDEAVKQL 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSAL 1727
Cdd:pfam01576  801 KKLQAQMKELQRELEETRASRDEILAQSKESEKKLKSLEAELLQLQEDLAASERAKRQAQQERDELADEIANGASGKSAL 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1728 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1807
Cdd:pfam01576  881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAERSFSQKSESARQQLERQNKELKAKLQEMEGT 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859 1808 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1887
Cdd:pfam01576  961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKANSRMKQLKRQLE 1040
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|.
gi 1034599859 1888 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAESMNREVSTLRSKL 1081
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-771 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  Cd Length: 673  Bit Score: 1451.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920    161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920    321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14920    401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14920    481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920    561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1034599859  739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920    641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
99-771 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  Cd Length: 662  Bit Score: 1332.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377     81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd01377    161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377    241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377    321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKPRQLKDKADF 575
Cdd:cd01377    400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtETAFGSAYKTKKGMFRTVGQ 655
Cdd:cd01377    478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  656 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd01377    547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1034599859  736 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01377    627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
99-771 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  Cd Length: 676  Bit Score: 1236.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932     81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14932    161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14932    241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932    321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14932    401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGsAYKTKKGMFRTVG 654
Cdd:cd14932    481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14932    560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1034599859  735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14932    640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-771 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  Cd Length: 670  Bit Score: 1209.54  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919     81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14919    158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919    238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919    318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14919    398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14919    478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14919    558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1034599859  739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14919    638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
99-771 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  Cd Length: 673  Bit Score: 1204.46  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921      1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921     81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14921    161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921    241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921    321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14921    401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14921    481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14921    561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1034599859  739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14921    641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
99-771 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  Cd Length: 675  Bit Score: 1187.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896     81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd15896    161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd15896    241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896    321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd15896    401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTEtaFGSAYKTKKGMFRTVG 654
Cdd:cd15896    481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd15896    559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1034599859  735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd15896    639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
99-771 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  Cd Length: 674  Bit Score: 1169.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911      1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASS---------HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911     81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  250 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 329
Cdd:cd14911    161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 409
Cdd:cd14911    241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911    321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQL 569
Cdd:cd14911    401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKTKKGM 649
Cdd:cd14911    477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGM 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911    553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599859  730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
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 ...
99-771 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  Cd Length: 670  Bit Score: 1151.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930      1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930     81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQETMEAMHIMGF 338
Cdd:cd14930    161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930    240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930    320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14930    400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayKTKKGMFRTVGQLYK 658
Cdd:cd14930    480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14930    558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1034599859  739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14930    638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
Myosin_head pfam00063
Myosin head (motor domain);
87-771 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 1115.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  247 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDN 325
Cdd:pfam00063  157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:pfam00063  237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  566 PRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETafgsAYKT 645
Cdd:pfam00063  474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859  646 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063  549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1034599859  726 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063  629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
80-783 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  Cd Length: 677  Bit Score: 1021.32  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859    80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 239
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599859   240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIP 318
Cdd:smart00242  155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL